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TitleYeast Display Reveals Plentiful Mutations That Improve Fusion Peptide Vaccine-Elicited Antibodies Beyond 59% HIV-1 Neutralization Breadth.
Journal, issue, pagesVaccines (Basel), Vol. 13, Issue 11, Year 2025
Publish dateOct 27, 2025
AuthorsCamila T França / Sergei Pletnev / Bharat Madan / Phinikoula S Katsamba / Krisha McKee / Nicholas C Morano / Baoshan Zhang / Fabiana Bahna / Tatsiana Bylund / Bob C Lin / Mark K Louder / Seetha Mannepalli / Rajani Nimrania / Sijy O'Dell / Nicole A Doria-Rose / Peter D Kwong / Lawrence Shapiro / Zizhang Sheng / Tongqing Zhou / Brandon J DeKosky /
PubMed Abstract: Vaccine elicitation of antibodies with high HIV-1 neutralization breadth is a long-standing goal. Recently, the induction of such antibodies has been achieved at the fusion peptide site of ...: Vaccine elicitation of antibodies with high HIV-1 neutralization breadth is a long-standing goal. Recently, the induction of such antibodies has been achieved at the fusion peptide site of vulnerability. Questions remain, however, as to how much anti-fusion peptide antibodies can be improved and whether their neutralization breadth and potency are sufficient to prevent HIV-1 infection. : Here, we use yeast display coupled with deep mutational screening and biochemical and structural analyses to study the improvement of the best fusion peptide-directed, vaccine-elicited antibody, DFPH_a.01, with an initial 59% breadth. : Yeast display identified both single and double mutations that improved recognition of HIV-1 envelope trimers. We characterized two paratope-distal light chain (LC) mutations, S10R and S59P, which together increased breadth to 63%. Biochemical analysis demonstrated DFPH-a.01_10R59P-LC, and its component mutations, to have increased affinity and stability. Cryo-EM structural analysis revealed elbow-angle influencing by S10R-LC and isosteric positioning by S59P-LC as explanations for enhanced breadth, affinity, and stability. : These results, along with another antibody with enhanced performance (DFPH-a.01_1G10A56K-LC with 64% breadth), suggest that mutations improving DFPH_a.01 are plentiful, an important vaccine insight.
External linksVaccines (Basel) / PubMed:41295471 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

72108

9q0w

EMDB-72108, PDB-9q0w:
Cryo-EM Structure of HIV-1 BG505DS-SOSIP.664 Env Trimer Bound to DFPH-a.01_10R59P_LC Fab
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

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

Source
  • human immunodeficiency virus 1
  • macaca (macaques)
KeywordsVIRAL PROTEIN / antibody improvement / broadly neutralizing antibody / epitope / fusion peptide / HIV-1 vaccine / paratope

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