Alteration of capsid proteins of coxsackievirus A13 by low ionic concentrations.
Several group A coxsackieviruses (A13, 15, 18, and 21), but not polioviruses or group B coxsackieviruses, are rapidly inactivated in low ionic strength solutions at neutral pH. The extent of inactivation is dependent upon temperature and molarity. Virions inactivated in this manner contain a normal complement of infectious RNA which remains in a state resistant to the action of ribonuclease. However, more than 95% of the virus particles are unable to attach to susceptible cells. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis reveals that coxsackievirus A13 virions contain five structural polypeptides (VP1, VP2a, VP2b, VP3, and VP4). Electrophoretic analysis indicates that inactivation of coxsackievirus A13 in low ionic strength solutions is due to the specific loss of the smallest polypeptide VP4 from the virus particle. These results suggest that adsorption of coxsackievirus A13 to receptors on susceptible cells is dependent upon the presence of the capsid protein VP4.
D000327:Adsorption; D000596:Amino Acids / Q000378:metabolism; D002021:Buffers; D002250:Carbon Radioisotopes; D004591:Electrophoresis, Polyacrylamide Gel; D004770:Enterovirus / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D007038:Hypotonic Solutions; D010455:Peptides / Q000378:metabolism; D017955:Poliovirus / Q000187:drug effects / Q000254:growth & development; D013696:Temperature; D014316:Tritium; D014529:Uridine / Q000378:metabolism; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000378:metabolism*
D000596:Amino Acids; D002021:Buffers; D002250:Carbon Radioisotopes; D007038:Hypotonic Solutions; D010455:Peptides; D014764:Viral Proteins; D014316:Tritium; D014529:Uridine