The V3 loop can adopt at least two different conformations for the highly conserved Gly-Pro-Gly-Arg sequence at the tip of the loop. Thus, the HIV-1 V3 loop has some inherent conformational flexibility that may relate to its biological function.
Oligomannose sugars on gp120 are of significance to HIV
vaccine design because of the description of the broadly
neutralizing mAb 2G12 and, more recently, of the potent
and broadly neutralizing ‘PGT’ series of mAbs, which bind
with high affinity to clusters of oligomannose moieties on
gp120. Attempts to elicit oligomannose-specific antibodies
have focused mainly on immunizing with antigenic clusters
of synthetic oligomannose or natural oligomannose.
These strategies have had limited success, suggesting that
alternative approaches are needed. Here, we present the
surface lipo-oligosaccharide (LOS) of Rhizobium radiobacter
Rv3 that antigenically mimics the 2G12 epitope, as one
potential new avenue of exploration
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