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TitleFusion peptide of HIV-1 as a site of vulnerability to neutralizing antibody.
Journal, issue, pagesScience, Vol. 352, Issue 6287, Page 828-833, Year 2016
Publish dateMay 13, 2016
AuthorsRui Kong / Kai Xu / Tongqing Zhou / Priyamvada Acharya / Thomas Lemmin / Kevin Liu / Gabriel Ozorowski / Cinque Soto / Justin D Taft / Robert T Bailer / Evan M Cale / Lei Chen / Chang W Choi / Gwo-Yu Chuang / Nicole A Doria-Rose / Aliaksandr Druz / Ivelin S Georgiev / Jason Gorman / Jinghe Huang / M Gordon Joyce / Mark K Louder / Xiaochu Ma / Krisha McKee / Sijy O'Dell / Marie Pancera / Yongping Yang / Scott C Blanchard / Walther Mothes / Dennis R Burton / Wayne C Koff / Mark Connors / Andrew B Ward / Peter D Kwong / John R Mascola /
PubMed AbstractThe HIV-1 fusion peptide, comprising 15 to 20 hydrophobic residues at the N terminus of the Env-gp41 subunit, is a critical component of the virus-cell entry machinery. Here, we report the ...The HIV-1 fusion peptide, comprising 15 to 20 hydrophobic residues at the N terminus of the Env-gp41 subunit, is a critical component of the virus-cell entry machinery. Here, we report the identification of a neutralizing antibody, N123-VRC34.01, which targets the fusion peptide and blocks viral entry by inhibiting conformational changes in gp120 and gp41 subunits of Env required for entry. Crystal structures of N123-VRC34.01 liganded to the fusion peptide, and to the full Env trimer, revealed an epitope consisting of the N-terminal eight residues of the gp41 fusion peptide and glycan N88 of gp120, and molecular dynamics showed that the N-terminal portion of the fusion peptide can be solvent-exposed. These results reveal the fusion peptide to be a neutralizing antibody epitope and thus a target for vaccine design.
External linksScience / PubMed:27174988 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.54 - 17.0 Å
Structure data

EMDB-8125:
BG505 SOSIP.664 HIV-1 Env trimer in complex with anti-HIV fusion peptide targeting N123-VRC34.01 Fab
Method: EM (single particle) / Resolution: 17.0 Å

PDB-5i8c:
Crystal Structure of HIV-1 Clade A BG505 Fusion Peptide (residue 512-520) in Complex with Broadly Neutralizing Antibody VRC34.01 Fab
Method: X-RAY DIFFRACTION / Resolution: 1.54 Å

PDB-5i8e:
Crystal Structure of Broadly Neutralizing HIV-1 Fusion Peptide-Targeting Antibody VRC34.01 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.655 Å

PDB-5i8h:
Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer in Complex with V3 Loop-targeting Antibody PGT122 Fab and Fusion Peptide-targeting Antibody VRC34.01 Fab
Method: X-RAY DIFFRACTION / Resolution: 4.301 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / HIV-1 / envelope / trimer / fusion peptide / antibody / neutralizing

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