Clinical coxsackievirus B isolates differ from laboratory strains in their interaction with two cell surface receptors.
Coxsackie B viruses interact with two putative cell surface receptor molecules. Experiments with prototype laboratory strains suggest that all 6 coxsackie B serotypes interact with a 46-kDa protein recognized by the monoclonal antibody RmcB, whereas CB1, CB3, and CB5 may also bind to decay accelerating factor. Antireceptor monoclonal antibodies were used to study interactions between low-passage clinical coxsackie B virus isolates and the two receptors. In contrast to observations made with single prototype strains, these data indicate that receptor use by clinical isolates is not strictly related to serotype and that even prototype strains with different passage histories may differ in receptor use. Within a given serotype, variation exists in the capacity of individual virus isolates to bind to specific receptors, and variants with altered receptor specificity may arise during infection in humans and in tissue culture.
Bergelson
J M
JM
Laboratory of Infectious Diseases, Dana-Farber Cancer Institute, Boston, Massachusetts, USA.
Modlin
J F
JF
Wieland-Alter
W
W
Cunningham
J A
JA
Crowell
R L
RL
Finberg
R W
RW
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral / Q000276:immunology; D018958:CD55 Antigens / Q000378:metabolism; D003384:Coxsackievirus Infections / Q000382:microbiology*; D029822:Enterovirus B, Human / Q000378:metabolism / Q000472:pathogenicity*; D006367:HeLa Cells; D006801:Humans; D011991:Receptors, Virus / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D000914:Antibodies, Viral; D018958:CD55 Antigens; D011991:Receptors, Virus