Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer

Sarkar, Anita; Bale, Shridhar; Behrens, Anna-Janina; Kumar, Sonu; Sharma, Shailendra Kumar; de Val, Natalia; Pallesen, Jesper; Irimia, Adriana; Diwanji, Devan C.; Stanfield, Robyn L.; Ward, Andrew B.; Crispin, Max; Wyatt, Richard T.; Wilson, Ian A.

doi:10.1038/s41467-018-04272-y

Title: Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer

Journal Article · Wed May 16 00:00:00 EDT 2018 · Nature Communications

DOI:https://doi.org/10.1038/s41467-018-04272-y· OSTI ID:1502220

^[1]; Bale, Shridhar ^[1]; Behrens, Anna-Janina ^[2];

^[1]; Sharma, Shailendra Kumar ^[1]; de Val, Natalia ^[1]; Pallesen, Jesper ^[1]; Irimia, Adriana ^[1]; Diwanji, Devan C. ^[1]; Stanfield, Robyn L. ^[1]; Ward, Andrew B. ^[1]; Crispin, Max ^[3]; Wyatt, Richard T. ^[1];

^[1]

The Scripps Research Inst., La Jolla, CA (United States)
Univ. of Oxford (United Kingdom)
The Scripps Research Inst., La Jolla, CA (United States); Univ. of Oxford (United Kingdom); Univ. of Southampton (United Kingdom)

Furin cleavage of the HIV envelope glycoprotein is an essential step for cell entry that enables formation of well-folded, native-like glycosylated trimers, releases constraints on the fusion peptide, and limits enzymatic processing of the N-glycan shield. Here, we show that a cleavage-independent, stabilized, soluble Env trimer mimic (BG505 NFL.664) exhibits a “closed-form”, native-like, prefusion conformation akin to furin-cleaved Env trimers. The crystal structure of BG505 NFL.664 at 3.39 Å resolution with two potent bNAbs also identifies the full epitopes of PGV19 and PGT122 that target the receptor binding site and N332 supersite, respectively. Quantitative site-specific analysis of the glycan shield reveals that native-like glycan processing is maintained despite furin-independent maturation in the secretory pathway. Thus, cleavage-independent NFL Env trimers exhibit quaternary protein and carbohydrate structures similar to the native viral spike that further validate their potential as vaccine immunogen candidates.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); International AIDS Vaccine Initiative Neutralizing Antibody Center; Collaboration for AIDS Vaccine Discovery; Bill & Melinda Gates Foundation; US Agency for International Development (USAID); National Cancer Institute (NCI); National Institute of General Medical Sciences (NIGMS); Scripps Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVI-ID); Corpus Christi College; National Institutes of Health (NIH)

Grant/Contract Number:: CAVD OPP1084519; OPP1115782; AC02-06CH11357

OSTI ID:: 1502220

Journal Information:: Nature Communications, Vol. 9, Issue 1; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 32 works

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59 BASIC BIOLOGICAL SCIENCES
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Title: Structure of a cleavage-independent HIV Env recapitulates the glycoprotein architecture of the native cleaved trimer

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