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dc.contributor.authorTauschek, M
dc.contributor.authorGorrell, RJ
dc.contributor.authorStrugnell, RA
dc.contributor.authorRobins-Browne, RM
dc.date.available2014-05-21T19:39:38Z
dc.date.issued2002-05-14
dc.identifierpii: 99/10/7066
dc.identifier.citationTauschek, M., Gorrell, R. J., Strugnell, R. A. & Robins-Browne, R. M. (2002). Identification of a protein secretory pathway for the secretion of heat-labile enterotoxin by an enterotoxigenic strain of Escherichia coli. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 99 (10), pp.7066-7071. https://doi.org/10.1073/pnas.092152899.
dc.identifier.issn0027-8424
dc.identifier.urihttp://hdl.handle.net/11343/26598
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractEnterotoxigenic Escherichia coli (ETEC) is an enteric pathogen that causes cholera-like diarrhea in humans and animals. ETEC secretes a heat-labile enterotoxin (LT), which resembles cholera toxin, but the actual mechanism of LT secretion is presently unknown. We have identified a previously unrecognized type II protein secretion pathway in the prototypic human ETEC strain, H10407 (serotype O78:H11). The genes for this pathway are absent from E. coli K-12, although examination of the K-12 genome suggests that it probably once possessed them. The secretory pathway bears significant homology at the amino acid level to the type II protein secretory pathway required by Vibrio cholerae for the secretion of cholera toxin. With this in mind, we determined whether the homologous pathway of E. coli H10407 played a role in the secretion of LT. To this end, we inactivated the pathway by inserting a kanamycin-resistance gene into one of the genes (gspD) of the type II secretion pathway by homologous recombination. LT secretion by E. coli H10407 and the gspD mutant was assayed by enzyme immunoassay, and its biological activity was assessed by using Y-1 adrenal cells. This investigation showed that the protein secretory pathway is functional and necessary for the secretion of LT by ETEC. Our findings have revealed the mechanism for the secretion of LT by ETEC, which previously was unknown, and provide further evidence of close biological similarities of the LT and cholera toxin.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherNATL ACAD SCIENCES
dc.subjectBacteriology ; Infectious Diseases
dc.titleIdentification of a protein secretory pathway for the secretion of heat-labile enterotoxin by an enterotoxigenic strain of Escherichia coli
dc.typeJournal Article
dc.identifier.doi10.1073/pnas.092152899
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentMicrobiology And Immunology
melbourne.source.titleProceedings of the National Academy of Sciences of USA
melbourne.source.volume99
melbourne.source.issue10
melbourne.source.pages7066-7071
melbourne.publicationid9233
melbourne.elementsid251647
melbourne.openaccess.pmchttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC124529
melbourne.contributor.authorStrugnell, Richard
melbourne.contributor.authorRobins-Browne, Roy
melbourne.contributor.authorTAUSCHEK, MARIJA
dc.identifier.eissn1091-6490
melbourne.accessrightsAccess this item via the Open Access location


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