The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles.
Many pathogenic bacteria use injectisomes to deliver effector proteins into host cells through type III secretion. Injectisomes consist of a basal body embedded in the bacterial membranes and a needle. In Yersinia, translocation of effectors requires the YopB and YopD proteins, which form a pore in the target cell membrane, and the LcrV protein, which assists the assembly of the pore. Here we report that LcrV forms a distinct structure at the tip of the needle, the tip complex. This unique localization of LcrV may explain its crucial role in the translocation process and its efficacy as the main protective antigen against plague.
Mueller
Catherine A
CA
Biozentrum der Universität Basel, Klingelbergstrasse 50-70, CH-4056, Basel, Switzerland.
Broz
Petr
P
Müller
Shirley A
SA
Ringler
Philippe
P
Erne-Brand
Françoise
F
Sorg
Isabel
I
Kuhn
Marina
M
Engel
Andreas
A
Cornelis
Guy R
GR
D000942:Antigens, Bacterial / Q000502:physiology / Q000648:ultrastructure*; D001425:Bacterial Outer Membrane Proteins / Q000502:physiology / Q000648:ultrastructure; D005816:Genetic Complementation Test; D008855:Microscopy, Electron, Scanning; D052899:Pore Forming Cytotoxic Proteins; D015008:Yersinia enterocolitica / Q000502:physiology / Q000648:ultrastructure*
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; C043908:LcrV protein, Yersinia; D052899:Pore Forming Cytotoxic Proteins; C078909:YopB protein, Yersinia; C078910:YopD protein, Yersinia