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© Michel-Robert Popoff
Clostridium difficile en microscopie à contraste de phase. On distingue des bactéries sporulées, non sporulées et d'autres en cours de lyse (destruction). Bactérie de l'environnement (sol, eau, foin, sable), elle est à l'origine d'infections nosocomiales survenant après un traitement antibiotique : Clostridium difficile prédomine alors que les autres bactéries de la flore intestinale ont été détruites. L'infection peut provoquer deux types de pathologies graves : les colites pseudo-membraneuses dont l'origine est quasiment due à 100 % à C. difficile et la diarrhée post-antibiothérapie due à C. difficile dans 30 % des cas de ces diarrhées.
Publication : Journal of bacteriology

The levanase operon of Bacillus subtilis expressed in Escherichia coli can substitute for the mannose permease in mannose uptake and bacteriophage lambda infection

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of bacteriology - 01 Dec 1996

Martin-Verstraete I, Michel V, Charbit A

Link to Pubmed [PMID] – 8955391

J. Bacteriol. 1996 Dec;178(24):7112-9

Bacteriophage lambda adsorbs to its Escherichia coli K-12 host by interacting with LamB, a maltose- and maltodextrin-specific porin of the outer membrane. LamB also serves as a receptor for several other bacteriophages. Lambda DNA requires, in addition to LamB, the presence of two bacterial cytoplasmic integral membrane proteins for penetration, namely, the IIC(Man) and IID(Man) proteins of the E. coli mannose transporter, a member of the sugar-specific phosphoenolpyruvate:sugar phosphotransferase system (PTS). The PTS transporters for mannose of E. coli, for fructose of Bacillus subtilis, and for sorbose of Klebsiella pneumoniae were shown to be highly similar to each other but significantly different from other PTS transporters. These three enzyme II complexes are the only ones to possess distinct IIC and IID transmembrane proteins. In the present work, we show that the fructose-specific permease encoded by the levanase operon of B. subtilis is inducible by mannose and allows mannose uptake in B. subtilis as well as in E. coli. Moreover, we show that the B. subtilis permease can substitute for the E. coli mannose permease cytoplasmic membrane components for phage lambda infection. In contrast, a series of other bacteriophages, also using the LamB protein as a cell surface receptor, do not require the mannose transporter for infection.

http://www.ncbi.nlm.nih.gov/pubmed/8955391