Role of serine proteases in human T4+ lymphocytes in the process of HIV-1 infection.
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概要
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Cellular proteases in human T4<SUP>+</SUP> lymphocytes play important roles in membrane fusion and internalization of HIV-1 and in virus replication. We observed a novel membrane-bound serine protease, named tryptase TL<SUB>2</SUB>, in human T4<SUP>+</SUP> lymphocytes, which specifically binds to the V 3 domain of HIV-1 gp 120. The V 3 domain of HIV-1, containing the central motif-GPGR-sequence that is homologous to the active site Kunitz-type inhibitors, is conserved in almost all HIV-1 isolates. Neutralizing antibody against the V 3 domain of HTLV-III<SUB>B</SUB>, inhibitors of tryptase TL<SUB>2</SUB> with a-GPCR-sequence in their reactive site and synthetic peptides corresponding to the sequ-ences of the V 3 domains of various HIV-1 strains inhibited the binding of HIV-1 gp 120 to tryptase TL<SUB>2</SUB> and also inhibited syncytia formation induced by HIV-1. These findings suggest that tryptase TL<SUB>2</SUB> binds to gp 120 intracting with the V 3 domain.<BR>Signal peptidase and HIV-1 envelope precursor processing protease in Golgi apparatus are required for HIV-1 replication. We purified the HIV-1 envelope precursor processing enzyme from Golgi apparatus of human T 4<SUP>+</SUP> lymphocytes. The enzyme had a molecular mass of 25 kDa and converted gp 160 to gp 120 and gp 41 without any further processing, with high efficiency at a pH optimum of 6.5-7.0.
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