Glycan microheterogeneity at the PGT135 antibody recognition site on HIV-1 gp120 reveals a molecular mechanism for neutralization resistance

TY - JOUR

T1 - Glycan microheterogeneity at the PGT135 antibody recognition site on HIV-1 gp120 reveals a molecular mechanism for neutralization resistance

AU - Pritchard, Laura K

AU - Spencer, Daniel I R

AU - Royle, Louise

AU - Vasiljevic, Snezana

AU - Krumm, Stefanie A

AU - Doores, Katie J

AU - Crispin, Max

PY - 2015

Y1 - 2015

N2 - Broadly neutralizing antibodies have been isolated which bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392 and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity are therefore important parameters in HIV-1 vaccine design.

AB - Broadly neutralizing antibodies have been isolated which bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392 and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity are therefore important parameters in HIV-1 vaccine design.

U2 - 10.1128/JVI.00230-15

DO - 10.1128/JVI.00230-15

M3 - Article

C2 - 25878100

SN - 0022-538X

JO - Journal of Virology

JF - Journal of Virology

ER -