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TitlePriming antibody responses to the fusion peptide in rhesus macaques.
Journal, issue, pagesNPJ Vaccines, Vol. 9, Issue 1, Page 126, Year 2024
Publish dateJul 12, 2024
AuthorsChristopher A Cottrell / Payal P Pratap / Kimberly M Cirelli / Diane G Carnathan / Chiamaka A Enemuo / Aleksandar Antanasijevic / Gabriel Ozorowski / Leigh M Sewall / Hongmei Gao / Joel D Allen / Bartek Nogal / Murillo Silva / Jinal Bhiman / Matthias Pauthner / Darrell J Irvine / David Montefiori / Max Crispin / Dennis R Burton / Guido Silvestri / Shane Crotty / Andrew B Ward /
PubMed AbstractImmunodominance of antibodies targeting non-neutralizing epitopes and the high level of somatic hypermutation within germinal centers (GCs) required for most HIV broadly neutralizing antibodies ...Immunodominance of antibodies targeting non-neutralizing epitopes and the high level of somatic hypermutation within germinal centers (GCs) required for most HIV broadly neutralizing antibodies (bnAbs) are major impediments to the development of an effective HIV vaccine. Rational protein vaccine design and non-conventional immunization strategies are potential avenues to overcome these hurdles. Here, we report using implantable osmotic pumps to continuously deliver a series of epitope-targeted immunogens to rhesus macaques over the course of six months to prime and elicit antibody responses against the conserved fusion peptide (FP). GC responses and antibody specificities were tracked longitudinally using lymph node fine-needle aspirates and electron microscopy polyclonal epitope mapping (EMPEM), respectively, to show antibody responses to the FP/N611 glycan hole region were primed, although exhibited limited neutralization breadth. Application of cryoEMPEM delineated key residues for on-target and off-target responses that can drive the next round of structure-based vaccine design.
External linksNPJ Vaccines / PubMed:38997302 / PubMed Central
MethodsEM (single particle)
Resolution3.37 - 3.9 Å
Structure data

40822

8swv

EMDB-40822, PDB-8swv:
BG505 Boost2 SOSIP.664 in complex with NHP polyclonal antibody IF1
Method: EM (single particle) / Resolution: 3.37 Å

40823

8sww

EMDB-40823, PDB-8sww:
BG505 Boost2 SOSIP.664 in complex with NHP polyclonal antibody IF3
Method: EM (single particle) / Resolution: 3.4 Å

40824

8swx

EMDB-40824, PDB-8swx:
BG505 Boost2 SOSIP.664 in complex with NHP polyclonal antibody Base4
Method: EM (single particle) / Resolution: 3.9 Å

40981

8t2e

EMDB-40981, PDB-8t2e:
BG505 Boost2 SOSIP.664 in complex with NHP polyclonal antibody FP3
Method: EM (single particle) / Resolution: 3.5 Å

40982

8t2f

EMDB-40982, PDB-8t2f:
BG505 Boost2 SOSIP.664 in complex with NHP polyclonal antibody N289
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

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

Source
  • human immunodeficiency virus 1
  • macaca mulatta (Rhesus monkey)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HIV-1 / Env / NHP / Antibody / Fusion Peptide / Polyclonal / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex

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