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Lookup NU author(s): Dr Sven Halbedel, Dr Richard DanielORCiD
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DivIVA is a well-conserved coiled-coil protein present in most Gram-positive bacteria and has been implicated in division site selection, peptidoglycan biosynthesis and sporulation. DivIVA proteins bind lipid membranes and characteristically accumulate at curved membrane areas, i.e. the cell poles and the division site, to which they recruit various interaction partners. We have studied the role of this morphogen in the human pathogen Listeria monocytogenes and our results suggest a novel mechanism by which DivIVA contributes to cell division. Contrary to expectation a ?divIVA mutant exhibited a pronounced chaining phenotype rather than a defect in cell division which we attributed to reduced extracellular levels of the autolytic enzymes p60 and MurA. We demonstrate that this is due to a malfunction in secretion of these autolysins and phenotypic comparison of the ?divIVA strain with a ?secA2 mutant suggests that DivIVA influences the activity of the SecA2 secretion route in L. monocytogenes. Also from the phenotypic analysis it was clear that divIVA affected swarming motility, biofilm formation, invasiveness and cell-to-cell spread in cell culture infection models. Thus, our experiments show that DivIVA is an important factor for various listerial traits that are essential for the pathogenicity of this organism.
Author(s): Halbedel S, Hahn B, Daniel RA, Flieger A
Publication type: Article
Publication status: Published
Journal: Molecular Microbiology
Year: 2012
Volume: 83
Issue: 4
Pages: 821-839
Print publication date: 18/01/2012
ISSN (print): 0950-382X
ISSN (electronic): 1365-2958
Publisher: Wiley-Blackwell Publishing Ltd.
URL: http://dx.doi.org/10.1111/j.1365-2958.2012.07969.x
DOI: 10.1111/j.1365-2958.2012.07969.x
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