Characterization of human rhinoviruses displaced by an anti-receptor monoclonal antibody.
The attachment of rhinoviruses to cellular receptors was studied by displacing bound virus particles with an anti-receptor monoclonal antibody. The two serotypes studied differed significantly with respect to the temperature dependence of displacement and the nature of the particles displaced. Binding was shown to be a two-step process, the first of which is reversible and is seen when viruses are bound either to isolated cell membranes or to cells at lower than physiological temperatures. Second-stage binding was seen with serotype 14 when bound to intact cells. Viral particles released from such cells by incubation at 37 degrees C or by anti-receptor antibody exhibited altered physical changes in the capsid and a loss of infectivity. In contrast, serotype 67 bound efficiently to cells at 37 degrees C and did not elute spontaneously but could be displaced by anti-receptor antibody to produce complete, infectious particles. Rhinoviruses labeled with [3H]myristic acid or with [35S]methionine were displaced similarly from cells or membranes by anti-receptor antibody, indicating that the majority of VP4 of rhinoviruses does not enter or remain attached to cells during either the first or second stage of virus binding. These data support the conclusion that the myristic acid moiety of VP4 is not involved in the initial viral interaction with cellular receptors.
Abraham
G
G
Department of Virus and Cell Biology, Merck Sharp and Dohme Research Laboratories, West Point, Pennsylvania 19486.
Colonno
R J
RJ
D000911:Antibodies, Monoclonal / Q000276:immunology*; D001667:Binding, Competitive; D002213:Capsid / Q000378:metabolism; D006367:HeLa Cells / Q000378:metabolism; D006801:Humans; D011991:Receptors, Virus / Q000276:immunology / Q000378:metabolism*; D012229:Rhinovirus / Q000145:classification / Q000378:metabolism*; D013696:Temperature
D000911:Antibodies, Monoclonal; D011991:Receptors, Virus