Secretion of the Escherichia coli K-12 SheA hemolysin is independent of its cytolytic activity
Open Access
- 1 November 2001
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 204 (2) , 281-285
- https://doi.org/10.1111/j.1574-6968.2001.tb10898.x
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Cytocidal and Apoptotic Effects of the ClyA Protein from Escherichia coli on Primary and Cultured Monocytes and MacrophagesInfection and Immunity, 2000
- Autodisplay: Functional Display of Active β-Lactamase on the Surface of Escherichia coli by the AIDA-I AutotransporterJournal of Bacteriology, 2000
- E. coli Hemolysin E (HlyE, ClyA, SheA)Cell, 2000
- Regulation of theEscherichia coli sheAgene and characterization of its encoded hemolytic activityFEMS Microbiology Letters, 1998
- The Escherichia coli K‐12 sheA gene encodes a 34‐kDa secreted haemolysinMolecular Microbiology, 1997
- Identification of two regions of Klebsiella oxytoca pullulanase that together are capable of promoting β‐lactamase secretion by the general secretory pathwayMolecular Microbiology, 1996
- Secretion across the bacterial outer membraneTrends in Genetics, 1992
- β‐lactamase as a probe of membrane protein assembly and protein exportMolecular Microbiology, 1990
- The normally periplasmic enzyme β‐lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell‐surface enzyme pullulanaseMolecular Microbiology, 1990
- Novel Method for Detection of β-Lactamases by Using a Chromogenic Cephalosporin SubstrateAntimicrobial Agents and Chemotherapy, 1972