AI Article Synopsis
- Bordetella bronchiseptica uses a type III secretion system (T3SS) to infect a range of mammals, affecting their respiratory systems by introducing virulence factors into host cells.
- BopN and BteA are key effectors: BopN increases IL-10 levels, while BteA is associated with cytotoxicity.
- Research on BopN shows that its N-terminal amino acid residues 1-200 are essential for its entry into host cells, and the removal of residues 6-50 completely stops this process, suggesting BopN also enhances BteA’s toxic effects.
Article Abstract
Bordetella bronchiseptica infects a wide variety of mammals, the type III secretion system (T3SS) being involved in long-term colonization by Bordetella of the trachea and lung. T3SS translocates virulence factors (commonly referred to as effectors) into host cells, leading to alterations in the host's physiological function. The Bordetella effectors BopN and BteA are known to have roles in up-regulation of IL-10 and cytotoxicity, respectively. Nevertheless, the mechanism by which BopN is translocated into host cells has not been examined in sufficient detail. Therefore, to determine the precise mechanisms of translocation of BopN into host cells, truncated derivatives of BopN were built and the derivatives' ability to translocate into host cells evaluated by adenylate cyclase-mediated translocation assay. It was found that N-terminal amino acid (aa) residues 1-200 of BopN are sufficient for its translocation into host cells. Interestingly, BopN translocation was completely blocked by deletion of the N-terminal aa residues 6-50, indicating that the N-terminal region is critical for BopN translocation. Furthermore, BopN appears to play an auxiliary role in BteA-mediated cytotoxicity. Thus, BopN can apparently translocate into host cells and may facilitate activity of BteA.
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| http://dx.doi.org/10.1111/1348-0421.12489 | DOI Listing |
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