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Biochemical and Antigenic Comparisons of the Envelope Glycoproteins of Venezuelan Equine Encephalomyelitis Virus Strains

Vector-Borne Diseases Division, Center for Disease Control, Public Health Service, U.S. Department of Health, Education, and Welfare, and Colorado State University, Fort Collins, Colorado 80522, U.S.A.

Pulse-chase experiments after synchronous initiation of translation indicate that the larger 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 36 x 10³). The mol. wt. of E₁ varied from 48 to 51 x 10³ and the mol. wt. of E₂ glycoproteins ranged from 53 to 59 x 10³. Pixuna virus contained a third envelope glycoprotein of 59 x 10³ mol. wt. in addition to the two major glycoproteins of mol. wt. 53 x 10³ and 48 x 10³ respectively. The isoelectric points (pI) of E₁ and E₂ for all VEE strains 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.

Received 30 August 1978; accepted 13 March 1979.

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