1887

Abstract

is typically recognized as an extracellular pathogen. However, a number of studies revealed its ability to invade epithelial cells, indicating a more complex pathogen–host interaction. The molecular mechanisms controlling and facilitating internalization of are poorly understood. In this study, we investigated the role of DIP0733 as virulence factor to elucidate how it contributes to the process of pathogen–host cell interaction. Based on experiments, it was suggested recently that the DIP0733 protein might be involved in adhesion, invasion of epithelial cells and induction of apoptosis. A corresponding mutant strain generated in this study was attenuated in its ability to colonize and kill the host in a infection model system. Furthermore, the mutant showed an altered adhesion pattern and a drastically reduced ability to adhere and invade epithelial cells. Subsequent experiments showed an influence of DIP0733 on binding of to extracellular matrix proteins such as collagen and fibronectin. Furthermore, based on its fibrinogen-binding activity, DIP0733 may play a role in avoiding recognition of by the immune system. In summary, our findings support the idea that DIP0733 is a multi-functional virulence factor of .

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2015-03-01
2024-04-20
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