Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin
Pathogen‐induced remodelling of the host cell actin cytoskeleton drives internalization of invasive Salmonella by non‐phagocytic intestinal epithelial cells. Two Salmonella actin‐binding proteins are involved in internalization: SipC is essential for the process, while SipA enhances its efficiency....
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Published in | The EMBO journal Vol. 20; no. 9; pp. 2131 - 2139 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Chichester, UK
John Wiley & Sons, Ltd
01.05.2001
Blackwell Publishing Ltd Oxford University Press |
Subjects | |
Online Access | Get full text |
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Summary: | Pathogen‐induced remodelling of the host cell actin cytoskeleton drives internalization of invasive Salmonella by non‐phagocytic intestinal epithelial cells. Two Salmonella actin‐binding proteins are involved in internalization: SipC is essential for the process, while SipA enhances its efficiency. Using purified SipC and SipA proteins in in vitro assays of actin dynamics and F‐actin bundling, we demonstrate that SipA stimulates substantially SipC‐mediated nucleation of actin polymerization. SipA additionally enhances SipC‐ mediated F‐actin bundling, and SipC–SipA collaboration generates stable networks of F‐actin bundles. The data show that bacterial SipC and SipA cooperate to direct efficient modulation of actin dynamics, independently of host cell proteins. The ability of SipA to enhance SipC‐induced reorganization of the actin cytoskeleton in vivo was confirmed using semi‐ permeabilized cultured mammalian cells. |
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Bibliography: | ark:/67375/WNG-S0XSL2W1-C ArticleID:EMBJ7593713 istex:E0D37A60062150400E6BBA3345FEF69FDE03BE09 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0261-4189 1460-2075 1460-2075 |
DOI: | 10.1093/emboj/20.9.2131 |