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SUMMARY:NMR and Biophysical Studies of Viral Fusion Peptides and Proteins
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20241204T160000
UID:2026-04-30-06-27-48@natsci.colostate.edu
DTSTAMP:20260430T062748
Description:About the Seminar:\n\nMany viruses that cause human disease are
  enveloped by a membrane obtained during budding from an infected host cel
 l. Example virus families are HIV\, influenza\, and coronaviruses. Infecti
 on of new cells requires joining (“fusion”) of viral and cellular memb
 ranes. Fusion is catalyzed by glycoprotein subunits that are part of the s
 pikes that protrude from the virus. Although subunits from different virus
  families share a common fusion function\, they not have similar amino aci
 d sequences. A major goal of the Weliky group is understanding how these s
 ubunits catalyze fusion. This new understanding should aid development of 
 anti-viral therapeutics and universal vaccines. NMR is an important techni
 que for this understanding\, in particular for determining structures and 
 motions of fusion subunit and lipid molecules in membranes. One way a fusi
 on subunit may catalyze fusion is by inducing lipid motions along the fusi
 on pathway. For example\, lipid protrusion out of the membrane accelerates
  joining of outer leaflets of the viral and cellular membranes which is an
  initial step in fusion. We showed by NMR that protrusion probability is i
 ncreased ~10 for lipids next to the fusion peptide (Fp) segment of the 
 influenza fusion subunit. One fairly-unexplored strength of solid-state NM
 R is determination of populations of distinct molecular structures when th
 e chemical shifts of the different structures are unresolved. We have done
  such determination for intermolecular registries (alignments) of adjacent
  molecules in antiparallel beta sheets of the membrane-bound Fp of the HIV
  fusion subunit. Global analysis of the NMR data reveals &gt\;10 populated
  registries which to our knowledge is unprecedented in molecular structure
 . HIV is a chronic infection in which the virus evades the immune system b
 y mutation while continuing to fuse with and infect cells. A broad distrib
 ution of Fp beta sheet registries\, many of which are fusion-active\, is a
 n evolutionary solution. Viruses with Fp mutations remain viable in fusion
  because the mutations only result in shifts in populations among differen
 t functional registries.\n\nAbout the Speaker:\nDavid Weliky grew up for t
 he most part in New Jersey and received a B.A. with High Honors in Chemist
 ry and Physics from Swarthmore College. David worked at Aerospace Corporat
 ion and subsequently received a Ph.D. in Chemistry from University of Chic
 ago working with Takeshi Oka and doing research on infrared spectroscopy o
 f deuterium impurity molecules in crystalline molecular hydrogen solid. At
  Chicago\, David was a NSF Pre-doctoral Fellow and an AT&amp\;T Ph.D. Scho
 lar and did research for a summer with Rob Tycko at AT&amp\;T. David then 
 worked as a post-doc with Rob at NIH and developed solid-state NMR methods
  to determine molecular structure and also determined the secondary struct
 ure of a peptide epitope bound to a neutralizing antibody. David’s indep
 endent career has been at Michigan State University where he is currently 
 a Professor of Chemistry. David’s research has focused on fusion subunit
 s of spike proteins of enveloped viruses\, recombinant proteins in bacteri
 al inclusion bodies\, and high-temperature NMR of phosphochalcogenides. 4:
 00 pm
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