MHVR-independent cell-cell spread of mouse hepatitis virus infection requires neutral pH fusion

Adv Exp Med Biol. 1995:380:351-7. doi: 10.1007/978-1-4615-1899-0_57.

Abstract

Receptor-specificity is a key determinant of viral tropism. In this report, however, we have demonstrated that cell-associated spread of MHV can bypass the requirement for binding to primary receptors and thereby spread to cells that are resistant to MHV infection. Anti-receptor antibody CC1, which blocks infection by MHV virions, failed to prevent cell-associated spread of MHV to receptor-negative BHK cells or receptor-positive DBT cells. Cell-associated MHV may be utilizing an alternative, low-affinity receptor that is inadequate for functional interaction with MHV virions. Theoretically, dissemination of MHV infection through a receptor-independent, cell-associated mechanism in vivo provides the potential for broader host and tissue range, and for spread of infection despite the presence neutralizing antibodies. Receptor-independent, cell-associated spread of MHV requires neutral pH fusion capability. The low pH-dependent MHV variant OBLV60, which utilizes an endocytic route of entry, does not spread through a receptor-independent mechanism. Additionally, antiviral antibodies that block MHV spike-mediated fusion inhibited cell-associated spread of infection.

Publication types

  • Review

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • Carcinoembryonic Antigen / genetics
  • Carcinoembryonic Antigen / physiology
  • Cell Adhesion Molecules
  • Cell Fusion*
  • Cell Line
  • Chloroquine / pharmacology
  • Glycoproteins / physiology
  • Hydrogen-Ion Concentration
  • Lysosomes / drug effects
  • Lysosomes / virology
  • Mice
  • Monensin / pharmacology
  • Murine hepatitis virus / drug effects
  • Murine hepatitis virus / pathogenicity*
  • Murine hepatitis virus / physiology*

Substances

  • Antibodies, Monoclonal
  • Carcinoembryonic Antigen
  • Ceacam2 protein, mouse
  • Cell Adhesion Molecules
  • Glycoproteins
  • Chloroquine
  • Monensin