Your browser doesn't support javascript.
loading
Localized incorporation of outer membrane components in the pathogen Brucella abortus.
Vassen, Victoria; Valotteau, Claire; Feuillie, Cécile; Formosa-Dague, Cécile; Dufrêne, Yves F; De Bolle, Xavier.
Afiliación
  • Vassen V; Research Unit in Biology of Microorganisms (URBM), Narilis University of Namur (UNamur), Namur, Belgium.
  • Valotteau C; Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain (UCL), Louvain-la-Neuve, Belgium.
  • Feuillie C; Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain (UCL), Louvain-la-Neuve, Belgium.
  • Formosa-Dague C; Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain (UCL), Louvain-la-Neuve, Belgium.
  • Dufrêne YF; Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain (UCL), Louvain-la-Neuve, Belgium.
  • De Bolle X; Walloon Excellence in Life Sciences and Biotechnology (WELBIO), Wavre, Belgium.
EMBO J ; 38(5)2019 03 01.
Article en En | MEDLINE | ID: mdl-30635335
ABSTRACT
The zoonotic pathogen Brucella abortus is part of the Rhizobiales, which are alpha-proteobacteria displaying unipolar growth. Here, we show that this bacterium exhibits heterogeneity in its outer membrane composition, with clusters of rough lipopolysaccharide co-localizing with the essential outer membrane porin Omp2b, which is proposed to allow facilitated diffusion of solutes through the porin. We also show that the major outer membrane protein Omp25 and peptidoglycan are incorporated at the new pole and the division site, the expected growth sites. Interestingly, lipopolysaccharide is also inserted at the same growth sites. The absence of long-range diffusion of main components of the outer membrane could explain the apparent immobility of the Omp2b clusters, as well as unipolar and mid-cell localizations of newly incorporated outer membrane proteins and lipopolysaccharide. Unipolar growth and limited mobility of surface structures also suggest that new surface variants could arise in a few generations without the need of diluting pre-existing surface antigens.
Asunto(s)
Palabras clave

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Brucella abortus / Peptidoglicano / Lipopolisacáridos / Porinas / Membrana Externa Bacteriana Idioma: En Revista: EMBO J Año: 2019 Tipo del documento: Article País de afiliación: Bélgica

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Brucella abortus / Peptidoglicano / Lipopolisacáridos / Porinas / Membrana Externa Bacteriana Idioma: En Revista: EMBO J Año: 2019 Tipo del documento: Article País de afiliación: Bélgica