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Fig. 7 | Retrovirology

Fig. 7

From: Mechanisms of escape from the PGT128 family of anti-HIV broadly neutralizing antibodies

Fig. 7

Model depicting the differences in dependency on the V3 loop and surrounding glycan sites (N295, N301, N332/N334) for PGT128 and PGT130 based on the donor 36 virus. a Model of bnAb epitope on the HIV trimer. b PGT128 neutralizes the N332 viruses very potently and requires glycosylation at either position N295 or N301. However, PGT128 can only neutralize the N334 variant when both glycan sites at N295 and N301 are present. PGT130 on the other hand neutralizes both N332 and N334 variants very potently, but depends on the presence of both glycan sites at N295 and N301. Differences are also observed in the V3 loop residues that should be reverted to confer and improve neutralization. PGT128 is less dependent on the V3 loop composition when N332 is glycosylated. It neutralizes the 1AA mutant virus potently and with increasing changes in V3, its potency, as well as the neutralization plateau, increases. If the glycan is at position N334, the bnAb only neutralizes the 7AA variant. The neutralization potency of PGT130, however, decreases slightly with increasing changes in the V3 loop in the N332 virus variants, hinting that PGT130 is less dependent on V3 loop conformation. In the presence of the N334 glycan, PGT130 only neutralized the 3AA and 7AA mutants and potency, as well as the neutralization plateau, increases when more changes were introduced. The dependencies are highlighted in accordance with the figure key

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