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

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

Broadly neutralizing antibodies have been isolated that 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.

0022-538X
6952-6959
Pritchard, Laura K.
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Spencer, Daniel I.R.
1b8ce4f6-518b-4add-b8af-f39b011c2e4d
Royle, Louise
310a52f9-a086-482c-9963-857a3af2363b
Vasiljevic, Snezana
17e075b4-520d-4b9b-a4a7-08ac394ae5e1
Krumm, Stefanie A.
534eb807-ab99-4eef-984a-c26dc5028c9e
Doores, Katie J.
52d36150-7a62-4f9d-8348-c83a789d52e6
Crispin, Matthew
cd980957-0943-4b89-b2b2-710f01f33bc9
Pritchard, Laura K.
bfa1d1b4-50b6-401f-b153-8c3322b2e726
Spencer, Daniel I.R.
1b8ce4f6-518b-4add-b8af-f39b011c2e4d
Royle, Louise
310a52f9-a086-482c-9963-857a3af2363b
Vasiljevic, Snezana
17e075b4-520d-4b9b-a4a7-08ac394ae5e1
Krumm, Stefanie A.
534eb807-ab99-4eef-984a-c26dc5028c9e
Doores, Katie J.
52d36150-7a62-4f9d-8348-c83a789d52e6
Crispin, Matthew
cd980957-0943-4b89-b2b2-710f01f33bc9

Pritchard, Laura K., Spencer, Daniel I.R., Royle, Louise, Vasiljevic, Snezana, Krumm, Stefanie A., Doores, Katie J. and Crispin, Matthew (2015) Glycan microheterogeneity at the PGT135 antibody recognition site on HIV-1 gp120 reveals a molecular mechanism for neutralization resistance. Journal of Virology, 89 (13), 6952-6959. (doi:10.1128/JVI.00230-15).

Record type: Article

Abstract

Broadly neutralizing antibodies have been isolated that 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.

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Published date: 2015

Identifiers

Local EPrints ID: 414267
URI: http://eprints.soton.ac.uk/id/eprint/414267
ISSN: 0022-538X
PURE UUID: 6ba58ba9-dc91-4f34-8441-9c403c0c9594
ORCID for Matthew Crispin: ORCID iD orcid.org/0000-0002-1072-2694

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Date deposited: 21 Sep 2017 16:31
Last modified: 16 Mar 2024 04:30

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Contributors

Author: Laura K. Pritchard
Author: Daniel I.R. Spencer
Author: Louise Royle
Author: Snezana Vasiljevic
Author: Stefanie A. Krumm
Author: Katie J. Doores
Author: Matthew Crispin ORCID iD

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