Transglutaminase covalently incorporates amines into human immunodeficiency virus envelope glycoprotein gp120 in vitro.

Abstract

Human immunodeficiency virus envelope glycoprotein gp120, but not its precursor gp160, covalently incorporates both spermidine and glycine ethyl ester in the presence of Ca2+ and transglutaminase purified from guinea pig liver. The examined ability to act as enzyme substrate of various glutamine-containing gp120 fragments, including the principal neutralizing determinant, the CD4 binding domain, and the sequence 254-274, suggested to be involved in post-binding events and in virus entry in the host cell, indicated the glutamine-265 as possible reactive acyl donor site of the protein.