A secretable serine proteinase with highly restricted specificity from cytolytic T lymphocytes inactivates retrovirus‐associated reverse transcriptase

FEBS Letters

Kramer, Michael D.¹  Fruth, Ulli²  Simon, Hans-Georg²  Simon, Markus M.² 

[1] Onkologisches Labor der Universitätsklinik, Im Neuenheimer Feld, D-6900 Heidelberg, FRG;Max-Planck-Institut für Immunbiologie, Stübeweg 51, D-7800 Freiburg FRG

关键词: Serine proteinase;    Reverse transcriptase;    Virus replication;    (Cytolytic T cell);    TSP-1;    T cell specific proteinase-1;    CTL;    cytolytic T lymphocyte;    TH;    T helper cells;    CTLL;    CTL line;    THL;    TH line;    IFNγ;    interferon-γ;    MoMuLV;    Moloney murine leukemia virus;    RT;    reverse transcriptase;    RTMoMuLV;    reverse transcriptase from MoMuLV;    PMSF;    phenylmethylsulfonyl fluoride;    PFR-CK;    H-D-Pro-Phe-Arg-chloromethylketone;    PFR-NA;    PFR-nitroanilide;   

DOI  :  10.1016/0014-5793(87)80318-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

TSP-1, a murine T cell specific proteinase, is expressed in cytolytic T lymphocytes and secreted upon their interaction with antigen bearing target cells. In searching for possible extracellular substrates of the enzyme in the physiological environment of cytolytic effector cells, we have investigated the proteolytic activity of TSP-1 on retroviral proteins. It is shown that reverse transcriptase derived from the retrovirus Moloney murine leukemia virus is inactivated by TSP-1 via limited proteolysis. The data suggest the possibility that cytolytic T lymphocytes are able to interfere with retroviral replication by secreting a serine proteinase which degrades viral proteins.

【 授权许可】

Unknown