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In vitroProperties and Pathogenesis of A59/MHV4 Chimeric Mouse Hepatitis Viruses

  • Jean C. Tsai
  • Susan R. Weiss
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 494)

Abstract

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.

Keywords

Recombinant Virus Virus Entry Receptor Binding Domain Mouse Hepatitis Virus Receptor Glycoprotein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

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Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Jean C. Tsai
    • 1
  • Susan R. Weiss
    • 1
  1. 1.Department of MicrobiologyUniversity of Pennsylvania School of MedicinePhiladelphiaUSA

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