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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Oswald, E. Labigne, A. Fiorentini, C. Wu, H. C. O'brien, A. D. Boquet, P. Sugai, M. |
| Description | Author Affiliation: Oswald E ( Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814-4799.); |
| Abstract | Cytotoxic necrotizing factor type 2 (CNF2) produced by Escherichia coli strains isolated from intestinal and extraintestinal infections is a dermonecrotic toxin of 110 kDa. We cloned the CNF2 gene from a large plasmid carried by an Escherichia coli strain isolated from a lamb with septicemia. Hydropathy analysis of the deduced amino acid sequence revealed a largely hydrophilic protein with two potential hydrophobic transmembrane domains. The N-terminal half of CNF2 showed striking homology (27% identity and 80% conserved residues) to the N-terminal portion of Pasteurella multocida toxin. Methylamine protection experiments and immunofluorescence studies suggested that CNF2 enters the cytosol of the target cell through an acidic compartment and induces the reorganization of actin into stress fibers. Since the formation of stress fibers in eukaryotic cells involves Rho proteins, we radiolabeled these small GTP-binding proteins from CNF2-treated and control cells with a Rho-specific ADP-ribosyltransferase. The [32P]ADP-ribosylated Rho proteins from CNF2-treated cells migrated slightly more slowly in SDS/PAGE than did the labeled proteins from the control cells. This shift in mobility of Rho proteins in SDS/PAGE was also observed when CNF2 and the RhoA protein were coexpressed in E. coli. We propose that Rho proteins are the targets of CNF2 in mammalian cells. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 9 |
| Volume Number | 91 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1994-06-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actins Metabolism Bacterial Toxins Genetics Pharmacology Cytotoxins Escherichia Coli Proteins Escherichia Coli Pathogenicity GTP-Binding Proteins Actin Cytoskeleton Ultrastructure Adenosine Diphosphate Ribose Cell Line Cloning, Molecular Genes, Bacterial In Vitro Techniques Molecular Sequence Data Restriction Mapping Sequence Alignment Sequence Homology, Amino Acid Rho GTP-Binding Proteins Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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