These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms.
    Author: Lilic M, Galkin VE, Orlova A, VanLoock MS, Egelman EH, Stebbins CE.
    Journal: Science; 2003 Sep 26; 301(5641):1918-21. PubMed ID: 14512630.
    Abstract:
    Like many bacterial pathogens, Salmonella spp. use a type III secretion system to inject virulence proteins into host cells. The Salmonella invasion protein A (SipA) binds host actin, enhances its polymerization near adherent extracellular bacteria, and contributes to cytoskeletal rearrangements that internalize the pathogen. By combining x-ray crystallography of SipA with electron microscopy and image analysis of SipA-actin filaments, we show that SipA functions as a "molecular staple," in which a globular domain and two nonglobular "arms" mechanically stabilize the filament by tethering actin subunits in opposing strands. Deletion analysis of the tethering arms provides strong support for this model.
    [Abstract] [Full Text] [Related] [New Search]