Moesin, and not the murine functional homologue (Crry/p65) of human membrane cofactor protein (CD46), is involved in the entry of measles virus (strain Edmonston) into susceptible murine cell lines.

Membrane cofactor protein (CD46) has been firmly established as the major high affinity receptor for measles virus (MV). In addition, another protein, moesin, has been shown to be linked with the susceptibility of human cells to MV infection. Murine cells are largely resistant to MV infection, although a number of cell types can be productively infected. As murine cells do not express CD46 an additional mechanism for the uptake of MV is likely. Murine cells possess a functional homologue of CD46 (Crry/p65) in addition to murine moesin, which has nucleotide and amino acid homology to human moesin. We report that anti-moesin monoclonal antibodies 119 and 38/87 reduce the number of infectious centres attributed to MV in murine cell lines NS20Y and L929, whereas polyclonal antisera specific for Crry/p65 and CD46 had no effect on MV infection of these cells. We suggest that moesin may be important in the non-CD46-mediated uptake of MV strain Edmonston by susceptible murine cell lines.