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Molecular characterization of the mycobacterial heparin-binding hemagglutinin, a mycobacterial adhesin.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Menozzi, Franco Bischoff, Richard Fort, Emmanuel Brennan, Michael James Locht, Camille |
| Copyright Year | 1998 |
| Abstract | Although it generally is accepted that the interaction of Mycobacterium tuberculosis with alveolar macrophages is a key step in the pathogenesis of tuberculosis, interactions with other cell types, especially epithelial cells, also may be important. In this study we describe the molecular characterization of a mycobacterial heparin-binding hemagglutinin (HBHA), a protein that functions as an adhesin for epithelial cells. The structural gene was cloned from M. tuberculosis and bacillus Calmette-Guérin, and the sequence was found to be identical between the two species. The calculated Mr was smaller than the observed Mr when analyzed by SDS/PAGE. This difference can be attributed to the Lys/Pro-rich repeats that occur at the C-terminal end of the protein and to a putative carbohydrate moiety. Glycosylation of HBHA appears to protect the protein from proteolytic degradation, which results in the removal of the C-terminal Lys/Pro-rich region responsible for binding of HBHA to sulfated carbohydrates. Evidence suggests that glycosylation is also important for HBHA-mediated hemagglutination and for certain immunologic properties of the protein. Finally, the absence of a signal peptide in the coding region of HBHA raises the possibility that this protein is not secreted via the general secretion pathway. |
| File Format | PDF HTM / HTML |
| DOI | 10.1073/pnas.95.21.12625 |
| Alternate Webpage(s) | http://www.pnas.org/content/95/21/12625.full.pdf |
| PubMed reference number | 9770536 |
| Alternate Webpage(s) | https://doi.org/10.1073/pnas.95.21.12625 |
| Journal | Medline |
| Volume Number | 95 |
| Issue Number | 21 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
