TY - JOUR
T1 - Equine cytomegalovirus
T2 - Structural proteins of virions and nucleocapsids
AU - Caughman, Gretchen B.
AU - Staczek, John
AU - O'Callaghan, Dennis J.
N1 - Funding Information:
We thank Ms. D. Brewer for excellent technical assistance; Ma. D. Sullivan and Mr. R. Baumann for preparing photographs; and Ms. L. Devine for typing the manuscript. This research was supported by a grant from the Grayson Foundation, Grant PCM-7% 22700 awarded by the National Science Foundation, and Grants AI02032, S-507-RR05386 and AI19415 awarded by the National Institutes of Health. G.B.C. is a postdoctoral fellow of the National Cancer Institute (5 F32 CA 07210-02).
PY - 1984/4/15
Y1 - 1984/4/15
N2 - Enveloped virions and nucleocapsids of equine cytomegalovirus (ECMV; equine herpesvirus type 2) have been purified from the supernatants and the nuclear extracts of infected rabbit kidney (RK) cells, respectively, and their structural protein compositions have been analyzed. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that ECMV nucleocapsids were composed of nine proteins (average molecular weights = 148K, 52K, 49.5K, 46K, 43.5K, 38.5K, 27K, 20K, and 18K), which together constituted 89% of the total nucleocapsid protein on the basis of incorporated 3H-labeled amino acids. The 148K protein comprised 47.3% of the total protein and thus appeared to be similar in molecular weight and proportional composition to the major capsid proteins of other herpesviruses. Purified virions were composed of 37 proteins whose average molecular weights ranged from 14K to greater than 200K. Three intense glycoprotein bands (83K, 78K, and 73.5K) as well as four less intensely labeled glycoproteins were detected in [3H]glucosamine-labeled virion preparations. At least 14 structural proteins were readily detected in extracts of infected cells which had been [3S)methionine labeled late in infection, and 11 of these were immunoprecipitated by rabbit antiserum against purified virions. The protein composition of ECMV differs substantially from those of equine herpesvirus type 1 and type 3 as well as from those of other herpesviruses.
AB - Enveloped virions and nucleocapsids of equine cytomegalovirus (ECMV; equine herpesvirus type 2) have been purified from the supernatants and the nuclear extracts of infected rabbit kidney (RK) cells, respectively, and their structural protein compositions have been analyzed. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis revealed that ECMV nucleocapsids were composed of nine proteins (average molecular weights = 148K, 52K, 49.5K, 46K, 43.5K, 38.5K, 27K, 20K, and 18K), which together constituted 89% of the total nucleocapsid protein on the basis of incorporated 3H-labeled amino acids. The 148K protein comprised 47.3% of the total protein and thus appeared to be similar in molecular weight and proportional composition to the major capsid proteins of other herpesviruses. Purified virions were composed of 37 proteins whose average molecular weights ranged from 14K to greater than 200K. Three intense glycoprotein bands (83K, 78K, and 73.5K) as well as four less intensely labeled glycoproteins were detected in [3H]glucosamine-labeled virion preparations. At least 14 structural proteins were readily detected in extracts of infected cells which had been [3S)methionine labeled late in infection, and 11 of these were immunoprecipitated by rabbit antiserum against purified virions. The protein composition of ECMV differs substantially from those of equine herpesvirus type 1 and type 3 as well as from those of other herpesviruses.
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U2 - 10.1016/0042-6822(84)90284-8
DO - 10.1016/0042-6822(84)90284-8
M3 - Article
C2 - 6324468
AN - SCOPUS:0021340981
SN - 0042-6822
VL - 134
SP - 184
EP - 195
JO - Virology
JF - Virology
IS - 1
ER -