Highly purified radiolabeled mouse hepatitis virus (MHV) A59 contained
a previously overlooked protein which coelectrophoreses with the gene
5b product immunoprecipitated from infected cells. The gene 5b protei
n is post-translationally acylated. Rabbit antibody raised against a r
ecombinant gene 5b protein expressed in Escherichia coli neutralized v
iral infectivity in the presence of complement, although not in the ab
sence of complement. Immunofluorescent staining of MHV-infected cells
with two anti-peptide antibodies revealed that the gene 5b product is
membrane-associated and is transported to the cell surface, findings c
onsistent with the prediction of a membrane-spanning segment in the ge
ne 5b polypeptide. These results suggest strongly that the gene 5b pol
ypeptide represents a new MHV virion envelope protein which is homolog
ous to the TGEV ORF 4 and IBV 3c proteins. (C) 1994 Academic Press, In
c.