Journal
ANNUAL REVIEW OF MICROBIOLOGY, VOL 65
Volume 65, Issue -, Pages 71-90Publisher
ANNUAL REVIEWS
DOI: 10.1146/annurev-micro-090110-102943
Keywords
RtxA; Vibrio; Pseudomonas; VCBS; FrhA; Legionella pneumophila
Categories
Funding
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R21AI072461, R01AI051490] Funding Source: NIH RePORTER
- NIAID NIH HHS [AI051490-08, R01 AI051490, AI072461-02] Funding Source: Medline
Ask authors/readers for more resources
The Repeats-in-Toxins (RTX) family of proteins classically consists of cytolysins and hemolysins. Over the past decade, genome sequencing revealed the existence of very large members of this family. These are all repetitive proteins ranging in size from 200 to 900 kDa that function as toxins or adhesins. Many are exported by Type I secretion. One major new subfamily is the large repetitive RTX adhesins and biofilm-associated proteins. These are characterized by 80- to 300-amino-acid repeats ordered in tandem, although the sequence and number of the repeats vary by protein. The second major new subfamily is the multifunctional-autoprocessing RTX toxins, which are associated with cytotoxicity and pathogenesis. These proteins are in turn distantly related to Yersinia hypothetical RTX proteins that may autoprocess by a similar mechanism. This review discusses current knowledge regarding the structure and function of these new subfamilies of RTX proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available