Purification and disposition of a surface protein associated with virulence of Aeromonas salmonicida
| Autor: | J P Monette, William W. Kay, B M Phipps, Edward E. Ishiguro, J T Buckley, Trevor J. Trust |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
chemistry.chemical_classification
biology Lactoperoxidase Membrane Proteins Virulence biology.organism_classification Microbiology Amino acid chemistry.chemical_compound Aeromonas salmonicida Bacterial Proteins chemistry Biochemistry Aeromonas Membrane protein Amino Acids Bacterial outer membrane Guanidine Molecular Biology Research Article |
| Zdroj: | Journal of Bacteriology. 147:1077-1084 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.147.3.1077-1084.1981 |
| Popis: | Virulent strains of Aeromonas salmonicida observed by electron microscopy were characterized by an outer layer exhibiting a tetragonal repeat pattern. Attenuated strains had a 2.5 X 10(3)- to 5 X 10(3)-fold reduction in virulence and lost the outer layer, autoaggregating properties, and a 49-kilodalton protein (A protein) simultaneously. The A protein is the major protein component of outer membrane fractions of virulent strains. A variety of radiolabeling studies showed that this protein was surface localized and that it provided an effective barrier against iodination of other outer membrane proteins with either lactoperoxidase or diazoiodosulfanilic acid; A protein was not labeled with lactoperoxidase but was specifically labeled with diazoidosulfanilic acid. The A protein was purified by selective extraction with detergent and guanidine hydrochloride, and its amino acid composition was determined. The properties of A protein are compared with those of other bacterial surface layer proteins. |
| Databáze: | OpenAIRE |
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