Budded Autographa californica NPV 64K protein: Further biochemical analysis and effects of postimmunoprecipitation sample preparation conditions
| Autor: | Loy E. Volkman, Phyllis A. Goldsmith |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Antiserum
Agricultural and Veterinary Sciences biology medicine.drug_class Biological Sciences biology.organism_classification Monoclonal antibody Medical and Health Sciences Molecular biology Virus Epitope Article Vaccine Related Autographa californica Infectious Diseases Isoelectric point Antigen Viral envelope Virology medicine Biotechnology |
| Zdroj: | Virology Virology, vol 139, iss 2 |
| ISSN: | 1096-0341 0042-6822 |
| Popis: | Previously it was shown that AcV1, a neutralizing monoclonal antibody of the Autographa californica nuclear polyhedrosis virus-budded phenotype reacted with a surface antigen present on infected cells during virus budding, and in the viral envelope (L. E. Volkman, P. A. Goldsmith, R. T. Hess, and P. Faulkner (1984), Virology 133, 354-362). Radioimmune precipitation of solubilized, [35S]methionine-labeled budded virus with AcV1 and analysis on SDS-PAGE revealed four bands consistently: one major band at 64,000 Da, and three minor bands at 127,000, 59,000, and 49,000 Da. The reason for the appearance of four bands instead of one was unclear. Data suggest that two of the bands, 49K and 59K, are aberrant, and are the products of sample preparation conditions. Further, evidence is presented that the 127K band is composed of dimers of the 64K protein, and that under nonreducing conditions, oligomers (trimers and tetramers) of 64K protein can also be detected. BVGP 64 is additionally shown to be phosphorylated and to have an isoelectric point of 3.15. The BVGP 64 epitope reactive with AcV1 is destroyed by interaction with SDS. This could account for the lack of neutralizing activity of antiserum made to the SDS-PAGE purified BVGP 64. |
| Databáze: | OpenAIRE |
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