Gokul Raghunath
Emory University, GA·Biophysics
HIV-1 leaves an infected cell as a harmless, immature particle. It only becomes infectious after an enzyme snips its large Gag polyprotein into smaller pieces that rearrange into the virus's inner architecture.
- Fields
Biophysics
Microbiology & Immunology
Biochemistry
- Topics
spacer peptide 2
matrix protein
Gag polyprotein
- Grants
- 1 known grant, through May 2028
What they work on
- Test how specific amino acids in synthetic spacer peptide 2 (SP2), a short conserved HIV-1 peptide, control its binding to the viral matrix protein and its remodeling of lipid membranes, using fluorescence imaging and biophysical assays on liposomes.
- Measure whether SP2 alone or in complex with purified matrix protein increases lipid order and membrane tension in synthetic and plasma-membrane-derived liposomes, the properties the lab's pilot data link to SP2 binding.
- Determine how the presence or absence of SP2 in Gag polyprotein variants changes the lipid order and membrane tension of intact HIV-1 particles.
- Correlate viral membrane properties with fusion activity across virus panels using a real-time split NanoLuc assay, a luminescent reporter that signals the instant viral and cell membranes merge.
More about the research
One of those pieces, a short conserved stretch called spacer peptide 2 (SP2), has long been dismissed as leftover filler with no job of its own. This project asks whether SP2 actually helps the virus fuse with a target cell's membrane, the first committed step of infection.
Why it matters
HIV-1 must fuse with a host cell membrane to infect it, and drugs that block this step are clinically valuable. By clarifying whether a short, conserved viral peptide tunes the stiffness and ordering of the viral membrane to permit fusion, this work could identify a previously overlooked target for antiviral strategies against a conserved part of the virus that is less likely to vary between strains.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Yongli Zhang
Yale University, CT·Biophysics
Reconstitute the full primed SNARE complex, adding complexin and the calcium sensor synaptotagmin-1 to Munc18-1, syntaxin-1, VAMP2 and Munc13-1, and characterize its stability, structure and dynamics on membranes.
Thomas Gallagher
Loyola University Chicago, IL·Microbiology & Immunology
Determine how mutations in the S2 fusion segment of the SARS-CoV-2 spike control the receptor-binding domain and its engagement with receptors, identifying specific variant substitutions that alter receptor reactivity and spike stability.
Stefan Oliver
Stanford University, CA·Biophysics
Determine the near-atomic structure of the varicella-zoster virus gB/gH-gL complex, the machinery that fuses viral and cell membranes, using single-particle cryo-electron microscopy on complexes kept in their native lipid environment.
The school
Emory University: 70 labs on PI Pages, $1.2B a year on research, 286 research doctorates a year.
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