Biochemical and antigenic comparisons of the envelope glycoproteins of Venezuelan equine encephalomyelitis virus strains

J. K. France, B. C. Wyrick, D. W. Trent

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

Pulse-chase experiments after synchronous initiation of translation indicate that the Venezuelan equine encephalomyelitis (VEE) virus membrane glycoprotein, E2, is derived by proteolytic cleavage of the precursor, PE2. The structural proteins of VEE virus strains representing each of the antigenic subtypes and varieties have been compared by discontinuous SDS-polyacrylamide gel electrophoresis. Nucleocapsid proteins of all isolates were similar in size (mol. wt. 35 to 36x103). The mol. wt. of E1 varied from 48 to 51x103 and the mol. wt. of E2 glycoproteins ranged from 53 to 59x103. Pixuna virus contained a third envelope glycoprotein of 59x103 mol. wt.in addition to the two major glycoproteins of mol. wt. 53x103 and 48x103 respectively. The isoeletric points (pI) of E1 and E2 for all VEE stains studied were approx. 7 and 9 respectively. Both glycoproteins of TC-83 virus induced precipitating antibodies which reacted only with the homologous purified E1 and E2 glycoproteins. Antibodies to E2 protein of each virus neutralized virus infectivity and inhibited the agglutination of goose erythrocytes by virions. Haemagglutination-inhibition tests using antisera to E2 glycoproteins of prototype viruses, representing each of the antigenic subtypes and varieties, differentiated the viruses into subtypes I, II, III and IV with subtype I divided into variants 1AB, 1C, 1D and 1E.

Original languageEnglish (US)
Pages (from-to)725-740
Number of pages16
JournalJournal of General Virology
Volume44
Issue number3
StatePublished - 1979

Fingerprint

Venezuelan Equine Encephalitis Viruses
Glycoproteins
Viruses
Venezuelan Equine Encephalomyelitides
Hemagglutination Inhibition Tests
Nucleocapsid Proteins
Geese
Antibodies
Membrane Glycoproteins
Agglutination
Virion
Immune Sera
Polyacrylamide Gel Electrophoresis
Proteins
Coloring Agents
Erythrocytes

ASJC Scopus subject areas

  • Immunology
  • Virology

Cite this

Biochemical and antigenic comparisons of the envelope glycoproteins of Venezuelan equine encephalomyelitis virus strains. / France, J. K.; Wyrick, B. C.; Trent, D. W.

In: Journal of General Virology, Vol. 44, No. 3, 1979, p. 725-740.

Research output: Contribution to journalArticle

@article{86a27173f09b4fe5a403e7bfc2df04cb,
title = "Biochemical and antigenic comparisons of the envelope glycoproteins of Venezuelan equine encephalomyelitis virus strains",
abstract = "Pulse-chase experiments after synchronous initiation of translation indicate that the Venezuelan equine encephalomyelitis (VEE) virus membrane glycoprotein, E2, is derived by proteolytic cleavage of the precursor, PE2. The structural proteins of VEE virus strains representing each of the antigenic subtypes and varieties have been compared by discontinuous SDS-polyacrylamide gel electrophoresis. Nucleocapsid proteins of all isolates were similar in size (mol. wt. 35 to 36x103). The mol. wt. of E1 varied from 48 to 51x103 and the mol. wt. of E2 glycoproteins ranged from 53 to 59x103. Pixuna virus contained a third envelope glycoprotein of 59x103 mol. wt.in addition to the two major glycoproteins of mol. wt. 53x103 and 48x103 respectively. The isoeletric points (pI) of E1 and E2 for all VEE stains studied were approx. 7 and 9 respectively. Both glycoproteins of TC-83 virus induced precipitating antibodies which reacted only with the homologous purified E1 and E2 glycoproteins. Antibodies to E2 protein of each virus neutralized virus infectivity and inhibited the agglutination of goose erythrocytes by virions. Haemagglutination-inhibition tests using antisera to E2 glycoproteins of prototype viruses, representing each of the antigenic subtypes and varieties, differentiated the viruses into subtypes I, II, III and IV with subtype I divided into variants 1AB, 1C, 1D and 1E.",
author = "France, {J. K.} and Wyrick, {B. C.} and Trent, {D. W.}",
year = "1979",
language = "English (US)",
volume = "44",
pages = "725--740",
journal = "Journal of General Virology",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "3",

}

TY - JOUR

T1 - Biochemical and antigenic comparisons of the envelope glycoproteins of Venezuelan equine encephalomyelitis virus strains

AU - France, J. K.

AU - Wyrick, B. C.

AU - Trent, D. W.

PY - 1979

Y1 - 1979

N2 - Pulse-chase experiments after synchronous initiation of translation indicate that the Venezuelan equine encephalomyelitis (VEE) virus membrane glycoprotein, E2, is derived by proteolytic cleavage of the precursor, PE2. The structural proteins of VEE virus strains representing each of the antigenic subtypes and varieties have been compared by discontinuous SDS-polyacrylamide gel electrophoresis. Nucleocapsid proteins of all isolates were similar in size (mol. wt. 35 to 36x103). The mol. wt. of E1 varied from 48 to 51x103 and the mol. wt. of E2 glycoproteins ranged from 53 to 59x103. Pixuna virus contained a third envelope glycoprotein of 59x103 mol. wt.in addition to the two major glycoproteins of mol. wt. 53x103 and 48x103 respectively. The isoeletric points (pI) of E1 and E2 for all VEE stains studied were approx. 7 and 9 respectively. Both glycoproteins of TC-83 virus induced precipitating antibodies which reacted only with the homologous purified E1 and E2 glycoproteins. Antibodies to E2 protein of each virus neutralized virus infectivity and inhibited the agglutination of goose erythrocytes by virions. Haemagglutination-inhibition tests using antisera to E2 glycoproteins of prototype viruses, representing each of the antigenic subtypes and varieties, differentiated the viruses into subtypes I, II, III and IV with subtype I divided into variants 1AB, 1C, 1D and 1E.

AB - Pulse-chase experiments after synchronous initiation of translation indicate that the Venezuelan equine encephalomyelitis (VEE) virus membrane glycoprotein, E2, is derived by proteolytic cleavage of the precursor, PE2. The structural proteins of VEE virus strains representing each of the antigenic subtypes and varieties have been compared by discontinuous SDS-polyacrylamide gel electrophoresis. Nucleocapsid proteins of all isolates were similar in size (mol. wt. 35 to 36x103). The mol. wt. of E1 varied from 48 to 51x103 and the mol. wt. of E2 glycoproteins ranged from 53 to 59x103. Pixuna virus contained a third envelope glycoprotein of 59x103 mol. wt.in addition to the two major glycoproteins of mol. wt. 53x103 and 48x103 respectively. The isoeletric points (pI) of E1 and E2 for all VEE stains studied were approx. 7 and 9 respectively. Both glycoproteins of TC-83 virus induced precipitating antibodies which reacted only with the homologous purified E1 and E2 glycoproteins. Antibodies to E2 protein of each virus neutralized virus infectivity and inhibited the agglutination of goose erythrocytes by virions. Haemagglutination-inhibition tests using antisera to E2 glycoproteins of prototype viruses, representing each of the antigenic subtypes and varieties, differentiated the viruses into subtypes I, II, III and IV with subtype I divided into variants 1AB, 1C, 1D and 1E.

UR - http://www.scopus.com/inward/record.url?scp=0018651872&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018651872&partnerID=8YFLogxK

M3 - Article

C2 - 119035

AN - SCOPUS:0018651872

VL - 44

SP - 725

EP - 740

JO - Journal of General Virology

JF - Journal of General Virology

SN - 0022-1317

IS - 3

ER -