In vitroProperties and Pathogenesis of A59/MHV4 Chimeric Mouse Hepatitis Viruses
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Early in infection, the mouse hepatitis virus (MHV) envelope glycoprotein spike (S) binds a cell surface receptor glycoprotein and is postulated to undergo a conformational change to reveal a hydrophobic domain, promoting the fusion of the viral envelope and the cell membrane. The actual steps of MHV entry and their effects on pathogenesis are largely unknown. By binding truncated S1 peptides to receptor glycoproteins blotted on membranes, the putative receptor binding domain (RBD) was mapped to the N-terminal 330 amino acids of S (Kubo et al., 1994). In this study, we have generated two groups of chimeric recombinant viruses in an isogenic background in order to study the role of the RBD in pathogenesis.