Ex Parte Nash et al

Board of Patent Appeals and Interferences

Mar 28, 2007

10025567 (B.P.A.I. Mar. 28, 2007)

The opinion in support of the decision being entered today was not written
for publication and is not binding precedent of the Board.

UNITED STATES PATENT AND TRADEMARK OFFICE
__________

BEFORE THE BOARD OF PATENT APPEALS
AND INTERFERENCES
__________

Ex parte PETER NASH, JOHN W. ROSEVEAR (DECEASED),
D. L. ROBINSON (LEGAL REPRESENTATIVE),
and DONALD ROBINSON
__________

Appeal 2006-2575
Application 10/025,5671
Technology Center 1600
__________

ON BRIEF
__________

Before ADAMS, GRIMES, and LINCK, Administrative Patent Judges.

GRIMES, Administrative Patent Judge.

DECISION ON APPEAL
This appeal involves claims to compositions for inhibiting the
adherence of harmful microorganisms in the intestinal tracts of food animals.
The examiner has rejected the claims as being nonenabled, lacking written

1 This is a divisional application of Serial No. 09/616,843, which is pending
before us as Appeal No. 2006-3378.

Appeal No. 2006-2575
Application No. 10/025,567

description, having new matter, and being obvious. We have jurisdiction
under 35 U.S.C. § 134. We affirm-in-pa rt.
BACKGROUND
The bacteria Peptostreptococcus anaerobius, Clostridium
aminophilum, and Clostridium sticklandii, are among organisms
“responsible for wasting up to 25 percent of the protein in cattle diets. This
is a loss of as much as $25 billion annually to cattle producers . . . .”
(Specification 1.)
The Specification discloses that these organisms act by degrading
protein consumed by the host to ammonia. (Id.) The ammonia is then
“converted to urea by the liver and kidneys and thus lost to the host when
excreted as urine. These deleterious organisms also compete with beneficial
organisms which the host needs for the efficient utilization of ammonia.”
(Id. at 1-2.)
Antibodies to these bacteria can be produced by inoculating female
birds with a bacterial immunogen, and then harvesting the eggs from the
inoculated birds. (Id. at 5-6.) “The total antibody-containing contents of the
eggs are [then] separated from the shells and dried.” (Id. at 6.) The dried
antibody-containing egg material may be mixed with animal feed. (Id.)
The Specification discloses that orally administering the dried
antibody-containing egg preparations will inhibit the “ability of colony-
forming protein-wasting organisms, such as P. anaerobius, C. sticklandii
and C. aminophilum, and colony forming disease-causing organisms, such as
E. coli 0157:H7, Listeria, Salmonella and Campylobacter, to adhere in the
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rumen or intestinal tracts of food animals and thus reduce their ability to
multiply, grow and colonize.” (Id. at 7 (underlining omitted).)
DISCUSSION
1. CLAIM CONSTRUCTION
Claims 1, 3, 5-7, and 12-29 are pending and on appeal. Appellants
separate the claims into two groups for argument. (Br. 11.) Group I consists
of claims 1, 3, 5, 13, 16, and 19, and Group II consists of claims 6, 7, 12, 14,
15, 17, 18, and 20-29. (Id. at 11-12.)
Claims 1, 5, 6, and 13 are representative, and read as follows:
1. A microbial adherence inhibitor for administration to food
animals to inhibit the adherence of a targeted colony-forming immunogen in
the rumen or intestinal tracts of said food animals produced by the method
of:
A. Inoculating female chickens, in or about to reach their
egg laying age, with a particular target colony-forming immunogen;
B. Allowing a period of time sufficient to permit the
production in the chickens of antibody to the target colony-forming
immunogen, said antibody in the eggs including IgY immunoglobulins in
the yolks of the eggs and IgM and IgA immunoglobulins in the albumin of
the eggs;
C. Harvesting the eggs laid by the chickens;
D. Separating the entire contents of said harvested eggs
from the shells; and
E. Drying said separated entire contents of said eggs, said
dried entire contents of said eggs when administered to food animals with
animal feed promoting the growth of the food animals by decreasing the
waste of dietary protein caused by the presence of a colony-forming
immunogen in the rumen or intestinal tracts of the food animals by binding
the IgY immunoglobulins to the colony-forming immunogen, said binding
of the IgY immunoglobulins to the colony-forming immunogen being
assisted by the IgM and IgA immunoglobulins to inhibit the ability of the
protein-wasting immunogen to adhere to the rumen or intestinal tracts of the
animals.
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5. A microbial adherence inhibitor for administration to a living
being to inhibit the adherence of a colony-forming immunogen in the
digestive tract of the living being, said colony-forming immunogen is from
the class consisting of E. coli, Listeria, Salmonella and Campylobacter
produced by the method of:
A. Inoculating female birds in or about to reach their egg
laying age with the colony-forming immunogen;
B. Allowing a period of time sufficient to permit the
production in the birds of antibody to the colony-forming immunogen, said
antibody in the eggs including IgY immunoglobulins in the yolks of the eggs
and IgM and IgA immunoglobulins in the albumin of the eggs;
C. Harvesting the eggs laid by the birds;
D. Separating the entire contents of said harvested eggs
from the shells; and
E. Drying said separated entire contents of said eggs, said
dried entire contents of said eggs when administered to the living being
inhibiting the adherence of the colony-forming immunogen in the digestive
tract by binding the IgY immunoglobulins to the colony-forming
immunogen, said binding of the IgY immunoglobulins to the colony-
forming immunogen being assisted by the IgM and IgA immunoglobulins.

6. A microbial adherence inhibitor for administration to food
animals to inhibit the adherence of a targeted colony-forming immunogen in
the rumen or intestinal tracts of said food animals produced by the method
of:
A. Inoculating female chickens, in or about to reach their
egg laying age, with a particular target colony-forming immunogen;
B. Allowing a period of time sufficient to permit the
production in the chickens of antibody to the target colony-forming
immunogen, said antibody in the eggs including IgY immunoglobulins in
the yolks of the eggs and IgM and IgA immunoglobulins in the albumin of
the eggs;
C. Harvesting the eggs laid by the chickens;
D. Separating the entire contents of said harvested eggs
from the shells;
E. Providing a dry feed carrier material; and
F. Coating said dry feed carrier material with the separated
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entire contents of said harvested eggs, said dry food carrier material coated
with the entire contents of said eggs when administered to the food animals
inhibiting the adherence of colony-forming immunogen in the digestive tract
by binding the IgY immunoglobulins to the colony-forming immunogen,
said binding of the IgY immunoglobulins to the colony-forming immunogen
being assisted by the IgM and IgA immunoglobulins.

13. A microbial adherence inhibitor for promoting the growth of
food animals by decreasing the waste of dietary protein caused by the
presence of a protein-wasting immunogen in the rumen or intestinal tracts of
said food animals by inhibiting the ability of the immunogen to adhere to the
rumen or intestinal tracts of food animals to reduce the ability of the
immunogen to multiply, said protein-wasting immunogen is P antigen from
P. anaerobius produced by the method of:
A. Inoculating female birds, in or about to reach their egg
laying age, with P antigen from P. anaerobius;
B. Allowing a period of time sufficient to permit the
production in the bird and eggs laid by the birds of antibody to P antigen
from P. anaerobius, said antibody in the eggs including IgY
immunoglobulins in the yolks of the eggs and IgM and IgA
immunoglobulins in the albumin of the eggs;
C. Harvesting the eggs laid by the birds;
D. Separating the antibody-containing contents of said eggs
from the shells; and
E. Drying said entire contents of said eggs, said dried entire
contents of said eggs when administered to food animals with animal feed
promoting the growth of the food animals by decreasing the waste of dietary
protein caused by the presence of a protein-wasting immunogen in the
rumen or intestinal tracts of the food animals by binding the IgY
immunoglobulins to the protein-wasting immunogen, said binding of the
IgY immunoglobulins to the protein-wasting immunogen being assisted by
the IgM and IgA immunoglobulins to inhibit the ability of the protein-
wasting immunogen to adhere to the rumen or intestinal tracts of the
animals.

Claim 1 is a product-by-process claim directed to a composition
containing antibodies to a microorganism that forms colonies in the
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digestive tract of a food animal. The composition is made by inoculating
chickens with an immunogen from a microorganism that colonizes the
digestive tract of food animals, waiting for the chickens to produce
antibodies to the organism in their eggs, harvesting the eggs, separating the
entire contents of the eggs from the shells, and drying the contents of the
eggs.
Claim 1 also states that the antibody-containing dried egg
composition, “when administered to food animals,” promotes the growth of
the animals by decreasing the waste of protein; that the IgY in the
administered composition binds to the microorganism in the food animal’s
digestive tract; and that the IgM and IgA in the composition assists in the
binding of the IgY to the microorganism.
Claim 1 is directed to a product, not a process. As stated in Texas
Instruments Inc. v. U.S. Intern. Trade Com'n, 988 F.2d 1165, 1172,
26 USPQ2d 1018, 1023 (Fed. Cir. 1993), “[a] ‘whereby’ clause that merely
states the result of the limitations in the claim adds nothing to the
patentability or substance of the claim.” While the word “whereby” does not
appear in claim 1, the recitations regarding the effect of the composition
“when administered” do not affect the structure, form, or ingredients of the
composition. Therefore, other than confirming the presence of the IgY,
IgM, and IgA antibodies in the composition, we do not interpret claim 1’s
intended result recitations to place any positive limitations on the claim.
The preamble of claim 1 recites that the composition is “for
administration to food animals to inhibit the adherence of a targeted colony-
forming immunogen in the rumen or intestinal tracts of said food animals.”
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Because the body of claim 1 recites a structurally complete composition, we
do not interpret the preamble’s intended use recitation as placing any
limitations on the claimed composition. See Rowe v. Dror, 112 F.3d 473,
478, 42 USPQ2d 1550, 1553 (Fed. Cir. 1997) (“[w]here a patentee defines a
structurally complete invention in the claim body and uses the preamble only
to state a purpose or intended use for the invention, the preamble is not a
claim limitation.”).
Thus, overall, we interpret claim 1 as encompassing a composition
comprising the dried non-shell components of chicken eggs which contain
IgY, IgA, and IgM antibodies to microorganisms that cause the host to waste
dietary protein.
Claim 5 is similar to claim 1 but requires that the composition contain
antibodies to the bacterial species E. coli or a member of the bacterial genera
Listeria, Salmonella or Campylobacter. Therefore, overall, we interpret
claim 5 as encompassing a composition comprising the dried non-shell
components of bird eggs which contain IgY, IgA, and IgM antibodies to
E. coli, Listeria, Salmonella or Campylobacter.
Claim 6 is similar to claim 1 but contains the additional requirement
that the composition is prepared by coating the antibody-containing non-
shell portion of the eggs onto a dry feed carrier material. We therefore
interpret claim 6 as encompassing a composition comprising the dried non-
shell components of chicken eggs which contain IgY, IgA, and IgM
antibodies to microorganisms that adhere to the digestive tract of a host
animal, the antibody-containing egg composition having been coated on to a
dry feed carrier material.
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Claim 13 is similar to claim 1 but requires the antibodies in the
composition to be prepared by inoculating female birds with P antigen from
P. anaerobius. The Specification discloses that P antigen is prepared by
culturing P. anaerobius in broth, recovering the culture by low speed
centrifugation, removing whole cells by centrifugation, and recovering the P
antigen as the supernatant from the separated whole cells.
(Specification 16.)
Claims 16 and 19 recite essentially the same compositions as
claim 13. However, instead of antibodies to P antigen from P. anaerobius,
claims 16 and 19 require the compositions to contain antibodies to CS
antigen from Clostridium sticklandii and CA antigen from Clostridium
aminophilum, respectively. The Specification discloses that these antigens
can be prepared by culturing C. sticklandii or C. aminophilum in broth,
recovering the culture by low speed centrifugation, removing whole cells by
centrifugation, and recovering the CS or CA antigen as the supernatant from
the separated whole cells. (Specification 17-18.)
Thus, we interpret claims 13, 16, and 19 as encompassing
compositions comprising the dried non-shell components of bird eggs which
contain IgY, IgA, and IgM antibodies to antigens which can be separated
from whole cells in culture by centrifugation.
2. SCOPE OF ENABLEMENT
Claims 1, 3, 5-7, and 12-29 stand rejected under 35 U.S.C. § 112, first
paragraph, as enabling only “a microbial adherence inhibitor in the form of
IgY for administration to food animals to inhibit the adherence of targeted
colony-forming bacteria in the rumen or intestinal tracts of said food animal
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wherein the colony-forming bacteria are selected from the group consisting
of P. anaerobius, C. sticklandii, C. aminophilium[sic], E. Coli [sic], Listeria,
Salmonella and Campylobacter . . . .” (Answer 5.)
The Examiner notes that the Specification “discloses only five
microbial adherence inhibitors,” whereas the claim term “‘immunogen’
could be peptide, protein, bacteria, virus, or parasite.” (Id. at 5-6). The
Examiner argues that one cannot make egg antibody to a colony-forming
immunogen until one identifies the immunogen, and that “[g]iven the
indefinite number of colony-forming immunogen[s], there is insufficient
guidance as to the binding specificity of the microbial adherence inhibitor.”
(Id. at 6.)
The examiner summarizes the rationale for the enablement rejection
as follows:
Given the indefinite number of undisclosed colony-
forming immunogen[s], it is unpredictable which undisclosed
microbial inhibitor in the form of chicken antibody IgY
including IgA and IgM in the albumin would bind specifically
to said undisclosed colony-forming immunogen, in turn, would
be useful for inhibiting the adherence of any protein wasting
immunogen in the food animals or any living being. Given the
indefinite number of undisclosed microbial adherence
inhibitor[s], there is no in vivo working example demonstrating
that the claimed microbial adherence inhibitor is effective for
inhibiting the adherence of all colony-forming immunogen
(bacteria, parasites, virus, etc[.]) . . . in the rumen or intestinal
tracts of food animal.

(Id. at 7.)
Appellants argue that the Specification describes the steps required to
make and use the claimed compositions, including the preparation of
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immunogens, immunization of chickens, preparation of the dried antibody-
containing composition from the harvested eggs, and feeding the
composition to cattle. (Br. 15-16.) Appellants also point out that claims 3,
5, 12, and 24-29 are limited to compositions targeted to specific organisms,
and “do not include all targeted colony-forming immunogens.” (Id. at 16.)
Appellants argue that the specification provides “a representative
number of species of colony-forming protein-wasting immunogens to
describe the genus identified by the terms target colony-forming
immunogen,” and that “[t]hese immunogens are well known protein-wasting
immunogens.” (Id.) Appellants urge that the exemplified organisms are
“sufficient to identify a genus of like immunogens to a person skilled in the
art,” and that Stolle2 would have made the skilled artisan aware of
deleterious bacteria. (Id.)
The Examiner bears the burden of establishing that practicing the full
scope of the claimed subject matter would have required undue
experimentation. In re Wright, 999 F.2d 1557, 1561-62, 27 USPQ2d 1510,
1513 (Fed. Cir. 1993) (“[T]he PTO bears an initial burden of setting forth a
reasonable explanation as to why it believes that the scope of protection
provided by that claim is not adequately enabled by the description of the
invention provided in the specification of the application.”) .
While the specification must enable the skilled artisan to practice the
full scope of the claimed subject matter, the specification need not
“necessarily describe how to make and use every possible variant of the

2Stolle et al., U.S. Patent 4,748,018, issued May 31, 1988.
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claimed invention, for the artisan's knowledge of the prior art and routine
experimentation can often fill gaps, interpolate between embodiments, and
perhaps even extrapolate beyond the disclosed embodiments, depending
upon the predictability of the art.” AK Steel Corp. v. Sollac, 344 F.3d 1234,
1244, 68 USPQ2d 1280, 1287 (Fed. Cir. 2003) (citation omitted).
We agree with Appellants that the Examiner has not established that
practicing the full scope of the claims would have required undue
experimentation.
The Specification (page 1) discloses that protein-wasting
microorganisms were known in the art, and that degrading protein within the
digestive tract to ammonia is one mechanism by which the organisms waste
dietary protein. The Krause3 reference, cited by the Examiner in the
obviousness rejections, also discusses protein wasting in food animals by
ammonia production. (Krause 815, left col.) As argued by Appellants,
Stolle provides an extensive list of digestive tract pathogens to which
antibodies can be raised in chickens. (Stolle, col. 5, ll. 1-35.)
Thus, one skilled in the art would have known the identities and
properties of protein-wasting organisms and other undesirable digestive tract
organisms. In our view, given this knowledge, the experimentation required
to identify colony-forming immunogens would not have been undue. We
therefore do not agree with the Examiner (Answer 26) that the Specification

3 Krause et al., “An rRNA Approach for Assessing the Role of Obligate
Amino Acid-Fermenting Bacteria in Ruminal Amino Acid Deamination,”
Applied and Environmental Microbiology, Vol. 62, No. 3, pp. 815-821
(1996).
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provides “inadequate guidance as to the structure of the ‘colony-forming
immunogen.’”
We note, as argued by the Examiner, that the structure and binding of
proteins to antibodies is highly sensitive to small changes in amino acid
sequences. Nonetheless, a number of prior art references of record
demonstrate that antibodies produced from chicken eggs can effectively bind
to targeted microorganisms in the digestive tract. For example, Tokoro,4
Stolle, and Yokoyama5 disclose the preparation, from chicken eggs, of
antibodies having binding specificity sufficient to inhibit targeted
microorganisms in the digestive tract. (Tokoro, col. 12, line 4, through col.
14, line 17; Stolle, col. 6, ll. 38-46; Yokoyama 388, abstract.)
Therefore, although the sensitivity of protein-antibody interaction
might have led the skilled artisan to conclude that producing antibodies with
adequate binding specificities from chickens is not entirely predictable, the
prior art of record demonstrates that effective antibodies can be produced in
the manner recited in the claims without undue experimentation.
We agree with Appellants that one skilled in the art would have been
able to practice the full scope of the claimed subject matter without undue
experimentation. We therefore reverse the enablement rejection of claims 1,
3, 5-7 and 12-29.

4 Tokoro, U.S. Patent, 5,080,895, issued January 14, 1992.
5 Yokoyama et al., “Oral passive immunization against experimental
salmonellosis in mice using chicken egg yolk antibodies specific for
Salmonella enteritidis and S. typhimurium,” Vaccine, Vol. 16, No. 4,
pp. 388-393 (1998).
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3. WRITTEN DESCRIPTION
Claims 1, 3, 5-7, and 12-29 stand rejected under 35 U.S.C. § 112, first
paragraph, “as containing subject matter which was not described in the
specification in such a way as to reasonably convey to one skilled in the
relevant art that the inventor, at the time the application was filed, had
possession of the claimed invention.” (Answer 7.)
The Examiner urges that the claim term “immunogen” encompasses
peptide or protein antigens for which no amino acid structure has been
provided. (Id. at 8.) The Examiner also urges that “[g]iven the infinite
number of undisclosed colony-forming immunogen[s], the said undisclosed
colony[-]forming immunogen has not been adequately described. Since the
immunogen is not adequately described, the binding specificity of microbial
adherence inhibitor in the form of IgY including IgA and IgM to that
undisclosed immunogen is not adequately described.” (Id.)
The Examiner concludes that because the Specification describes
IgY-containing microbial inhibitor only from birds inoculated with
P. anaerobius, C. sticklandii, C. aminophilum, E. coli serogroup 0157: H7,
Salmonella, and Campylobacter, “one of skill in the art would reasonably
conclude that the disclosure fails to provide a representative number of
species of colony-forming immunogens, in turn, the microbial inhibitor to
said undisclosed colony-forming immunogens. Thus, Applicant was not in
possession of the claimed genus.” (Id.)
Appellants respond initially to the written description rejection by
reiterating their arguments regarding the enablement rejection. (Br. 17.)
Appellants then argue that the Specification explains how the IgY, IgA, and
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IgM from chickens’ eggs bind tightly to the adherins of invading
microorganisms to prevent the microorganisms from adhering to the
digestive tract of the host organisms, and how the albumin from the eggs
protects the antibodies’ binding activity. (Id. at 17-18.)
We will reverse this rejection. We first note that the Examiner
improperly included claims 3, 5, 12-21, and 24-29 in this ground of
rejection. Rather than reciting a broad genus, these claims recite
compositions targeted to the exact microorganisms conceded by the
Examiner as being described. (Answer 8 (“Other [than] the specific
microbial adherence inhibitor in the form of IgY that inhibits the specific
colony forming bacteria P. anaerobius, C. sticklandii, C. aminophilium, E[.]
coli, Listeria, [and] Salmonella from adhering to the rumen or digestive
track of food animal, there is inadequate written description about the
microbial adherence inhibitor . . . .”).) Thus, the rejection of these claims is
inconsistent with the Examiner’s own reasoning.
Turning to the remaining claims, the written description requirement
obliges an applicant to “convey with reasonable clarity to those skilled in the
art that, as of the filing date sought, he or she was in possession of the
invention. The invention is, for purposes of the ‘written description’ inquiry,
whatever is now claimed.” Vas-Cath Inc. v. Mahurkar, 935 F.2d 1555,
1563-64, 19 USPQ2d 1111, 1117 (Fed. Cir. 1991).
The Federal Circuit has cautioned that generic claims involving
immune responses are not invalid for lack of written description merely
because “success is not assured.” Capon v. Eshhar, 418 F.3d 1349, 1360,
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76 USPQ2d 1078, 1086 (Fed. Cir. 2005). Rather, in evaluating whether the
specification provides an adequate written description for generic claims to
biological subject matter, one must look to “a variety of factors, such as the
existing knowledge in the particular field, the extent and content of the prior
art, the maturity of the science or technology, the predictability of the aspect
at issue, and other considerations appropriate to the subject matter.” Id. at
1359, 76 USPQ2d at 1085.
Thus, “[i]t is not necessary that every permutation within a generally
operable invention be effective in order for an inventor to obtain a generic
claim, provided that the effect is sufficiently demonstrated to characterize a
generic invention.” Id.
In concluding that the Specification does not demonstrate possession
of the claimed subject matter, the Examiner has not, in our view, sufficiently
considered the state of the art. As discussed supra, both the Specification
and Krause teach that protein-wasting microorganisms were known in the
art, and that one route of protein loss is the microorganisms’ conversion of
protein to ammonia in the host’s digestive tract. (Specification 1; Krause
815, left col.)
As also discussed supra, Stolle provides an extensive list of digestive
tract pathogens to which antibodies can be raised in chickens. (Stolle, col. 5,
ll. 1-35.) Tokoro and Yokoyama also disclose the preparation, from chicken
eggs, of antibodies having binding specificity sufficient to inhibit targeted
microorganisms within the digestive tract. (Tokoro, col. 12, line 4, through
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col. 14, line 17; Yokoyama 388, abstract.) Sugita-Konishi6 also produced,
in chicken eggs, antibody capable of inhibiting pathogenic digestive tract
bacteria. (Sugita-Konishi 886.)
Therefore, the Specification and prior art provide the properties and
identities of protein-wasting and colony-forming organisms to which
antibodies can be raised. Given the extent and specificity of the prior art, we
do not agree with the Examiner that the Specification fails to demonstrate
possession of the generic claims.
Rather, when the Specification is properly viewed alongside the
knowledge in the prior art, one of skill would have recognized that
Appellants were in possession of the full scope of the claimed subject
matter. We therefore reverse the written description rejection of claims 1, 3,
5-7, and 12-29.
4. NEW MATTER
Claims 5 and 12 stand rejected under 35 U.S.C. § 112, first paragraph,
as containing new matter. (Answer 9.)
The Examiner urges that the term “‘living being’ in Claims 5 and 12
represents a departure from the Specification and the claims as originally
filed. The passages pointed out by applicant in the amendment filed
10/23/03 do not provide a clear support for the said phrase.” (Id.)
Appellants argue that “[t]he [S]pecification describes the microbial
adherence inhibitor used for food animals and hosts to inhibit adherence of

6 Sugita-Konishi et al., “Immune Functions of Immunoglobulin Y Isolated
from Egg Yolk of Hens Immunized with Various Infectious Bacteria,”
Biosci. Biotech. Biochem., Vol. 60, No. 5, pp. 886-888 (1996).
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colony-forming immunogens in the rumen and intestinal tracts,” and that the
generic term “host” is present in the Specification. (Br. 18.)
The Examiner does not explain, and we do not see, how the term
“living being,” as used in claim 5, departs from the originally filed claims
and Specification. As discussed supra, we do not interpret claim 5’s
preamble recitation, “for administration to a living being to inhibit the
adherence of a colony-forming immunogen in the digestive tract of the
living being,” as placing any limitation on claim 5, because the body of the
claim recites a structurally complete composition. Rowe v. Dror, 112 F.3d
at 478, 42 USPQ2d at 1553.
As also discussed supra, we interpret the intended result recitation in
the body of claim 5, regarding the composition’s effect “when administered
to the living being,” as not placing a positive limitation on the claim. Thus,
because it does not affect any portion of the claim having patentable weight,
the amendment of claim 5 to recite “living being” does not change the scope
of the claim. Because the amendment does not change the scope of the
claim, the amendment cannot add new matter to the claim. This analysis
applies equally to claim 12.
We therefore reverse the new matter rejection of claims 5 and 12.
5. OBVIOUSNESS OF CLAIMS 1, 3, 5, 13, 16, and 19
Claims 1, 3, 5, 13, 16, and 19 stand rejected under 35 U.S.C. § 103(a) as
being obvious over Tokoro, Kaspers,7 Pimentel,8 and Krause. (Answer 9.)

7 Kaspers et al. “Transfer of IgA from Albumen into the Yolk sac during
Embryonic Development in the Chicken,” J. Vet. Med. A, Vol. 43, pp. 225-
231 (1996).
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As an initial matter, we note that the Examiner’s reliance on the
abstract of the Kaspers article, rather than the full text, is contrary to
established Office-approved practice. The Memorandum from Stephen
Kunin, Deputy Commissioner for Patent Examination Policy, dated
April 29, 2002 (copy attached), states that, except in circumstances not
applicable here, no appeal with a rejection relying on an abstract should be
forwarded when the underlying article qualifies as prior art. See also MPEP
§ 706.02 (“Citation of and reliance upon an abstract without citation of and
reliance upon the underlying scientific document is generally inappropriate
where both the abstract and the underlying document are prior art.”).
However, the full text of the Kaspers article was cited to Appellants
on February 13, 2004, in related Application Serial No. 10/038,260.
Appellants therefore had notice of the contents of the Kaspers article before
they filed their Appeal Brief. Appellants do not allege that the Examiner’s
interpretation of the abstract is inconsistent with the full text of the article.
We therefore do not consider the Examiner’s failure to cite the full article to
be prejudicial to Appellants, and see no reason to remand the application.
The Examiner cites Tokoro as preparing antibodies to pathogenic
E. coli strains in chicken eggs, separating the yolk and albumin from the
shell, drying the antibody containing egg preparation to form a powder
product, and adding the product to livestock food. (Answer 9-10.) The
Examiner relies on Kaspers to establish that “IgG (IgY) is [the] primary
8 Pimentel, U.S. Patent 5,741,489, issued April 21, 1998.
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immunoglobulin isotype from the egg yolk[,] while IgM and IgA are mainly
found in the albumin.” (Id. at 10.)
The Examiner cites Pimentel as teaching that “whole egg (white and
yolk) antibody can be dried and mixed with feed without first isolating the
antibodies from the yolk,” and that “antibodies have been reported to be
more resistant to degradation by gastric acidity when [] contained in the
spray-dried whole egg as compared to purified spray[]-dried antibodies.”
(Id. at 10-11.)
The Examiner cites Krause as disclosing that P. anaerobius,
C. aminophilum, and C. sticklandii cause nutrition depletion in livestock,
thereby decreasing growth. (Id. at 11.)
The Examiner concludes that it would have been obvious to substitute
P. anaerobius, C. aminophilum, and C. sticklandii for the E. coli strains of
Tokoro to produce eggs containing antibodies to the protein wasting
organisms. (Id.) As motivation for the substitution, the Examiner cites
Tokoro’s disclosure of the simplicity, efficiency and low cost of making egg
antibody, Pimentel’s disclosure that whole egg preparations of antibodies
resist gastric degradation, and Krause’s disclosure that P. anaerobius,
C. aminophilum, and C. sticklandii cause growth-inhibiting nutrition
depletion in livestock. (Id.)
We agree with the Examiner that these teachings would have made
claims 1, 3, and 5 obvious to one of ordinary skill.
Claim 5 is representative of claims 1, 3 and 5. As discussed supra, we
interpret claim 5 to encompass a composition comprising the dried non-shell

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components of a bird egg which contains IgY, IgA, and IgM antibodies to
E. coli, Listeria, Salmonella or Campylobacter.
Tokoro describes (col. 4, line 67, through col. 5, line 6) the production
of antibodies in chickens to a number of pathogenic E. coli strains,
“includ[ing] those coliform bacteria or factors which cause colibacillosis,
particularly diarrhea such as ‘scour’ in young animals such as piglets or
calves. Specific examples of such bacteria or factors are porcine ETEC
(enterotoxigenic E. coli) . . . .”
Tokoro also discloses that “[i]n a preferred embodiment of the
production method of an antibody-containing substance, the yolk, albumen,
or overall ovum of an egg of an immunized hen is simply dried to form a
powder after homogenization to yield the desired product without
fractionation such as ultrafiltration.” (Col. 8, ll. 14-19 (emphasis added).)
Tokoro uses “overall ovum” to refer to the yolk and albumin separated from
the egg shells. (See col. 6, ll. 17-18 (“In some cases, both the yolk and
albumen (overall ovum) of each egg may be used.”).)
Tokoro therefore describes a composition containing antibodies to
E. coli, one of the organisms recited in claim 5. The composition is prepared
by inoculating a female bird, obtaining antibodies in the non-shell portion of
the birds’ eggs, and drying the resulting composition. (Tokoro, col. 5, line
29, through col. 6, line 27.) The composition is therefore prepared using the
exact steps recited in claim 5. Because Tokoro’s composition is obtained
exactly as claimed, Tokoro’s composition necessarily contains the IgY, IgM
and IgA recited in claim 5. By itself, Tokoro therefore describes all of the
limitations in claim 5.
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“It is well settled that a claim is anticipated if each and every
limitation is found either expressly or inherently in a single prior art
reference.” Celeritas Techs. Ltd. v. Rockwell Int’l Corp., 150 F.3d 1354,
1361, 47 USPQ2d 1516, 1522 (Fed. Cir. 1998). Because “anticipation is the
epitome of obviousness,” Connell v. Sears, Roebuck & Co., 722 F.2d 1542,
1548, 220 USPQ 193, 198 (Fed. Cir. 1983), we agree with the Examiner that
claim 5 would have been obvious in view of the cited references.
Appellants argue that “[t]here is no disclosure in Tokoro '895 of an
IgY immunoglobulin that binds to a colony-forming immunogen.”
(Br. 23-24.) We do not agree.
“Under the principles of inherency, if the prior art necessarily
functions in accordance with, or includes, the claims limitations, it
anticipates.” In re Cruciferous Sprout Litig., 301 F.3d 1343, 1349, 64
USPQ2d 1202, 1206 (Fed. Cir. 2002) (quoting MEHL/Biophile Int’l Corp. v.
Milgraum, 192 F.3d 1362, 1365, 52 USPQ2d 1303, 1305 (Fed. Cir. 1999)).
As discussed supra, Tokoro describes inoculating chickens with
pathogenic E. coli strains. Claim 5 clearly states that E. coli is a “colony-
forming immunogen.” As also discussed supra, one of Tokoro’s preferred
embodiments is the composition prepared by simply separating the antibody-
containing yolk and albumin from the egg shells, and drying the
composition, the exact steps recited in claim 5. Because it is made using the
exact steps recited in claim 5, Tokoro’s preferred composition necessarily
contains the IgY, IgM and IgA antibodies recited in the claim.
Appellants argue that Kaspers, Pimentel, and Krause do not
individually teach various claim limitations. (Br. 24-25.)
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We do not find Appellants’ argument persuasive. First, the Examiner
relies on the combined teachings of the references, and it is well settled that
“[n]on-obviousness cannot be established by attacking references
individually where the rejection is based upon the teachings of a
combination of references. . . . [The reference] must be read, not in
isolation, but for what it fairly teaches in combination with the prior art as a
whole.” In re Merck & Co., Inc., 800 F.2d 1091, 1097, 231 USPQ 375, 380
(Fed. Cir. 1986). In addition, Tokoro discloses all of the limitations of claim
5, and claims 1, 3, and 5 stand or fall together.
Appellants argue that
[T]here are no motivating directions or suggestions in these
references that would impel one skilled in the art to produce the
claimed method. There is no teaching of a method of
promoting the growth of food animals by binding IgY
immunoglobulins combined with IgM and IgA
immunoglobulins to protein-wasting immunogens to inhibit the
ability of the protein-wasting immunogens to adhere to the
rumen or intestinal tracts of food animals and to reduce the
ability of the immunogens to multiply.

(Br. 25-26 (emphasis added).)
We are not persuaded by Appellants’ argument. All of the pending
claims are directed to products, not processes. Thus, claim 5 does not
require a step of binding antibodies to a microorganism. Rather, claim 5
recites a dried composition comprising the non-shell portions of an egg that
contains IgY, IgA, and IgM antibodies to E. coli, Listeria, Salmonella or
Campylobacter.
As established supra, Tokoro describes a composition having the
exact ingredients required by claim 5. Tokoro therefore demonstrates that
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one of ordinary skill would have been motivated to produce the composition
recited in claim 5.
Thus, we agree with the Examiner that claim 5 would have been
obvious to one of ordinary skill at the time of the invention. Claims 1 and 3
fall with claim 5 because Appellants do not argue them separately. We
therefore affirm the rejection of claims 1, 3 and 5 over Tokoro, Kaspers,
Pimentel, and Krause.
Claims 13, 16, and 19 stand on a different footing, however.
As discussed supra, claims 13, 16, and 19 recite dried avian egg
compositions containing antibodies to P antigen from P. anaerobius,
CS antigen from C. sticklandii, or CA antigen from C. aminophilum. As
also discussed supra, P, CS, and CA antigens are bacterial antigens which
can be separated from whole cells in culture by centrifugation.
We agree with the Examiner that, because Krause identifies
P. anaerobius, C. sticklandii and C. aminophilum as causing the waste of
dietary protein in food animals, the reference suggests inoculating birds with
cells of these organisms, so as to produce antibodies to the organisms in the
birds’ eggs. However, we do not see, and the Examiner does not point to,
any evidence suggesting that immunizing birds with whole cells of
P. anaerobius, C. sticklandii, or C. aminophilum would yield antibody to P,
CS, or CA antigen, specifically. That is, the Examiner has not pointed to
any evidence showing that immunizing birds with cells of the organisms
would necessarily result in the production of eggs having antibodies to P,
CS, or CA antigen, as required in claims 13, 16, and 19.
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Moreover, the Examiner has not shown that the cited references
would have suggested to one of ordinary skill in the art seeking to produce
protective antibodies against P. anaerobius, C. sticklandii, and
C. aminophilum that it would have been desirable to make compositions
containing antibodies to the culture supernatants of those organisms, rather
than the cells. Nor has the Examiner shown that one of ordinary skill would
have had a reasonable expectation that inoculating birds with the culture
supernatants of P. anaerobius, C. sticklandii, and C. aminophilum, rather
than whole cells, would have yielded antibodies capable of inhibiting the
organism in the digestive tracts of food animals.
Thus, in our view, the Examiner has not established that one of
ordinary skill would have been motivated to produce compositions
containing antibodies to P antigen from P. anaerobius, CS antigen from
C. sticklandii, or CA antigen from C. aminophilum, with a reasonable
expectation that inoculating birds with P, CS, or CA antigen would have
successfully produced antibody capable of inhibiting P. anaerobius,
C. sticklandii, or C. aminophilum. We therefore reverse the obviousness
rejection of claims 13, 16 and 19.
To summarize, Tokoro describes a composition encompassed by
representative claim 5. We therefore affirm the obviousness rejection of
claims 1, 3 and 5. However, because the cited references do not teach or
suggest preparing a dried avian egg composition containing antibodies to P,
CS, or CA antigens, we reverse the obviousness rejection of claims 13, 16,
and 19.

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6. OBVIOUSNESS OF CLAIMS 14, 15, 17, 18, 20 AND 21
Claims 14, 15, 17, 18, 20 and 21 stand rejected under 35 U.S.C.
§ 103(a) as being obvious in view of Tokoro, Kaspers, Pimentel, and
Krause, as applied to claims 1, 3, 5, 13, 16, and 19, and further in view of
Adalsteinsson9 and Betz.10 (Answer 11-13.)
We reverse this rejection.
Claims 14, 15, 17, 18, 20, and 21 all ultimately depend from claim 13,
16, or 19. As discussed supra, claims 13, 16, and 19 recite compositions
comprising antibodies to either P antigen, CS antigen, or CA antigen. As
also discussed supra, the Examiner has not shown, and we do not see, where
Tokoro, Kaspers, Pimentel, and Krause suggest a composition containing
antibodies to those antigens. We see nothing in Adalsteinsson, Betz, or the
Examiner’s reasoning, which remedies the deficiencies of Tokoro, Kaspers,
Pimentel, and Krause. We therefore reverse the obviousness rejection of
claims 14, 15, 17, 18, 20 and 21.
7. OBVIOUSNESS OF CLAIM 5
Claim 5 also stands rejected under 35 U.S.C. § 103(a) as being
obvious in view of Tokoro, Kaspers, Pimentel, Stolle, Sugita-Konishi, and
Yokoyama. (Answer 13.)
As we understand it, the basis of this rejection is that the non-E. coli
embodiments of claim 5 would have been obvious based on the cited
references. However, for the reasons discussed supra, we conclude that
Tokoro anticipates claim 5. We therefore agree with the Examiner that

9 Adalsteinsson et al., U.S. Patent 6,086,878, issued July 11, 2000.
10 Betz et al., U.S. Patent 4,166,867, issued September 4, 1979.
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claim 5 is unpatentable over the cited references, regardless of whether the
references would have suggested the Listeria, Salmonella, or Campylobacter
embodiments of the claim.
In response to this rejection, Appellants reiterate their previous
arguments regarding Tokoro, Kaspers, and Pimentel. (Br. 28.) These
arguments are addressed above. Appellants also argue that Stolle, Sugita-
Konishi, and Yokoyama do not disclose binding IgY, IgM, and IgA with
protein-wasting organisms in the digestive tract or that the binding of IgY to
organisms is assisted by IgM and IgA. (Id. at 29-30.) Appellants further
argue that the objective evidence of record does not provide a clear and
particular showing sufficient to motivate one of skill to combine the
references. (Id. at 30.)
We do not find these arguments persuasive. Again, Tokoro discloses,
expressly or inherently, a method encompassed by claim 5. Therefore, the
teachings of Stolle, Sugita-Konishi, and Yokoyama, as well as the
combinability of those references, are all irrelevant to the patentability of
claim 5.
We therefore affirm the Examiner’s rejection of claim 5 over Tokoro,
Kaspers, Pimentel, Stolle, Sugita-Konishi, and Yokoyama.
8. OBVIOUSNESS OF CLAIMS 6, 7, 12, 22, AND 23
Claim 6, 7, 12, 22, and 23 stand rejected under 35 U.S.C. § 103(a) as
being obvious over Tokoro, Kaspers, Pimentel, Stolle, Sugita-Konishi,
Yokoyama, Adalsteinsson, and Betz. (Answer 16.)
As discussed supra, Tokoro teaches preparing dried whole avian egg
compositions containing antibodies to pathogenic digestive tract
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microorganisms, including E. coli. The Examiner concedes that Tokoro
does not disclose coating the antibody-containing composition onto feed
carrier materials as recited in claim 6 (Answer 17), nor does Tokoro disclose
using a feed carrier material having soybean hulls, rice hulls, corn,
cottonseed hulls, distilled dried grains, or beet pulp, as recited in claim 7
(id. at 18).
To meet these deficiencies, the Examiner cites Adalsteinsson as
disclosing that “hyperimmunized spray-dried egg powder can be mixed with
food animal feed rations or sprayed to coat directly onto carrier[s] such as
food pellets to maintain[] antibody titers sufficient to increase muscle
protein and reduce fat in subject animal[s].” (Id. at 19.) The Examiner cites
Betz as disclosing the desirability of using the ingredients recited in claim 7
in animal feed. (Id.)
Appellants argue that these claims require that “[t]he separated entire
contents of the harvested eggs are not dried before they are coated onto the
dry feed carrier material. This avoids the reduction of the effectiveness of
the IgY, IgM and IgA immunoglobulins caused by the process of drying the
entire contents of the harvested eggs.” (Br. 31.) Appellants further argue
that the Examiner has failed to show any clear and particular motivation for
combining Tokoro with the other references.
We do not find Appellants’ argument persuasive.
Claim 6 is representative of these claims. As discussed supra, we
interpret claim 6 as encompassing a composition comprising the dried non-
shell components of chicken eggs which contain IgY, IgA, and IgM
antibodies to microorganisms which adhere to the digestive tract of a host
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animal, the antibody-containing egg composition having been coated on to a
dry feed carrier material.
Contrary to Appellants’ argument, claim 6 does not require the
claimed composition to be produced by a process in which the contents of
the harvested eggs are not dried before they are coated on to the feed carrier.
Claim 6 recites the steps of separating the contents of the harvested eggs,
providing a dry feed carrier material, and then coating the feed carrier
material with the contents of the eggs. Claim 6 does not contain any
language limiting the claim to the positively recited steps.
Adalsteinsson describes a composition comprising an orally
administered chicken egg-derived antibody that binds a gastrointestinal
neuro-modulator, such as cholecystokinin. (Col. 4, line 58, through col. 5,
line 10.) Adalsteinsson teaches that the composition can be made by “drying
the egg into an egg powder . . . [which] can be mixed with food animal feed
rations or sprayed directly onto food pellets preferably in oil and thus fed
directly to food animals in a simple fashion.” (Col. 9, ll. 29-38.)
Thus, one of ordinary skill, applying Tokoro’s teachings to make
orally administered dried whole egg compositions comprising antibodies to
microorganisms harmful to food animals, would have recognized from
Adalsteinsson the desirability of coating antibody-containing dried egg
powder intended for oral administration onto feed pellets. We therefore
agree with the Examiner that one of ordinary skill would have been
motivated by Adalsteinsson to coat Tokoro’s compositions onto a feed
carrier, as recited in claim 6.
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We affirm the obviousness rejection of claim 6. Claims 7, 12, 22, and
23 fall with claim 6.
9. OBVIOUSNESS OF CLAIMS 24-29
Claims 24-29 stand rejected under 35 U.S.C. § 103(a) as being
obvious over Tokoro, Kaspers, Pimentel, Stolle, Krause, Adalsteinsson, and
Betz. (Answer 20.)
We reverse this rejection.
Claims 24-29 all recite compositions comprising antibodies to either
P antigen, CS antigen, or CA antigen. As discussed supra with respect to
claims 13-21, the Examiner has not shown, and we do not see, where
Tokoro, Kaspers, Pimentel, Krause, Adalsteinsson and Betz, alone or in
combination, suggest a composition containing antibodies to those antigens.
We see nothing in Stolle, or the Examiner’s reasoning, that remedies the
deficiencies of Tokoro, Kaspers, Pimentel, Krause, Adalsteinsson and Betz.
We therefore reverse the obviousness rejection of claims 24-29.
SUMMARY
We reverse the written description and enablement rejections of
claims 1, 3, 5-7, and 12-29.
We reverse the new matter rejection of claims 5 and 12.
We affirm the obviousness rejections of claims 1, 3, 5-7, 12, 22 and
23.
We reverse the obvious rejections of claims 13-21 and 24-29.

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Appeal No. 2006-2575
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No time period for taking any subsequent action in connection with
this appeal may be extended under 37 CFR § 1.136(a)(1)(iv)(2006).

AFFIRMED-IN-PART

Donald E. Adams )
Administrative Patent Judge )
)
)
) BOARD OF PATENT
Eric B. Grimes )
Administrative Patent Judge ) APPEALS AND
)
) INTERFERENCES
)
Nancy J. Linck )
Administrative Patent Judge )

EBG/lbg

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Appeal No. 2006-2575
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RICHARD JOHN BARTZ
SUITE 350
6750 FRANCE AVENUE SOUTH
EDINA, MN 55435

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