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J. Biochem, 2004, Vol. 135, No. 3 447-453
© 2004 The Japanese Biochemical Society

BIOCHEMISTRY

Blocking of Human Immunodeficiency Virus Type-1 Virion Autolysis by Autologous p2gag Peptide

Shogo Misumi, Yukimi Morikawa, Mitsunori Tomonaga, Kouichi Ohkuma, Nobutoki Takamune and Shozo Shoji*

Department of Biochemistry, Faculty of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Kumamoto 862-0973, Japan

Our previous study suggested that the p2gag peptide, AEAMSQVTNTATIM, inhibits human immunodeficiency virus type 1 (HIV-1) protease (PR) activity in vitro. In this study, Ala substitutions (Met4Ala and Thr8Ala) and deletion of amino acid Asn9 within the nona p2gag peptide (AEAMSQVTN) were found to decrease the inhibitory effect on HIV-1 PR activity. Furthermore, treatment of PMA-activated latently infected T lymphocytes, ACH-2 cells, with the p2gag peptide (100 and 250 µM) resulted in a decrease in the amount of p24gag in the resultant viral lysates derived from the cell-free supernatant. In addition, the HIV-1-Tat-p2gag fusion peptide was synthesized to effectively deliver the p2gag peptide into the cells. The fusion peptide was incorporated into chronically infected T lymphocytes, CEM/LAV-1 cells, as detected on indirect immunofluorescence analysis using anti-p2gag peptide monoclonal antibodies, which recognize the nona peptide (AEAMSQVTN) derived from the N-terminus of the p2gag peptide, and cleaved by HIV-1 PR in vitro. Treatment of CEM/LAV-1 cells with the fusion peptide also resulted in a decrease in the amount of p24gag in the resultant viral lysate derived from the cell-free supernatant. Taken together, these data suggest that the p2gag peptide consequently blocks the autolysis of HIV-1 virions for the conservation of viral species.

* To whom correspondence should be addressed: Tel: +81-96-371-4362, Fax: +81-96-362-7800; E-mail: shoji{at}gpo.kumamoto-u.ac.jp


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