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Journal of Bacteriology, November 2008, p. 7315-7325, Vol. 190, No. 22
0021-9193/08/$08.00+0     doi:10.1128/JB.00861-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

YspM, a Newly Identified Ysa Type III Secreted Protein of Yersinia enterocolitica{triangledown}

Sarah E. Witowski,1 Kimberly A. Walker,1 and Virginia L. Miller1,2*

Departments of Molecular Microbiology,1 Pediatrics, Washington University School of Medicine, St. Louis, Missouri 631102

Received 24 June 2008/ Accepted 8 September 2008

Yersinia enterocolitica has three type three secretion systems, the flagellar, the plasmid Ysc type III secretion system (T3SS), and the chromosomal Ysa T3SS. The Ysc T3SS, through the proteins it secretes (Yops), prevents phagocytosis of Y. enterocolitica and is required for disease processes in the mouse host. Recent data demonstrate a role for the Ysa T3SS during initial colonization of the mouse via secretion of Ysps (Yersinia secreted proteins). This work characterizes the discovery of a newly identified Ysa type III secreted protein, YspM. Expression of yspM is regulated by temperature, NaCl concentration, and other known regulators of the ysa system. In addition, YspM is translocated into host cells via the Ysa T3SS. YspM is homologous to proteins classified as GDSL bacterial lipases, which possess a catalytic triad of amino acids (Ser, Asp, and His) located in three of five blocks of amino acid identity. Sequence analysis of the JB580v strain of Y. enterocolitica shows that, due to a premature stop codon, it no longer encodes the fifth block of amino acid identity containing the predicted catalytic histidine. However, seven other biotype 1B strains sequenced did possess the domain. A functional difference between the forms was revealed when YspM was expressed in Saccharomyces cerevisiae. Yeast growth was uninhibited when YspM from JB580v was expressed but greatly inhibited when YspM from Y295 (YspMY295) was expressed. Site-directed mutagenesis of the histidine of YspMY295 ablated the toxic effects. These results indicate that YspM is secreted by the Ysa T3SS and that, possibly due to lipase activity, it targets eukaryotic cellular component(s).

* Corresponding author. Present address: Department of Microbiology and Immunology, 116 Manning Drive, 804 Mary Ellen Jones CB# 7290, University of North Carolina, Chapel Hill, NC 27599. Phone: (919) 966-9956. Fax: (919) 962-8103. E-mail: vlmiller{at}med.unc.edu

{triangledown} Published ahead of print on 19 September 2008.

Journal of Bacteriology, November 2008, p. 7315-7325, Vol. 190, No. 22
0021-9193/08/$08.00+0     doi:10.1128/JB.00861-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Christen, M., Coye, L. H., Hontz, J. S., LaRock, D. L., Pfuetzner, R. A., Megha, , Miller, S. I. (2009). Activation of a Bacterial Virulence Protein by the GTPase RhoA. Sci Signal 2: ra71-ra71 [Abstract] [Full Text]  
  • Walker, K. A., Miller, V. L. (2009). Synchronous Gene Expression of the Yersinia enterocolitica Ysa Type III Secretion System and Its Effectors. J. Bacteriol. 191: 1816-1826 [Abstract] [Full Text]  
  • Matsumoto, H., Young, G. M. (2009). Essential Role of the SycP Chaperone in Type III Secretion of the YspP Effector. J. Bacteriol. 191: 1703-1715 [Abstract] [Full Text]  


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