Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein.

@article{Rein1994FunctionOT,
  title={Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein.},
  author={Alan Rein and Jane Mirro and Janine G. Haynes and Sjef M.P.G. Ernst and Kunio Nagashima},
  journal={Journal of virology},
  year={1994},
  volume={68 3},
  pages={
          1773-81
        }
}
In the murine leukemia viruses (MuLVs), the Env complex is initially cleaved by a cellular protease into gp70SU and pre15ETM. After the virus particle is released from the cell, the C-terminal 16 residues are removed from the cytoplasmic domain of pre15E by the viral protease, yielding the mature p15ETM and p2E. We have investigated the function of this cleavage by generating a Moloney MuLV mutant, termed p2E-, in which the Env coding region terminates at the cleavage site. This mutant… CONTINUE READING

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