|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 41, 38714-38722, October 11, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the The type III secretion system is used by
pathogenic Yersinia to translocate virulence factors
into the host cell. A key component is the multifunctional LcrV
protein, which is present on the bacterial surface prior to host cell
contact and up-regulates translocation by blocking the repressive
action of the LcrG protein on the cytosolic side of the secretion
apparatus. The functions of LcrV are proposed to involve
self-interactions (multimerization) and interactions with other
proteins including LcrG. Coiled-coil motifs predicted to be present are
thought to play a role in mediating these protein-protein interactions.
We have purified recombinant LcrV, LcrG, and site-directed mutants of
LcrV and demonstrated the structural integrity of these proteins using
circular dichroism spectroscopy. We show that LcrV interacts both with
itself and with LcrG and have obtained micromolar and nanomolar
affinities for these interactions, respectively. The effects of LcrV
mutations upon LcrG binding suggest that coiled-coil interactions
indeed play a significant role in complex formation. In addition,
comparisons of secretion patterns of effector proteins in
Yersinia, arising from wild type and mutants of LcrV,
support the proposed role of LcrG in titration of LcrV in
vivo but also suggest that other factors may be involved.
Interactions of the Type III Secretion Pathway Proteins LcrV and
LcrG from Yersinia pestis Are Mediated by Coiled-Coil
Domains*
,
,,, and**
Department of Biological Sciences, Centre
for Molecular Microbiology and Infection, Flowers Building, Imperial
College of Science, Technology and Medicine, London SW7 2AY, United
Kingdom, the § Department of Haematology, National Institute
for Biological Standards and Control, Blanche Lane, South Mimms,
Potters Bar, Hertfordshire EN6 3QG, United Kingdom, the ¶ School
of Crystallography, Birkbeck College, University of London, London WC1E
7HX, United Kingdom, and Defense Science and Technology
Laboratory, Chemical and Biological Sciences, Porton Down, Wiltshire
SP4 0JQ, United Kingdom
*
This work was supported by the UK Biotechnology and
Biological Sciences Research Council, UK Ministry of Defense, and
Defense Science and Technology Laboratory.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  G. Caroline, F. Eric, Y.-S. T. Bohn, E. Sylvie, and I. Attree Oligomerization of PcrV and LcrV, Protective Antigens of Pseudomonas aeruginosa and Yersinia pestis J. Biol. Chem., August 29, 2008; 283(35): 23940 - 23949. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Li and R. Yang Interaction between Yersinia pestis and the Host Immune System Infect. Immun., May 1, 2008; 76(5): 1804 - 1811. [Full Text] [PDF]
|
|
|
|
 |
|
 J. E. Broms, M. S. Francis, and A. Forsberg Diminished LcrV Secretion Attenuates Yersinia pseudotuberculosis Virulence J. Bacteriol., December 1, 2007; 189(23): 8417 - 8429. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. A. Hamad and M. L. Nilles Structure-Function Analysis of the C-Terminal Domain of LcrV from Yersinia pestis J. Bacteriol., September 15, 2007; 189(18): 6734 - 6739. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Johnson, P. Roversi, M. Espina, A. Olive, J. E. Deane, S. Birket, T. Field, W. D. Picking, A. J. Blocker, E. E. Galyov, et al. Self-chaperoning of the Type III Secretion System Needle Tip Proteins IpaD and BipD J. Biol. Chem., February 9, 2007; 282(6): 4035 - 4044. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 X. Yang, B. J. Hinnebusch, T. Trunkle, C. M. Bosio, Z. Suo, M. Tighe, A. Harmsen, T. Becker, K. Crist, N. Walters, et al. Oral Vaccination with Salmonella Simultaneously Expressing Yersinia pestis F1 and V Antigens Protects against Bubonic and Pneumonic Plague J. Immunol., January 15, 2007; 178(2): 1059 - 1067. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W. Swietnicki, S. O'Brien, K. Holman, S. Cherry, E. Brueggemann, J. E. Tropea, H. B. Hines, D. S. Waugh, and R. G. Ulrich Novel Protein-Protein Interactions of the Yersinia pestis Type III Secretion System Elucidated with a Matrix Analysis by Surface Plasmon Resonance and Mass Spectrometry J. Biol. Chem., September 10, 2004; 279(37): 38693 - 38700. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. R. Clarke, L. Cuthbertson, and C. Whitfield Nonreducing Terminal Modifications Determine the Chain Length of Polymannose O Antigens of Escherichia coli and Couple Chain Termination to Polymer Export via an ATP-binding Cassette Transporter J. Biol. Chem., August 20, 2004; 279(34): 35709 - 35718. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |