Abstract
1 Institut für Medizinische Mikrobiologie und Hygiene, Abteilung Virologie, Haus 47, Universitätskliniken, 66421 Homburg/Saar
and2 Deutsches Krebsforschungszentrum, Institut für angewandte Tumorvirologie, Im Neuenheimer Feld 242, 69120 Heidelberg, Germany
The proteinase of the human endogenous retrovirus K (HERV-K) shows similarity to retrovirus aspartic proteinases. It is translated from a transcript composed of gag and prt. The proteinase was expressed either as full-length native protein or as truncated protein in Escherichia coli. Functional protein was demonstrated by its autocatalytic cleavage into an 18 kDa fragment recognized by a polyclonal antiserum. This autocatalytic cleavage was specifically inhibited by a human immunodeficiency virus type 1 proteinase inhibitor. The HERV-K proteinase expressed in E. coli was capable of cleaving HERV-K Gag translated in vitro. Major protein fragments of 39 and 30 kDa, and minor protein fragments of 26, 22 and 21 kDa were obtained. Similar fragments are also observed in the human teratocarcinoma cell line Teral. Our data suggest that the HERV-K proteinase is functionally equivalent to other retrovirus proteinases and thus probably functions in the processing of Gag precursor protein.