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J. Biochem, 1988, Vol. 103, No. 5 747-749
© 1988 Japanese Biochemical Society

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Antimyristoylation of gag Proteins in Human T-Cell Leukemia and Human Immunodeficiency Viruses with N-Myristoyl Glycinal Diethylacetal1

Shozo Shoji, Faculty of Pharmaceutical Sciences, Akira Tashiro, Faculty of Pharmaceutical Sciences and Yukiho Kubota, Faculty of Pharmaceutical Sciences

Department of Biochemistry,Kumamoto University Kumamoto, Kumamoto 862

N-Myristoyl (N-Myr-) glycinal (aminoacetoaldehyde, GO) diethylacetal (A), which is abbreviated as N-Myr-GOA, and other N-Myr-compounds (N-Myr-Gly-GOA, N-Myr-Gly-Gly-GOA, and N-Myr-Gly-Gly-Gly-GOA) were newly synthesized and then employed for NH2 -terminal antimyristoylation of structure proteins in the human T-cell leukemia virus (HTLV-I) and the human immunodeficiency virus (HIV). The protein myristoylation of structure proteins pl9gag, of HTLV-I, and pl7gag, of HIV, was determined separately, using radiolabeled myristic acid, in vitro. The radiolabeled proteins, after immunoprecipitation with an antiserum to adult T-cell leukemia (ATL) or the anti-pl7gag monoclonal antibody of HIV, were identified as pl9gag of HTLV-I and pl7gag of HIV by fluorography after SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The protein myristoylation was resistant to NH2 OH-treatment. Of the N-Myr-compounds tested, N-Myr-GOA remarkably prevented the myristoylation of pl9gag and pl7gag, but N-Myr-Gly-Gly-GOA and N-Myr-Gly-Gly-Gly-GOA did not.

1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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