Bacillus cereus Certhrax ADP-ribosylates vinculin to disrupt focal adhesion complexes and cell adhesion. J Biol Chem 2014 Apr 11;289(15):10650-10659
Date
02/28/2014Pubmed ID
24573681Pubmed Central ID
PMC4036183DOI
10.1074/jbc.M113.500710Scopus ID
2-s2.0-84898669505 (requires institutional sign-in at Scopus site) 18 CitationsAbstract
Bacillus cereus is often associated with mild to moderate gastroenteritis; however, some recent isolates cause inhalational anthrax-like diseases and death. These potential emerging human pathogens express multiple virulence factors. B. cereus strain G9241 expresses anthrax toxin, several polysaccharide capsules, and the novel ADP-ribosyltransferase, Certhrax. In this study, we show that Certhrax ADP-ribosylates Arg-433 of vinculin, a protein that coordinates actin cytoskeleton and extracellular matrix interactions. ADP-ribosylation of vinculin disrupted focal adhesion complexes and redistributed vinculin to the cytoplasm. Exogenous vinculin rescued these phenotypes. This provides a mechanism for strain G9241 to breach host barrier defenses and promote bacterial growth and spread. Certhrax is the first bacterial toxin to add a post-translational modification to vinculin to disrupt the actin cytoskeleton.
Author List
Simon NC, Barbieri JTAuthor
Joseph T. Barbieri PhD Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ADP Ribose TransferasesActins
Adenosine Diphosphate Ribose
Amino Acid Sequence
Antigens, Bacterial
Bacillus cereus
Bacterial Proteins
Bacterial Toxins
Cell Adhesion
Cytoskeleton
Extracellular Matrix
Focal Adhesions
HeLa Cells
Humans
Immunity, Innate
Molecular Sequence Data
Mutagenesis
Phenotype
Protein Processing, Post-Translational
Recombinant Proteins
Sequence Homology, Amino Acid
Streptavidin
Vinculin