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TitleEpitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1.
Journal, issue, pagesNat Med, Vol. 24, Issue 6, Page 857-867, Year 2018
Publish dateJun 4, 2018
AuthorsKai Xu / Priyamvada Acharya / Rui Kong / Cheng Cheng / Gwo-Yu Chuang / Kevin Liu / Mark K Louder / Sijy O'Dell / Reda Rawi / Mallika Sastry / Chen-Hsiang Shen / Baoshan Zhang / Tongqing Zhou / Mangaiarkarasi Asokan / Robert T Bailer / Michael Chambers / Xuejun Chen / Chang W Choi / Venkata P Dandey / Nicole A Doria-Rose / Aliaksandr Druz / Edward T Eng / S Katie Farney / Kathryn E Foulds / Hui Geng / Ivelin S Georgiev / Jason Gorman / Kurt R Hill / Alexander J Jafari / Young D Kwon / Yen-Ting Lai / Thomas Lemmin / Krisha McKee / Tiffany Y Ohr / Li Ou / Dongjun Peng / Ariana P Rowshan / Zizhang Sheng / John-Paul Todd / Yaroslav Tsybovsky / Elise G Viox / Yiran Wang / Hui Wei / Yongping Yang / Amy F Zhou / Rui Chen / Lu Yang / Diana G Scorpio / Adrian B McDermott / Lawrence Shapiro / Bridget Carragher / Clinton S Potter / John R Mascola / Peter D Kwong /
PubMed AbstractA central goal of HIV-1 vaccine research is the elicitation of antibodies capable of neutralizing diverse primary isolates of HIV-1. Here we show that focusing the immune response to exposed N- ...A central goal of HIV-1 vaccine research is the elicitation of antibodies capable of neutralizing diverse primary isolates of HIV-1. Here we show that focusing the immune response to exposed N-terminal residues of the fusion peptide, a critical component of the viral entry machinery and the epitope of antibodies elicited by HIV-1 infection, through immunization with fusion peptide-coupled carriers and prefusion stabilized envelope trimers, induces cross-clade neutralizing responses. In mice, these immunogens elicited monoclonal antibodies capable of neutralizing up to 31% of a cross-clade panel of 208 HIV-1 strains. Crystal and cryoelectron microscopy structures of these antibodies revealed fusion peptide conformational diversity as a molecular explanation for the cross-clade neutralization. Immunization of guinea pigs and rhesus macaques induced similarly broad fusion peptide-directed neutralizing responses, suggesting translatability. The N terminus of the HIV-1 fusion peptide is thus a promising target of vaccine efforts aimed at eliciting broadly neutralizing antibodies.
External linksNat Med / PubMed:29867235 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.55 - 19.6 Å
Structure data

7459

6cde

EMDB-7459, PDB-6cde:
Cryo-EM structure at 3.8 A resolution of vaccine-elicited antibody vFP20.01 in complex with HIV-1 Env BG505 DS-SOSIP, and antibodies VRC03 and PGT122
Method: EM (single particle) / Resolution: 3.8 Å

7460

6cdi

EMDB-7460, PDB-6cdi:
Cryo-EM structure at 3.6 A resolution of vaccine-elicited antibody vFP16.02 in complex with HIV-1 Env BG505 DS-SOSIP, and antibodies VRC03 and PGT122
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-8420:
Cryo-EM structure of BG505 DS-SOSIP HIV-1 Env trimer in complex with vaccine elicited, fusion peptide-directed antibody vFP1.01
Method: EM (single particle) / Resolution: 8.58 Å

EMDB-8421:
Cryo-EM structure of an asymmetric complex of BG505 DS-SOSIP HIV-1 Env trimer with vaccine elicited, fusion peptide-directed antibody vFP5.01
Method: EM (single particle) / Resolution: 14.7 Å

EMDB-8422:
Cryo-EM structure of an asymmetric complex of BG505 DS-SOSIP HIV-1 Env trimer with vaccine elicited, fusion peptide-directed antibody vFP5.01
Method: EM (single particle) / Resolution: 19.6 Å

PDB-5tkj:
Structure of vaccine-elicited diverse HIV-1 neutralizing antibody vFP1.01 in complex with HIV-1 fusion peptide residue 512-519
Method: X-RAY DIFFRACTION / Resolution: 2.118 Å

PDB-5tkk:
Structure of mouse vaccination-elicited HIV neutralizing antibody vFP5.01 in complex with HIV-1 fusion peptide residue 512-519
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-6cdm:
Structure of vaccine-elicited HIV-1 neutralizing antibody vFP7.04 in complex with HIV-1 fusion peptide residue 512-519
Method: X-RAY DIFFRACTION / Resolution: 2.408 Å

PDB-6cdo:
Structure of vaccine-elicited HIV-1 neutralizing antibody vFP16.02 in complex with HIV-1 fusion peptide residue 512-519
Method: X-RAY DIFFRACTION / Resolution: 2.099 Å

PDB-6cdp:
Vaccine-elicited HIV-1 neutralizing antibody vFP20.01 in complex with HIV-1 fusion peptide residue 512-519
Method: X-RAY DIFFRACTION / Resolution: 2.456 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

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

ChemComp-MAN:
alpha-D-mannopyranose

Source
  • homo sapiens (human)
  • human immunodeficiency virus 1
  • mus musculus (house mouse)
KeywordsIMMUNE SYSTEM / Neutralizing / antibody / fusion-peptide / complex / mouse / VIRAL PROTEIN / HIV-1 Env / BG505 SOSIP / fusion peptide / VRC03 / PGT122 / vFP20.01 / vFP16.02

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