NDLI: Identification of a domain within the multifunctional Vibrio cholerae RTX toxin that covalently cross-links actin

Content Provider	PubMed Central
Author	Sheahan, Kerri-lynn Cordero, Christina L. Satchell, Karla J. Fullner
Copyright Year	2004
Abstract	The Gram-negative pathogen Vibrio cholerae causes diarrheal disease through the export of enterotoxins. The V. cholerae RTX toxin was previously identified and characterized by its ability to round human laryngeal epithelial (HEp-2) cells. Further investigation determined that cell rounding is caused by the depolymerization of actin stress fibers, through the unique mechanism of covalent actin cross-linking. In this study, we identify a domain within the full-length RTX toxin that is capable of mediating the cross-linking reaction when transiently expressed within eukaryotic cells. A structure/function analysis of the actin cross-linking domain (ACD) reveals that a 412-aa, or a 47.8-kDa, region is essential for cross-linking activity. When this domain is deleted from the full-length toxin gene, actin cross-linking, but not cell rounding, is eliminated, indicating that this toxin carries multiple dissociable activities. The ACD shares 59% amino acid identity with a hypothetical protein from V. cholerae, VC1416, and transient expression of the C-terminal domain of VC1416 also results in actin cross-linking in eukaryotic cells. The presence of this second ACD linked to an Rhs-like element suggests that V. cholerae acquired the domain by horizontal gene transfer and the ACD was inserted into the RTX toxin by gene duplication through the evolution of V. cholerae.
Related Links	http://dx.doi.org/10.1073/pnas.0401104101
Starting Page	9798
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	26
Volume Number	101
Language	English
Publisher	National Academy of Sciences
Publisher Date	2004-06-29
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Identification of a domain within the multifunctional Vibrio cholerae RTX toxin that covalently cross-links actin.

The Actin Cross-Linking Domain of the Vibrio cholerae RTX Toxin Directly Catalyzes the Covalent Cross-Linking of Actin

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