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Medientyp:
E-Artikel
Titel:
Structure of the bacterial cell division determinant GpsB and its interaction with penicillin‐binding proteins
Beteiligte:
Rismondo, Jeanine;
Cleverley, Robert M.;
Lane, Harriet V.;
Großhennig, Stephanie;
Steglich, Anne;
Möller, Lars;
Mannala, Gopala Krishna;
Hain, Torsten;
Lewis, Richard J.;
Halbedel, Sven
Erschienen:
Wiley, 2016
Erschienen in:Molecular Microbiology
Sprache:
Englisch
DOI:
10.1111/mmi.13279
ISSN:
0950-382X;
1365-2958
Entstehung:
Anmerkungen:
Beschreibung:
<jats:title>Summary</jats:title><jats:p>Each bacterium has to co‐ordinate its growth with division to ensure genetic stability of the population. Consequently, cell division and growth are tightly regulated phenomena, albeit different bacteria utilise one of several alternative regulatory mechanisms to maintain control. Here we consider GpsB, which is linked to cell growth and division in Gram‐positive bacteria. Δ<jats:italic>gpsB</jats:italic> mutants of the human pathogen <jats:italic>Listeria monocytogenes</jats:italic> show severe lysis, division and growth defects due to distortions of cell wall biosynthesis. Consistent with this premise, GpsB interacts both <jats:italic>in vitro</jats:italic> and <jats:italic>in vivo</jats:italic> with the major bi‐functional penicillin‐binding protein. We solved the crystal structure of GpsB and the interaction interfaces in both proteins are identified and validated. The inactivation of <jats:italic>gpsB</jats:italic> results in strongly attenuated virulence in animal experiments, comparable in degree to classical listerial virulence factor mutants. Therefore, GpsB is essential for <jats:italic>in vitro</jats:italic> and <jats:italic>in vivo</jats:italic> growth of a highly virulent food‐borne pathogen, suggesting that GpsB could be a target for the future design of novel antibacterials.</jats:p>