Soluble receptor-resistant poliovirus mutants identify surface and internal capsid residues that control interaction with the cell receptor.
Poliovirus initiates infection by binding to its cell receptor and undergoing a receptor-mediated conformational alteration. To identify capsid residues that control these interactions, we have isolated and characterized poliovirus mutants that are resistant to neutralization by a soluble form of the poliovirus receptor. Twenty one soluble receptor-resistant (srr) mutants were identified which still use the poliovirus receptor to infect cells. All but one srr mutant contain a single amino acid change at one of 13 different positions, either on the surface or in the interior of the virion. The results of binding and alteration assays demonstrate that both surface and internal capsid residues regulate attachment to the receptor and conformational change of the virus. Mutations that reduce alteration also affect receptor binding, suggesting a common structural basis for early events in poliovirus infection.
Colston
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Department of Microbiology, Columbia University College of Physicians & Surgeons, New York, NY 10032.
Racaniello
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VR
D002213:Capsid / Q000235:genetics / Q000378:metabolism*; D036022:Capsid Proteins; D003001:Cloning, Molecular; D006367:HeLa Cells; D006801:Humans; D008565:Membrane Proteins; D008958:Models, Molecular; D009154:Mutation; D017955:Poliovirus / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D011485:Protein Binding; D011991:Receptors, Virus / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012641:Selection, Genetic; D017422:Sequence Analysis, DNA; D012995:Solubility; D013329:Structure-Activity Relationship
D036022:Capsid Proteins; D008565:Membrane Proteins; D011991:Receptors, Virus; D011994:Recombinant Proteins; C442540:VP1 protein, Poliovirus; C442541:VP2 protein, Poliovirus; C442542:VP3 protein, Poliovirus; C066100:poliovirus receptor