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TitleMutation-guided vaccine design: A process for developing boosting immunogens for HIV broadly neutralizing antibody induction.
Journal, issue, pagesCell Host Microbe, Vol. 32, Issue 5, Page 693-709.e7, Year 2024
Publish dateMay 8, 2024
AuthorsKevin Wiehe / Kevin O Saunders / Victoria Stalls / Derek W Cain / Sravani Venkatayogi / Joshua S Martin Beem / Madison Berry / Tyler Evangelous / Rory Henderson / Bhavna Hora / Shi-Mao Xia / Chuancang Jiang / Amanda Newman / Cindy Bowman / Xiaozhi Lu / Mary E Bryan / Joena Bal / Aja Sanzone / Haiyan Chen / Amanda Eaton / Mark A Tomai / Christopher B Fox / Ying K Tam / Christopher Barbosa / Mattia Bonsignori / Hiromi Muramatsu / S Munir Alam / David C Montefiori / Wilton B Williams / Norbert Pardi / Ming Tian / Drew Weissman / Frederick W Alt / Priyamvada Acharya / Barton F Haynes /
PubMed AbstractA major goal of HIV-1 vaccine development is the induction of broadly neutralizing antibodies (bnAbs). Although success has been achieved in initiating bnAb B cell lineages, design of boosting ...A major goal of HIV-1 vaccine development is the induction of broadly neutralizing antibodies (bnAbs). Although success has been achieved in initiating bnAb B cell lineages, design of boosting immunogens that select for bnAb B cell receptors with improbable mutations required for bnAb affinity maturation remains difficult. Here, we demonstrate a process for designing boosting immunogens for a V3-glycan bnAb B cell lineage. The immunogens induced affinity-matured antibodies by selecting for functional improbable mutations in bnAb precursor knockin mice. Moreover, we show similar success in prime and boosting with nucleoside-modified mRNA-encoded HIV-1 envelope trimer immunogens, with improved selection by mRNA immunogens of improbable mutations required for bnAb binding to key envelope glycans. These results demonstrate the ability of both protein and mRNA prime-boost immunogens for selection of rare B cell lineage intermediates with neutralizing breadth after bnAb precursor expansion, a key proof of concept and milestone toward development of an HIV-1 vaccine.
External linksCell Host Microbe / PubMed:38670093
MethodsEM (single particle)
Resolution3.57 - 4.32 Å
Structure data

27706

8dto

EMDB-27706, PDB-8dto:
Vaccine elicited Antibody MU89 bound to CH848.D949.10.17_N133D_N138T.DS.SOSIP.664 HIV-1 Env trimer
Method: EM (single particle) / Resolution: 3.57 Å

27776

8dy6

EMDB-27776, PDB-8dy6:
Vaccine elicited Antibody MU89+S27Y bound to CH848.D949.10.17_N133D_N138T.DS.SOSIP.664 HIV-1 Env trimer
Method: EM (single particle) / Resolution: 4.32 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • Homo sapiens (human)
  • human immunodeficiency virus 1
  • human immunodeficiency virus
  • mus musculus (house mouse)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HIV-1 envelope / vaccine-induced antibody / broadly neutralizing antibody / VIRAL PROTEIN-IMMUNE SYSTEM complex

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