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A novel monoclonal antibody to N-myristoyl glycine moiety found a new N-myristoylated HIV-1 p28gag protein in HIV-1-infected cells.

作者信息

Furuishi K, Misumi S, Shoji S

机构信息

Department of Biochemistry, Faculty of Pharmaceutical Sciences, Kumamoto University, Japan.

出版信息

Biochem Biophys Res Commun. 1996 May 15;222(2):344-51. doi: 10.1006/bbrc.1996.0746.

Abstract

A novel monoclonal antibody was raised against a synthetic N-myristoyl glycine that is characteristic of all N-myristoylated proteins. The immunoreaction suppressed in the presence of hemocyanin as well as albumin conjugated with N-myristoyl glycine and other N-myristoyl glycyl peptides, while underivatized and myristoyl amino acid proteins or various fatty acids other myristic acid exerted no effect. The antibody specifically reacted with N-myristoylated pp60c-src in human colon adenocarcinoma cells, N-myristoylated pp60v-src in Rous sarcoma virus-infected cells, and N-myristoylated Gag precursor protein Pr55gag in HIV-1 producing cells. Furthermore, the antibody immunoreacted with a new N-myristoylated p28gag derived from HIV-1 gag protein. The antibody is shown to be a very useful tool for identification of N-myristoylated proteins.

摘要

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