Glycan Microheterogeneity at the PGT135 Antibody Recognition Site on HIV-1 gp120 Reveals a Molecular Mechanism for Neutralization Resistance |
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| Authors: | Laura K Pritchard Daniel I R Spencer Louise Royle Snezana Vasiljevic Stefanie A Krumm Katie J Doores Max Crispin |
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| Institution: | aOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom;bLudger Ltd., Culham Science Centre, Abingdon, Oxfordshire, United Kingdom;cKing''s College London School of Medicine at Guy''s, King''s and St Thomas'' Hospitals, Guy''s Hospital, Great Maze Pond, London, United Kingdom |
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| 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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