Interaction of the capsid protein p24 (HIV-1) with sequence-derived peptides: Influence on p24 dimerization

Citation
K. Hilpert et al., Interaction of the capsid protein p24 (HIV-1) with sequence-derived peptides: Influence on p24 dimerization, VIROLOGY, 254(1), 1999, pp. 6-10
Citations number
18
Categorie Soggetti
Microbiology
Journal title
VIROLOGY
ISSN journal
00426822 → ACNP
Volume
254
Issue
1
Year of publication
1999
Pages
6 - 10
Database
ISI
SICI code
0042-6822(19990201)254:1<6:IOTCPP>2.0.ZU;2-E
Abstract
Protein-protein interactions of the p24 (HIV-1) capsid protein play an esse ntial role in the production of infectious virus particles. To map the puta tive p24 dimerization site, a set of overlapping peptides spanning the p24 sequence was prepared using spot synthesis on a cellulose membrane and prob ed with recombinant p24 (rp24). Three sequence regions interacting with rp2 4 were Identified. Peptides from each region were synthesized, but only one peptide was effectively able to inhibit rp24 dimerization in solution. Ami no acids that were exposed in the corresponding p24 region were mutated in rp24, resulting in a significant decrease of rp24 dimerization. Thus, parti cipation of this region in virus capsid assembly can be assumed. (C) 1999 A cademic Press.