Appeal No. 2002-1366
Application No. 09/069,628
The examiner relies on Ladner for the disclosure of the identification of B. subtilis
spore coat polypeptides. Id. Ladner generally describes a method for the directed
evolution of novel binding proteins. For example, DNA molecules from a family of
similar binding domains and other structural signals which call for the display of the
protein on the outer surface of a chosen bacterial cell, bacterial spore or phage are
introduced into a genetic package. The cells or viruses bearing the binding domains
which recognize a target molecule are isolated and amplified. Successful binding
domains are characterized. Abstract. Ladner indicates that several polypeptide
components of B. subtilis spore coat have been identified, including two complete coat
protein sequences and several fragment sequences. Answer, page 6, Ladner, column
65, lines 41-54.
The examiner concludes (Answer, pages 6-7):
it would have been obvious at the time of applicant’s invention to
have used the known spore coat protein sequences or fragments and the
hybridoma technology as taught by Ladner [], with the known antibodies
labeled to heat stable spores of Bacillus cereus and subtilis wherein recent
studies have shown that crystals and endospores contain one or more
common antigens and there are known antigen-antibody reactions at
spore surface of Bacillus as taught by Walker [], because Ladner [], teach
no more than routine skill would have been required to use bacterial
spores to make monoclonal antibodies since it is well known that spores
permit the use of a variety of affinity selection conditions; and Ladner [],
teach that identification of several polypeptide components derived from
the B. subtilis spore coat.
Again, we do not find that the examiner has provided sufficient evidence to
establish a prima facie case of obviousness. The examiner has not put forth sufficient
evidence to establish a nexus between the polyclonal sera to the bacterial spores
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