Appeal No. 95-2419
Application 07/850,770
The findings of the present study suggest that consensus N-linked
glycosylation sites that are important for viral infectivity are not randomly
distributed in the gp120 molecule. Bolmstedt et al. (27) reported that the
removal of N-linked glycosylation sites represented by our mutants 406 and
463 from the envelope recombinant proteins expressed by a vaccine
expression vector did not affect CD4 receptor binding or syncytium
formation (27). Their results are compatible with our findings that CD4-
positive SupT1 cells were readily infected by our mutants 406 and 463, and
support our hypothesis that the N-linked glycosylation sites located in the
carboxyl-terminal half of gp120 are more dispensable for viral infectivity that
those located in the amino-terminal half.
The Bolmstedt reference cited in Lee is of record. According to the record copy of the
document, Bolmstedt was published in 1991. Thus, it appears to be legally available prior
art on this record. Lee indicates that Bolmstedt “reported that the removal of N-linked
glycosylation sites represented by our mutants 406 and 463 . . . did not effect CD4
receptor binding or syncytium formation.” We point out that the allowed claims pending in
this application encompass proteins “in which at least one of the N-linked glycosylation
sequences corresponding to . . . 406 and 463" has been deglycosylated.
See claim 10 on appeal.
Upon return of the application, appellants and the examiner should take a step back
and reassess the patentability of the allowed claims on appeal in light of the disclosure of
Bolmstedt. The examiner should make sure that the record accurately reflects the outcome
of that consideration.
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