Ian Wilson
Weill Medical College of Cornell University, NY·Microbiology & Immunology
A vaccine against HIV has to solve an unusual problem. The antibodies that can neutralize many different strains of the virus, called broadly neutralizing antibodies, are rare, and the immune system only makes them after a long series of mutations.
- Fields
Microbiology & Immunology
Biochemistry
Biophysics
- Topics
broadly neutralizing antibodies
bNAb
germline targeting
- Grants
- 1 known grant, through Apr 2031
What they work on
- Determine how GT1.1-primed antibodies against the CD4 binding site, the pocket HIV uses to grip host cells, recognize shaping and polishing immunogens, using X-ray crystallography, electron microscopy and biophysical analysis of responses from mice, non-human primates and human trial participants.
- Explain why priming of antibodies to the apex at the top of the HIV envelope trimer is inconsistent, by mapping polyclonal and monoclonal reactivity with electron microscopy polyclonal epitope mapping, B cell receptor repertoire analysis and surface plasmon resonance.
- Solve high-resolution structures of inferred germline antibody precursors bound to GT1.1 immunogens by cryo-electron microscopy and X-ray crystallography, to reveal the molecular basis of precursor recognition at the apex epitope.
- Structurally characterize combination immunogens that target the CD4 binding site, the V2 apex and a third cluster including the fusion peptide and V3-N332, using alternative and AI-generated trimer scaffolds, and quantify on- and off-target responses to down-select candidates for clinical trials.
More about the research
Germline-targeting vaccine design addresses this by building a sequence of engineered proteins: a first shot that engages the rare naive B cells carrying the right starting receptor, followed by shots that shape and polish the response toward breadth. The engineered proteins used here are SOSIP trimers, stabilized versions of the three-part envelope spike that HIV uses to enter cells. Making this strategy work depends on knowing, in atomic detail, exactly how each immunogen is recognized.
Why it matters
An HIV vaccine remains out of reach largely because the antibodies capable of blocking diverse viral strains are hard to elicit. Detailed structures of how engineered spike proteins engage the rare precursor B cells that can mature into such antibodies could sharpen the sequence of immunogens used in vaccination and help select which candidates advance to human trials, a step toward a vaccine that would benefit populations at risk of HIV infection worldwide.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Ashley Nelson
Weill Medical College of Cornell University, NY·Microbiology & Immunology
Compare giving germline-targeting HIV envelope immunogens one after another versus all at once for waking up precursor B cells of two broadly neutralizing antibody classes: those binding the CD4 binding site and those binding the V2 apex of the viral spike.
David Veesler
University of Washington, WA·Microbiology & Immunology
Characterize how broadly serum antibodies from nonhuman primates immunized with nanoparticle vaccines co-displaying multiple receptor-binding-domain and spike antigens bind and neutralize betacoronaviruses.
Justin Bailey
Johns Hopkins University, MD·Microbiology & Immunology
Test whether a dengue vaccine's serotype composition determines the balance, neutralizing potency, and durability of serotype-specific versus cross-reactive memory B cells and monoclonal antibodies, and whether those responses predict protection after controlled human challenge with serotype 2.
The school
Weill Medical College of Cornell University: 35 labs on PI Pages, $1.6B a year on research, 59 research doctorates a year.
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