A NOVEL MONOCLONAL-ANTIBODY TO N-MYRISTOYL GLYCINE MOIETY FOUND A NEWN-MYRISTOYLATED HIV-1 P28(GAG) PROTEIN IN HIV-1-INFECTED CELLS

Citation
K. Furuishi et al., A NOVEL MONOCLONAL-ANTIBODY TO N-MYRISTOYL GLYCINE MOIETY FOUND A NEWN-MYRISTOYLATED HIV-1 P28(GAG) PROTEIN IN HIV-1-INFECTED CELLS, Biochemical and biophysical research communications, 222(2), 1996, pp. 344-351
Citations number
30
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
222
Issue
2
Year of publication
1996
Pages
344 - 351
Database
ISI
SICI code
0006-291X(1996)222:2<344:ANMTNG>2.0.ZU;2-4
Abstract
A novel monoclonal antibody was raised against a synthetic N-myristoyl glycine that is characteristic of all N-myristoylated proteins. The i mmunoreaction suppressed in the presence of hemocyanin as well as albu min conjugated with N-myristoyl glycine and other N-myristoyl glycyl p eptides, while underivatized and myristoyl amino acid proteins or vari ous fatty acids other than myristic acid exerted no effect. The antibo dy specifically reacted with N-myristoylated pp60(c-src) in human colo n adenocarcinoma cells, N-myristoylated pp60(v-src) in Rous sarcoma vi rus-infected cells, and N-myristoylated Gag precursor protein Pr55(gag ) in HIV-1-producing cells. Furthermore, the antibody immunoreacted wi th a new N-myristoylated p28(gag) derived from HIV-1 gag protein. The antibody is shown to be a very useful tool for identification of N-myr istoylated proteins. (C) 1996 Academic Press, Inc.