Murine coronavirus with an extended host range uses heparan sulfate as an entry receptor.
Only a relatively few mutations in its spike protein allow the murine coronavirus to switch from a murine-restricted tropism to an extended host range by being passaged in vitro. One such virus that we studied had acquired two putative heparan sulfate-binding sites while preserving another site in the furin-cleavage motif. The adaptation of the virus through the use of heparan sulfate as an attachment/entry receptor was demonstrated by increased heparin binding as well as by inhibition of infection through treatment of cells and the virus with heparinase and heparin, respectively.
de Haan
Cornelis A M
CA
Virology Division, Department of Infectious Diseases and Immunology, Yalelaan 1, 3584CL Utrecht, The Netherlands. x.haan@vet.uu.nl
Li
Zhen
Z
te Lintelo
Eddie
E
Bosch
Berend Jan
BJ
Haijema
Bert Jan
BJ
Rottier
Peter J M
PJ
D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D016384:Consensus Sequence; D017934:Coronavirus / Q000502:physiology*; D006367:HeLa Cells; D006497:Heparan Sulfate / Q000502:physiology*; D006801:Humans; D051379:Mice; D000085064:Receptors, Coronavirus; D011991:Receptors, Virus / Q000502:physiology*
D006497:Heparan Sulfate; D000085064:Receptors, Coronavirus; D011991:Receptors, Virus