Journal Article

PreJuSER-31426

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Disruption of Cg-Ppm1, a polyprenol monophosphomannose synthase and the generation of lipoglycan-less mutants in Corynebacterium glutamicum

Gibson, K. J. ; Eggeling, L.FZJ* ; Maughan, W. N. ; Krumbach, K.FZJ* ; Gurcha, S. S. ; Nigou, J. ; Puzo, G. ; Besra, N. A. M. ; Sahm, H.FZJ*

2003
Soc. Bethesda, Md.

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Please use a persistent id in citations: http://hdl.handle.net/2128/2825  doi:10.1074/jbc.M307988200

Abstract: The glycosyl donor, polyprenyl monophosphomannose (PPM), has been shown to be involved in the biosynthesis of the mycobacterial lipoglycans: lipomannan and lipoarabinomannan. The mycobacterial PPM synthase (Mt-ppm1) catalyzes the transfer of mannose from GDP-mannose to polyprenyl phosphates. Based on sequence homology to Mt-ppm1, we have identified the PPM synthase from Corynebacterium glutamicum. In the present study, we demonstrate that the corynebacterial synthase is composed of two distinct domains; a catalytic domain (Cg-ppm1) and a membrane domain (Cg-ppm2). Through the inactivation of Cg-ppm1, we observed a complex phenotype that included altered cell growth rate and inability to synthesize PPM molecules and lipoglycans. When Cg-ppm2 was deleted, no observable phenotype was noted, indicating the clear organization of the two domains. The complementation of the inactivated Cg-ppm1 strain with the corresponding mycobacterial enzyme (Mt-Ppm1/D2) led to the restoration of a wild type phenotype. The present study illustrates, for the first time, the generation of a lipoglycan-less mutant based on a molecular strategy in a member of the Corynebacterianeae family. Lipoglycans are important immunomodulatory molecules involved in determining the outcome of infection, and so the generation of defined mutants and their subsequent immunological characterization is timely.

Keyword(s): Bacterial Proteins: chemistry (MeSH) ; Bacterial Proteins: genetics (MeSH) ; Chromatography, Thin Layer (MeSH) ; Corynebacterium: enzymology (MeSH) ; DNA: metabolism (MeSH) ; Electrophoresis, Polyacrylamide Gel (MeSH) ; Escherichia coli: metabolism (MeSH) ; Genetic Complementation Test (MeSH) ; Lipopolysaccharides: metabolism (MeSH) ; Mannose: biosynthesis (MeSH) ; Mannose: chemistry (MeSH) ; Mannosyltransferases: biosynthesis (MeSH) ; Mannosyltransferases: chemistry (MeSH) ; Mannosyltransferases: genetics (MeSH) ; Mannosyltransferases: metabolism (MeSH) ; Models, Genetic (MeSH) ; Mutation (MeSH) ; Phenotype (MeSH) ; Phylogeny (MeSH) ; Plasmids: metabolism (MeSH) ; Protein Structure, Tertiary (MeSH) ; Time Factors (MeSH) ; Bacterial Proteins ; Lipopolysaccharides ; Mannose ; DNA ; Mannosyltransferases ; polyprenyl monophosphomannose synthase, bacteria ; J

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Biotechnologie 1 (IBT-1)

Research Program(s):

1. Biotechnologie (L02)

Appears in the scientific report 2003

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Database coverage:

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