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TitleVaccine-elicited and naturally elicited antibodies differ in their recognition of the HIV-1 fusion peptide.
Journal, issue, pagesFront Immunol, Vol. 15, Page 1484029, Year 2024
Publish dateNov 14, 2024
AuthorsMateo Reveiz / Kai Xu / Myungjin Lee / Shuishu Wang / Adam S Olia / Darcy R Harris / Kevin Liu / Tracy Liu / Andrew J Schaub / Tyler Stephens / Yiran Wang / Baoshan Zhang / Rick Huang / Yaroslav Tsybovsky / Peter D Kwong / Reda Rawi /
PubMed AbstractBroadly neutralizing antibodies have been proposed as templates for HIV-1 vaccine design, but it has been unclear how similar vaccine-elicited antibodies are to their naturally elicited templates. To ...Broadly neutralizing antibodies have been proposed as templates for HIV-1 vaccine design, but it has been unclear how similar vaccine-elicited antibodies are to their naturally elicited templates. To provide insight, here we compare the recognition of naturally elicited and vaccine-elicited antibodies targeting the HIV-1 fusion peptide, which comprises envelope (Env) residues 512-526, with the most common sequence being AVGIGAVFLGFLGAA. Naturally elicited antibodies bound peptides with substitutions to negatively charged amino acids at residue positions 517-520 substantially better than the most common sequence, despite these substitutions rarely appearing in HIV-1; by contrast, vaccine-elicited antibodies were less tolerant of sequence variation, with no substitution of residues 512-516 showing increased binding. Molecular dynamics analysis and cryo-EM structural analysis of the naturally elicited ACS202 antibody in complex with the HIV-1 Env trimer with an alanine 517 to glutamine substitution suggested enhanced binding to result from electrostatic interactions with positively charged antibody residues. Overall, vaccine-elicited antibodies appeared to be more fully optimized to bind the most common fusion peptide sequence, perhaps reflecting the immunization with fusion peptide of the vaccine-elicited antibodies.
External linksFront Immunol / PubMed:39611147 / PubMed Central
MethodsEM (single particle)
Resolution2.3 Å
Structure data

41461

8tox

EMDB-41461, PDB-8tox:
Cryo-EM structure of BG505 Env mutant A517E in complex with antibody ACS202 Fab
Method: EM (single particle) / Resolution: 2.3 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/ANTIVIRAL PROTEIN / IMMUNE SYSTEM / complex / viral antigen / antibody / VIRAL PROTEIN / VIRAL PROTEIN-ANTIVIRAL PROTEIN / IMMUNE SYSTEM complex

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