A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi and Borrelia hermsii
| Autor: | J L Benach, J A Gebbia, P B Backenson, J L Coleman, Pedro Anda |
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| Rok vydání: | 1996 |
| Předmět: |
Molecular Sequence Data
Immunology Spirochaetaceae Cross Reactions Biology Polymerase Chain Reaction Microbiology Borrelia burgdorferi Group Species Specificity stomatognathic system Antibody Specificity Borrelia Amino Acid Sequence Borrelia burgdorferi Gene Peptide sequence Glyceraldehyde 3-phosphate dehydrogenase Antigens Bacterial Lyme Disease Base Sequence Sequence Homology Amino Acid Relapsing Fever Antibodies Monoclonal Glyceraldehyde-3-Phosphate Dehydrogenases Chromosomes Bacterial bacterial infections and mycoses biology.organism_classification Antibodies Bacterial Molecular biology Infectious Diseases Immunoglobulin M Genes Bacterial biology.protein Lyme disease microbiology Parasitology Borrelia hermsii DNA Probes Sequence Analysis Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.64.1.262-268.1996 |
| Popis: | A polyreactive monoclonal antibody recognized a 38.5-kDa polypeptide with amino-terminal sequence identity to conserved regions of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in Borrelia burgdorferi, the Lyme disease agent, and Borrelia hermsii, an agent of American relapsing fever. This monoclonal antibody also recognized GAPDH from other pathogenic spirochetes and other prokaryotes and eukaryotes as well. GAPDH activity was detected in sonicates of both B. burgdorferi and B. hermsii but not in live, intact organisms, indicating the possibility of a subsurface localization for the Borrelia GAPDH activity. Degenerate primers constructed from highly conserved regions of gapdh of other prokaryotes successfully amplified this gene homolog in both B. burgdorferi and B. hermsii. Nuclei acid and deduced amino acid sequence analysis of the 838-bp probes for each borrelia indicated 93.9% identity between B. burgdorferi and B. hermsii at the amino acid level. Amino acid identities of B. burgdorferi and B. hermsii with Bacillus stearothermophilus were 59.2% and 58.8% respectively. Southern hybridization studies indicated that the gene encoding GAPDH is located on the chromosome of each borrella. In other bacterial species, GAPDH has other functions in addition to its traditional enzymatic role in the glycolytic pathway. GAPDH may play a similar role in borrelias. |
| Databáze: | OpenAIRE |
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