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PMID: 1654440 Published · ppublish English Journal Article

An assembly defect as a result of an attenuating mutation in the capsid proteins of the poliovirus type 3 vaccine strain.

Journal of virology ·Vol. 65 ·No. 10 ·1991-10-00 ·Pages 5225-31

Macadam AJ, Ferguson G, Arnold C, Minor PD

Abstract

The molecular basis of the temperature-sensitive (ts) phenotype of P3/Sabin, the type 3 vaccine strain of poliovirus, was investigated in light of the known correlation between ts and attenuation phenotypes. A phenylalanine at residue 91 of the capsid protein VP3 was a major determinant of both phenotypes, and attenuation and ts could be reverted by the same second-site mutations. The ts phenotype was due to a defect early in the assembly process that inhibited the formation of 14S pentamers, empty capsids, and virions. It was further shown that capsid proteins that were not incorporated into higher-order structures had short half-lives at the nonpermissive temperature.

MeSH Terms
Capsid/genetics,immunology,isolation & purification Cell Line Centrifugation, Density Gradient Humans Kinetics Mutation Phenotype Poliovirus/genetics,growth & development,immunology Poliovirus Vaccine, Oral RNA, Viral/genetics,isolation & purification Temperature Vaccines, Attenuated
Chemicals
Poliovirus Vaccine, Oral RNA, Viral Vaccines, Attenuated
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Macadam A J
National Institute for Biological Standards and Control, Hertfordshire, United Kingdom.
Ferguson G
Arnold C
Minor P D
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31 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.65.10.5225-5231.1991
Published
1991-10-00
Pages
5225-31
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC249000
Subset
IM
External Links
PubMed source DOI: 10.1128/JVI.65.10.5225-5231.1991 PMC Full Text View journal details
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