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. 1983 Aug;46(2):297–303. doi: 10.1128/aem.46.2.297-303.1983

Characterization of Gypsy Moth (Lymantria dispar) Nuclear Polyhedrosis Virus

Brad Stiles 1, John P Burand 1, Marta Meda 1, H A Wood 1
PMCID: PMC239376  PMID: 16346355

Abstract

Characterization of the proteins and nucleic acid of the gypsy moth nuclear polyhedrosis virus isolated in Ithaca, N.Y. (LdNPV-IT) is presented. A total of 29 viral structural proteins were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis when the virus was isolated in the absence of alkaline protease activity. Fourteen surface envelope viral proteins were identified by lactoperoxidase iodination. Eleven proteins were associated with nucleocapsids prepared by Nonidet P-40 detergent treatment. Distinct alterations of viral proteins were documented when virions were purified in the presence of occlusion body-associated alkaline protease(s). Restriction enzyme digests of viral DNA indicated that this isolate was composed of a large number of genetic variants. On the basis of the major molar fragments resulting from EcoRI, BamHI, BglII, and HindIII digests, the molecular weight of the LdNPV genome was approximately 88 × 106.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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