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TitleEngineering immunogens that select for specific mutations in HIV broadly neutralizing antibodies.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 9503, Year 2024
Publish dateNov 3, 2024
AuthorsRory Henderson / Kara Anasti / Kartik Manne / Victoria Stalls / Carrie Saunders / Yishak Bililign / Ashliegh Williams / Pimthada Bubphamala / Maya Montani / Sangita Kachhap / Jingjing Li / Chuancang Jaing / Amanda Newman / Derek W Cain / Xiaozhi Lu / Sravani Venkatayogi / Madison Berry / Kshitij Wagh / Bette Korber / Kevin O Saunders / Ming Tian / Fred Alt / Kevin Wiehe / Priyamvada Acharya / S Munir Alam / Barton F Haynes /
PubMed AbstractVaccine development targeting rapidly evolving pathogens such as HIV-1 requires induction of broadly neutralizing antibodies (bnAbs) with conserved paratopes and mutations, and in some cases, the ...Vaccine development targeting rapidly evolving pathogens such as HIV-1 requires induction of broadly neutralizing antibodies (bnAbs) with conserved paratopes and mutations, and in some cases, the same Ig-heavy chains. The current trial-and-error search for immunogen modifications that improve selection for specific bnAb mutations is imprecise. Here, to precisely engineer bnAb boosting immunogens, we use molecular dynamics simulations to examine encounter states that form when antibodies collide with the HIV-1 Envelope (Env). By mapping how bnAbs use encounter states to find their bound states, we identify Env mutations predicted to select for specific antibody mutations in two HIV-1 bnAb B cell lineages. The Env mutations encode antibody affinity gains and select for desired antibody mutations in vivo. These results demonstrate proof-of-concept that Env immunogens can be designed to directly select for specific antibody mutations at residue-level precision by vaccination, thus demonstrating the feasibility of sequential bnAb-inducing HIV-1 vaccine design.
External linksNat Commun / PubMed:39489734 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 4.31 Å
Structure data

43225

8vgv

EMDB-43225, PDB-8vgv:
DH270.6 Fab bound to the HIV-1 CH848 DE3 SOSIP
Method: EM (single particle) / Resolution: 3.6 Å

43228

8vgw

EMDB-43228, PDB-8vgw:
VRC01 Fab bound to the HIV-1 CH848 DE3 SOSIP
Method: EM (single particle) / Resolution: 3.9 Å

43231

8vh1

EMDB-43231, PDB-8vh1:
CH235.12 Fab bound to the HIV-1 CH505.M5 SOSIP
Method: EM (single particle) / Resolution: 4.08 Å

43232

8vh2

EMDB-43232, PDB-8vh2:
CH235.12 Fab bound to the HIV-1 CH505.M5 SOSIP
Method: EM (single particle) / Resolution: 4.31 Å

43233

8vh3

EMDB-43233, PDB-8vh3:
CH505.M5.G458Y CE2 Design SOSIP
Method: EM (single particle) / Resolution: 3.9 Å

Source
  • human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Immunogen / Vaccine / Antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex

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