Function and molecular architecture of the Yersinia injectisome tip complex.

Détails

ID Serval
serval:BIB_9A8CE65AE586
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Function and molecular architecture of the Yersinia injectisome tip complex.
Périodique
Molecular Microbiology
Auteur(s)
Broz P., Mueller C.A., Müller S.A., Philippsen A., Sorg I., Engel A., Cornelis G.R.
ISSN
0950-382X (Print)
ISSN-L
0950-382X
Statut éditorial
Publié
Date de publication
2007
Peer-reviewed
Oui
Volume
65
Numéro
5
Pages
1311-1320
Langue
anglais
Résumé
By quantitative immunoblot analyses and scanning transmission electron microscopy (STEM), we determined that the needle of the Yersinia enterocolitica E40 injectisome consists of 139 +/- 19 YscF subunits and that the tip complex is formed by three to five LcrV monomers. A pentamer represented the best fit for an atomic model of this complex. The N-terminal globular domain of LcrV forms the base of the tip complex, while the central globular domain forms the head. Hybrids between LcrV and its orthologues PcrV (Pseudomonas aeruginosa) or AcrV (Aeromonas salmonicida) were engineered and recombinant Y. enterocolitica expressing the different hybrids were tested for their capacity to form the translocation pore by a haemolysis assay. There was a good correlation between haemolysis, insertion of YopB into erythrocyte membranes and interaction between YopB and the N-terminal globular domain of the tip complex subunit. Hence, the base of the tip complex appears to be critical for the functional insertion of YopB into the host cell membrane.

Mots-clé
Antigens, Bacterial/chemistry, Antigens, Bacterial/genetics, Antigens, Bacterial/metabolism, Bacterial Proteins/chemistry, Bacterial Proteins/genetics, Bacterial Proteins/metabolism, Models, Molecular, Multiprotein Complexes, Pore Forming Cytotoxic Proteins/chemistry, Pore Forming Cytotoxic Proteins/genetics, Pore Forming Cytotoxic Proteins/metabolism, Protein Structure, Quaternary, Protein Subunits/chemistry, Protein Subunits/genetics, Protein Subunits/metabolism, Recombinant Fusion Proteins/chemistry, Recombinant Fusion Proteins/genetics, Recombinant Fusion Proteins/metabolism, Yersinia Infections/metabolism, Yersinia enterocolitica/pathogenicity, Yersinia enterocolitica/ultrastructure
Pubmed
Web of science
Open Access
Oui
Création de la notice
25/10/2017 11:05
Dernière modification de la notice
20/08/2019 16:01
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