| Autor: |
Deshpande RG; Department of Microbiology and Immunology, Morehouse School of Medicine, Atlanta, Georgia 30310., Khan MB, Bhat DA, Navalkar RG |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of medical microbiology [J Med Microbiol] 1994 Dec; Vol. 41 (6), pp. 378-83. |
| DOI: |
10.1099/00222615-41-6-378 |
| Abstrakt: |
A 66-kDa protein (TB66) was purified from culture filtrate (CF) and cell sonicate (CS) of Mycobacterium tuberculosis H37Rv by immobilised metal affinity chromatography (IMAC) on a Ni-nitrilotriacetic acid (NTA) column. TB66 was found to be a fibronectin-binding protein as determined by ELISA and could be purified by affinity chromatography with fibronectin-Sepharose. A similar 66-kDa protein could be isolated also from M. bovis, M. bovis BCG, M. africanum and M. tuberculosis H37Ra by IMAC, but not from any other mycobacteria. The NH2-terminal amino-acid sequence of TB66 from H37Rv and M. bovis was identical and showed 85% homology with the N-terminal sequence of bovine serum albumin (BSA). A monoclonal antibody (MAb) OD4AG3 recognised a heat-stable and trypsin-sensitive epitope near the C-terminal end of TB66. This MAb also recognised the 66-kDa protein isolated from the other members of the M. tuberculosis complex. In tests of immunogenicity, TB66 elicited a delayed type hypersensitivity reaction in guinea-pigs immunised with either TB66 or with M. tuberculosis H37Rv. TB66 also elicited an antibody response in immunised guinea-pigs and stimulated murine macrophages to produce tumour necrosis factor. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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