Purification and characterization of type 1 fimbriae of Salmonella typhi
| Autor: | Patrizia Muscas, Gian Maria Rossolini, Annalisa Santucci, Alessandra Chiesurin, Giuseppe Satta |
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| Rok vydání: | 1994 |
| Předmět: |
Antigenicity
Salmonella Protein Denaturation Immunology Fimbria Molecular Sequence Data Salmonella typhi medicine.disease_cause Microbiology Epitope Fimbriae Proteins Bacterial Proteins Species Specificity Virology medicine Animals Amino Acid Sequence Antiserum Antigens Bacterial biology Sequence Homology Amino Acid biochemical phenomena metabolism and nutrition bacterial infections and mycoses biology.organism_classification Enterobacteriaceae Antibodies Bacterial Fimbriae Bacterial bacteria Electrophoresis Polyacrylamide Gel Rabbits Peptides |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0385-5600 |
| Popis: | Type 1 fimbriae have been purified from a Salmonella typhi strain of clinical origin. Purified fimbriae retained their ability to bind to erythrocytes in a mannose-inhibitable fashion and, in doing so, behaved preferentially as a monovalent adhesin. SDS-PAGE analysis of the fimbrial preparation showed the presence of a 20-kDa major polypeptide component (fimbrillin) and of additional larger polypeptides present in smaller amounts. The amino-terminal sequence of fimbrillin was determined and turned out to be very similar but not identical to that of type 1 fimbrillins of other Salmonella serovars. A Western blot analysis of the purified fimbrial preparation using an antiserum raised against native fimbriae suggested that fimbrial proteins did not carry any major sequential epitope and that, in native fimbriae, conformational epitopes, possibly generated between different subunits, might provide for the major immunogenic epitopes. Analysis of different S. typhi clinical isolates using the anti-fimbrial antiserum showed an overall immunological similarity of these structures within this serovar. |
| Databáze: | OpenAIRE |
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