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First published online January 17, 2009


Journal of Cell Science 122, 204e (2009)
© The Company of Biologists Limited
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In this issue

Pneumococci take the integrin route


Figure 1

To promote its invasion into host cells, the Gram-positive bacterium Streptococcus pneumoniae (pneumococcus) interacts specifically with several host proteins, including cell-surface receptors and ECM components. For instance, pneumococci are known to bind to the ECM- and plasma-localised protein vitronectin, and Sven Hammerschmidt and colleagues (p. 256) now shed light on how this interaction affects pneumococcal uptake and host-cell signalling cascades. Using flow cytometry, the authors first show that pneumococci interact with the heparin-binding sites of multimeric (ECM-associated) vitronectin. Moreover, cell-associated multimeric vitronectin promotes pneumococcal adhesion to, and invasion of, human epithelial and endothelial cells. Notably, the authors show that {alpha}vβ3 integrin is required for vitronectin-dependent invasion – as is integrin-linked kinase (ILK), which is known to mediate several downstream effects of integrin activation (including actin-cytoskeleton reorganisation). In line with this observation, internalisation of pneumococci requires a dynamic actin cytoskeleton, and their interaction with the host cell causes the formation of microspike-like structures (see image) that are the sites of pneumococcal entrapment. The authors conclude that pneumococci exploit the dynamic processes of the host cell to enable invasion.


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Related articles in JCS:

Integrin-linked kinase is required for vitronectin-mediated internalization of Streptococcus pneumoniae by host cells
Simone Bergmann, Anke Lang, Manfred Rohde, Vaibhav Agarwal, Claudia Rennemeier, Carsten Grashoff, Klaus T. Preissner, and Sven Hammerschmidt
JCS 2009 122: 256-267. [Abstract] [Full Text]  




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