Hexon peptides of type 2, 3, and 5 adenoviruses and their relationship to hexon structure
| Autor: | H S Ginsberg, M F Stinski |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
viruses
Immunology Biology Tritium Microbiology Adenoviridae Iodine Radioisotopes Viral Proteins chemistry.chemical_compound Virology Carbon Radioisotopes Cyanogen Bromide Amino Acids Isoelectric focusing Lactoperoxidase virus diseases Molecular biology eye diseases stomatognathic diseases Isoelectric point Biochemistry Capsid chemistry Insect Science biology.protein Electrophoresis Polyacrylamide Gel Cyanogen bromide Isoelectric Focusing Antibody Peptides Research Article |
| Zdroj: | Journal of Virology. 15:898-905 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.15.4.898-905.1975 |
| Popis: | Peptides of hexons from type 2 and 5 (subgroup III) and type 3 (subgroup I) adenoviruses were produced by treatment with cyanogen bromide and were separated by isoelectric focusing in polyacrylamide gels containing 8 M urea. Peptides with identical isoelectric points, but from different hexon types, were considered to have structural similarities. According to this criterion for chemical relatedness, about two-thirds of the type 2 and 5 hexon peptides may be considered similar. In contrast, the majority of the type 3 hexon peptides differed chemically from peptides of type 2 and 5 hexons. Virions and free hexons were iodinated with 125-I in the presence of lactoperoxidase and H-2-O-2. When 125-I-labeled virions were disrupted and the hexon was purified, the highly labeled cyanogen bromide peptides were labeled. When purified hexons from the excess cellular pool were iodinated, peptides common to types 2, 3, and 5 (peptides 12 and 14) were most extensively labeled. Thus, hexons assembled in virions and those free in solution were iodinated differently. The data suggest that immunologically the hexons in viral capsids react differently from unassembled hexons because the polypeptide chains assume slightly different folding configurations in the two hexon forms and therefore expose different regions of the protein to antibodies. |
| Databáze: | OpenAIRE |
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