Abstract
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.
MeSH Terms
Adsorption
Amino Acids/metabolism
Buffers
Carbon Radioisotopes
Electrophoresis, Polyacrylamide Gel
Enterovirus/drug effects,growth & development,metabolism
HeLa Cells
Humans
Hypotonic Solutions
Peptides/metabolism
Poliovirus/drug effects,growth & development
Temperature
Tritium
Uridine/metabolism
Viral Plaque Assay
Viral Proteins/metabolism
Chemicals
Amino Acids
Buffers
Carbon Radioisotopes
Hypotonic Solutions
Peptides
Viral Proteins
Tritium
Uridine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Cords C E
James C G
McLaren L C
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