Structural protein relationships among eastern equine encephalitis viruses.
Abstract: We have re-evaluated the relationships among the polypeptides of eastern equine encephalitis (EEE) viruses using SDS-PAGE and peptide mapping of individual virion proteins. Four to five distinct polypeptide bands were detected upon SDS-PAGE analysis of viruses: the E1, E2 and C proteins normally associated with alphavirus virions, as well as an additional more rapidly-migrating E2-associated protein and a high M(r) (HMW) protein. In contrast with previous findings by others, the electrophoretic profiles of the virion proteins of EEE viruses displayed a marked correlation with serotype. The protein profiles of the 33 North American (NA)-serotype viruses examined were remarkably homogeneous, with variation detected only in the E1 protein of two isolates. In contrast, considerable heterogeneity was observed in the migration profiles of both the E1 and E2 glycoproteins of the 13 South American (SA)-type viruses examined. Peptide mapping of individual virion proteins using limited proteolysis with Staphylococcus aureus V8 protease confirmed that, in addition to the homogeneity evident among NA-type viruses and relative heterogeneity among SA-type viruses, the E1 and E2 proteins of NA- and SA-serotype viruses exhibited serotype-specific structural variation. The C protein was highly conserved among isolates of both virus serotypes. Endoglycosidase analyses of intact virions did not reveal substantial glycosylation differences between the glycoproteins of NA- and SA-serotype viruses. Both the HMW protein and the E2 protein (doublet) of EEE virus appeared to contain, at least in part, high-mannose type N-linked oligosaccharides. No evidence of O-linked glycans was found on either the E1 or the E2 glycoprotein. Despite the observed structural differences between proteins of NA- and SA-type viruses, Western blot analyses utilizing polyclonal antibodies indicated that immunoreactive epitopes appeared to be conserved.
Publication Date: 1994-11-01 PubMed ID: 7964601DOI: 10.1099/0022-1317-75-11-2897Google Scholar: Lookup
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- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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The research article analyses the relationships among the polypeptides of Eastern Equine Encephalitis (EEE) viruses and the differences in protein structures found in North American and South American variants of the virus.
Highlights of The Research
- The researchers used Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis (SDS-PAGE) and peptide mapping techniques to study the proteins of EEE viruses.
- Four or five distinct polypeptide bands were detected in the analysis, including the E1, E2 and C proteins associated with alphavirus virions, plus an additional E2-associated protein and a high molecular weight protein.
- Their findings contradict previous research, as they found that the profiles of the virion proteins of EEE viruses were highly correlated with serotype (sub-group of the viruses).
Differences in Protein Profiles between North and South American Viruses
- The research found that North American variants of the virus had very uniform protein profiles, with differences only found in the E1 protein of two samples.
- On the other hand, there was a lot more variance in the E1 and E2 glycoproteins of the South American variants.
- This suggests that each serotype has specific structural variations.
Conserved and Varied Elements
- The C protein was found to be highly conserved between the variants of the two serotypes.
- Despite the structural differences, the presence of immunoreactive epitopes, which invoke an immune response, seemed to be conserved as indicated by Western blot analysis using polyclonal antibodies.
- No major differences were found in glycosylation (attachment of sugar molecules which helps in protein folding and stability) among the NA and SA serotype viruses.
Implications of the Study
- This research could be crucial for understanding the pathogenic mechanisms of different variants of EEE viruses.
- This could potentially guide future therapeutic strategies and vaccine design against EEE virus infection.
Cite This Article
APA
Strizki JM, Repik PM.
(1994).
Structural protein relationships among eastern equine encephalitis viruses.
J Gen Virol, 75 ( Pt 11), 2897-2909.
https://doi.org/10.1099/0022-1317-75-11-2897 Publication
Researcher Affiliations
- Department of Microbiology & Immunology, Medical College of Pennsylvania, Philadelphia 19129.
MeSH Terms
- Animals
- Birds / virology
- Culicidae / virology
- Dogs / virology
- Electrophoresis, Polyacrylamide Gel
- Encephalitis Virus, Eastern Equine / classification
- Encephalitis Virus, Eastern Equine / isolation & purification
- Glycoproteins / analysis
- Glycoproteins / isolation & purification
- Horses / virology
- Humans
- Peptide Mapping
- Serotyping
- South America
- United States
- Viral Proteins / analysis
- Viral Proteins / isolation & purification
- Virion / chemistry
Grant Funding
- AI 24989 / NIAID NIH HHS
Citations
This article has been cited 2 times.- Crispin M, Harvey DJ, Bitto D, Bonomelli C, Edgeworth M, Scrivens JH, Huiskonen JT, Bowden TA. Structural plasticity of the Semliki Forest virus glycome upon interspecies transmission.. J Proteome Res 2014 Mar 7;13(3):1702-12.
- Cooper LA, Scott TW. Differential evolution of eastern equine encephalitis virus populations in response to host cell type.. Genetics 2001 Apr;157(4):1403-12.
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