Specific alterations of coxsackievirus B3 eluted from HeLa cells.

After the attachment of radioactive coxsackievirus B3 to HeLa cells at 0 C and subsequent incubation at 37 C, 50 to 80% of attached virus radioactivity was eluted from the cells within 1 hr. Eluted virus had a buoyant density of 1.21 in a potassium tartrate gradient, sedimented more slowly than native virus in sucrose gradients, was resistant to ribonuclease, was unstable in CsCl centrifugation, and did not reattach to uninfected cells. Electrophoretic studies of sodium dodecyl sulfate-disrupted B3 virus in sodium dodecyl sulfate-polyacrylamide gels revealed four radioactive virus polypeptides (VP 1 to 4), of which the three largest migrated slightly faster than their poliovirus T1 counterparts. In contrast, electrophoretic analysis of eluted virus, after banding in a tartrate gradient or pelleting by centrifugation, showed the absence of the fastest migrating polypeptide, VP 4. VP 4 was recovered in the supernatant fluid when the eluted virions were removed by high-speed centrifugation. The results indicate that VP 4 is located at the surface of the native virion, and its dissociation from the capsid may represent the first specific alteration of the virion after virus-receptor interaction at the cell surface.