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Author

Kang, Sebyung
Protein Nanobio Lab
Research Interests
  • Protein engineering, Drug/diagnostics delivery nanoplatform, Protein-base vaccine delivery systems, Biosensor & imaging

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Hydrogen/Deuterium Exchange Analysis of HIV-1 Capsid Assembly and Maturation

Cited 0 times inthomson ciCited 17 times inthomson ci
Title
Hydrogen/Deuterium Exchange Analysis of HIV-1 Capsid Assembly and Maturation
Author
Monroe, Eric B.Kang, SebyungKyere, Sampson K.Li, RuiPrevelige, Peter E., Jr.
Keywords
C-TERMINAL DOMAIN; ELECTRON CRYOTOMOGRAPHY; DIMERIZATION DOMAIN; GAG POLYPROTEIN; COAT PROTEIN; IN-VITRO; INHIBITOR; REVEALS; VIRIONS; BACTERIOPHAGE-P22
Issue Date
201011
Publisher
CELL PRESS
Citation
STRUCTURE, v.18, no.11, pp.1483 - 1491
Abstract
Following budding, HIV-1 virions undergo a maturation process where the Gag polyprotein in the immature virus is cleaved by the viral protease and rearranges to form the mature infectious virion. Despite the wealth of structures of isolated capsid domains and an in vitro-assembled mature lattice, models of the immature lattice do not provide an unambiguous model of capsid-molecule orientation and no structural information is available for the capsid maturation pathway. Here we have applied hydrogen/deuterium exchange mass spectrometry to immature, mature, and mutant Gag particles (CA5) blocked at the final Gag cleavage event to examine the molecular basis of capsid assembly and maturation. Capsid packing arrangements were very similar for all virions, whereas immature and CA5 virions contained an additional intermolecular interaction at the hexameric, 3-fold axis. Additionally, the N-terminal beta-hairpin was observed to form as a result of capsid-SP1 cleavage rather than driving maturation as previously postulated.
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DOI
http://dx.doi.org/10.1016/j.str.2010.08.016
ISSN
0969-2126
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