MOESIN, AND NOT THE MURINE FUNCTIONAL HOMOLOG (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 ma jor high afinity 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 infe cted. As murine cells do not express CD46 an additional mechanism for the uptake of MV is likely. Murine cells possess a functional homologu e of CD46 (Crry/p65) in addition to murine moesin, which has nucleotid e and amino acid homology to human moesin. We report that anti-moesin monoclonal antibodies 119 and 38/87 reduce the number of infectious ce ntres attributed to MV in murine cell lines NS20Y and L929, whereas po lyclonal antisera specific for Crry/p65 and CD46 had no effect on MV i nfection of these cells. We suggest that moesin may be important in th e non-CD46-mediated uptake of MV strain Edmonston by susceptible murin e cell lines.