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Poliovirus neutralization by antibodies to internal epitopes of VP4 and VP1 results from reversible exposure of these sequences at physiological temperature
- Source :
- Europe PubMed Central
-
Abstract
- Antisera were raised against peptide sequences that are normally internal in the poliovirus virion. These antisera contain neutralizing activity, but this neutralizing activity is dependent on coincubation of the virus and antisera at 37 degrees C. Immunoprecipitation analyses demonstrate that the neutralization is due to exposure of these normally internal sequences at 37 degrees C and subsequent antibody binding. Exposure of these sequences is reversible. These data demonstrate that the poliovirus particle is a dynamic entity that is capable of undergoing conformational alterations at physiological temperatures. This conformational flexibility provides an explanation for earlier observations of virus neutralization by antibodies to internal epitopes which can be accommodated within the framework of existing models for antibody-mediated neutralization of viral infectivity. Analogies between the sequences which are reversibly exposed at 37 degrees C with those which are irreversibly exposed upon receptor binding suggest that the observed conformational dynamics also may play a role in cell entry.
- Subjects :
- Immunoprecipitation
Protein Conformation
Immunology
Biology
medicine.disease_cause
Antibodies, Viral
Microbiology
Neutralization
Virus
Epitope
Epitopes
Protein structure
Capsid
Antibody Specificity
Neutralization Tests
Virology
medicine
Humans
Antigens, Viral
Antiserum
Poliovirus
Temperature
Molecular biology
Insect Science
Biophysics
Capsid Proteins
HeLa Cells
Research Article
Subjects
Details
- Database :
- OpenAIRE
- Journal :
- Europe PubMed Central
- Accession number :
- edsair.doi.dedup.....9655b60bb869a39decf45d1ff6f95d82