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J Gen Virol 54 (1981), 39-46; DOI 10.1099/0022-1317-54-1-39
© 1981 Society for General Microbiology

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Morphological Components of Herpesvirus. III. Localization of Herpes Simplex Virus Type 1 Nucleocapsid Polypeptides by Immune Electron Microscopy

Steven K. Vernon1, Manuel Ponce De Leon2, Gary H. Cohen2, Roselyn J. Eisenberg3 and B. A. Rubin1

1 Department of Biological Product Development, Wyeth Laboratories, P.O. Box 8299, Philadelphia, Pa. 19101
2 Department of Microbiology and Center for Oral Research, School of Dental Medicine, University of Pennsylvania, Philadelphia, Pa. 19174
and3 Department of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pa. 19174, U.S.A.

Herpes simplex virus type 1 (HSV-1) nucleocapsids were observed in the electron microscope after their reaction with IgG's purified from the sera of rabbits immunized with the individual nucleocapsid polypeptides. The combining sites of NC1, the major capsid protein (mol. wt. 154K), were distributed over the entire capsid surface. This result provides further evidence that NC1 represents the major hexamer constituent. NC2 (mol. wt. 50K) was less widely distributed and appeared to be located at capsid vertices; that antigen may be a constituent of the pentamers or of peripentameric hexamers. One or both of NC3 and NC4 (mol. wt. 40K and 38K) were also located all over the capsid, possibly at positions interior to those of NC1. One or both may represent the intercapsomeric fibrils, hexamer-associated protein or material associated with the pericore. The locations of the other nucleocapsid polypeptides could not be determined.

Received 1 July 1980; accepted 3 December 1980.


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