Antigenic and Sequence Diversity in Gonococcal Transferrin-Binding Protein A
| Autor: | Cynthia Nau Cornelissen, Ian C. Boulton, James E. Anderson, P F Sparling |
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| Jazyk: | angličtina |
| Rok vydání: | 2000 |
| Předmět: |
Sequence analysis
Immunology Molecular Sequence Data Cross Reactions medicine.disease_cause Microbiology Antigenic Diversity Species Specificity Iron-Binding Proteins Receptors Transferrin medicine Antigenic variation Amino Acid Sequence Peptide sequence chemistry.chemical_classification biology Sequence Homology Amino Acid Lactoferrin Iron-binding proteins Sequence Analysis DNA Transferrin-Binding Proteins Molecular biology Antibodies Bacterial Antigenic Variation Neisseria gonorrhoeae Infectious Diseases chemistry Transferrin biology.protein Molecular and Cellular Pathogenesis Parasitology Carrier Proteins |
| Popis: | Neisseria gonorrhoeaeis a gram-negative pathogen that is capable of satisfying its iron requirement with human iron-binding proteins such as transferrin and lactoferrin. Transferrin-iron utilization involves specific binding of human transferrin at the cell surface to what is believed to be a complex of two iron-regulated, transferrin-binding proteins, TbpA and TbpB. The genes encoding these proteins have been cloned and sequenced from a number of pathogenic, gram-negative bacteria. In the current study, we sequenced four additionaltbpAgenes from otherN. gonorrhoeaestrains to begin to assess the sequence diversity among gonococci. We compared these sequences to those from other pathogenic bacteria to identify conserved regions that might be important for the structure and function of these receptors. We generated polyclonal mouse sera against synthetic peptides deduced from the TbpA sequence from gonococcal strain FA19. Most of these synthetic peptides were predicted to correspond to surface-exposed regions of TbpA. We found that, while most reacted with denatured TbpA in Western blots, only one antipeptide serum reacted with native TbpA in the context of intact gonococci, consistent with surface exposure of the peptide to which this serum was raised. In addition, we evaluated a panel of gonococcal strains for antigenic diversity using these antipeptide sera. |
| Databáze: | OpenAIRE |
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