Boyce Thompson Institute for Plant Research, Cornell University, Ithaca, New York 14853.
Appl Environ Microbiol. 1983 Aug;46(2):297-303. doi: 10.1128/aem.46.2.297-303.1983.
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 x 10.
本文介绍了在纽约伊萨卡分离得到的舞毒蛾核多角体病毒（LdNPV-IT）的蛋白质和核酸特性。在没有碱性蛋白酶活性的情况下分离病毒时，通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳鉴定出 29 种病毒结构蛋白。通过乳过氧化物酶碘化法鉴定出 14 种表面包膜病毒蛋白。用非离子型去污剂 Nonidet P-40 处理制备核衣壳时，有 11 种蛋白与之相关。当在包含包埋体相关碱性蛋白酶的情况下纯化病毒时，记录到病毒蛋白的明显改变。病毒 DNA 的限制性内切酶消化表明，该分离物由大量遗传变异体组成。根据 EcoRI、BamHI、BglII 和 HindIII 消化产生的主要摩尔片段，LdNPV 基因组的分子量约为 88×10^6。
