Measles virus and C3 binding sites are distinct on membrane cofactor protein (CD46).

@article{Manchester1995MeaslesVA,
  title={Measles virus and C3 binding sites are distinct on membrane cofactor protein (CD46).},
  author={Marianne Manchester and Alexandra Valsamakis and Richard A. Kaufman and M Kathryn Liszewski and Jos{\'e} Alvarez and John P Atkinson and Douglas M. Lublin and Michael B A Oldstone},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 6},
  pages={
          2303-7
        }
}
The human complement regulatory protein membrane cofactor protein (CD46) is the cellular receptor for measles virus (MV), whereas decay accelerating factor (DAF; CD55), a structurally similar complement regulatory protein, does not bind MV. To characterize the interaction between MV and CD46, mutants of the CD46 protein and hybrid molecules between CD46 and DAF were tested for their ability to act as MV receptors. The transmembrane domain and cytoplasmic tail of CD46 were not required for… CONTINUE READING

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Interaction of CD46 with measles virus: accessory role of CD46 short consensus repeat IV.

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