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Extended nucleocapsid protein is cleaved from the Gag–Pol precursor of human immunodeficiency virus type 1

Experimental Pathology Unit¹ and Clinical Virology Unit², The Hebrew University, Hadassah Medical School, PO Box 12272, Jerusalem 91120, Israel
National Public Health Laboratories, Ministry of Health, Israel³

Author for correspondence: Moshe Kotler. Fax +972 2 6758190. e-mail MKOTLER{at}cc.huji.ac.il

Human immunodeficiency virus type 1 Gag and Gag–Pol precursors are translated from an mRNA which is indistinguishable from the full-length genomic RNA. The ratio of Gag to Gag–Pol polyproteins is approximately 20:1 and is controlled by a frameshift of the reading frame, which takes place downstream of the p7 nucleocapsid (NC) in the N terminus of the p1 peptide. The viral precursors Gag and Gag–Pol are cleaved by the virus-encoded protease (PR) into the structural proteins, and into p6^Pol, PR, reverse transcriptase and integrase. Due to the frameshift event, the cleavage site at the C terminus of NC coded in the Gag frame (ERQAN-FLGKI) changes either to ERQANFLRED or ERQANFFRED. The results presented in this report demonstrate that the NC released from the Gag–Pol precursor is 8 amino acid residues longer than the NC cleaved from the Gag polyprotein. Our results also show that truncated Gag–Pol precursors bearing cleavage site mutation at the NC/p6^Pol, and/or p6^Pol/PR junctions, undergo autoprocessing in bacterial and eukaryotic cells, indicating that PR is active when part of the precursor.

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