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Journal of Bacteriology, May 2009, p. 3237-3247, Vol. 191, No. 10
0021-9193/09/$08.00+0     doi:10.1128/JB.01837-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Mechanism for Sortase Localization and the Role of Sortase Localization in Efficient Pilus Assembly in Enterococcus faecalis{triangledown} ,{dagger}

Kimberly A. Kline,1,{ddagger} Andrew L. Kau,1,{ddagger},§ Swaine L. Chen,1 Adeline Lim,1 Jerome S. Pinkner,1 Jason Rosch,1,¶ Sreedhar R. Nallapareddy,2 Barbara E. Murray,2 Birgitta Henriques-Normark,3 Wandy Beatty,1 Michael G. Caparon,1* and Scott J. Hultgren1*

Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110,1 Division of Infectious Diseases, Department of Internal Medicine, University of Texas Medical School at Houston, Houston, Texas 77030,2 Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Solna, Sweden3

Received 31 December 2008/ Accepted 6 March 2009

Pathogenic streptococci and enterococci primarily rely on the conserved secretory (Sec) pathway for the translocation and secretion of virulence factors out of the cell. Since many secreted virulence factors in gram-positive organisms are subsequently attached to the bacterial cell surface via sortase enzymes, we sought to investigate the spatial relationship between secretion and cell wall attachment in Enterococcus faecalis. We discovered that sortase A (SrtA) and sortase C (SrtC) are colocalized with SecA at single foci in the enterococcus. The SrtA-processed substrate aggregation substance accumulated in single foci when SrtA was deleted, implying a single site of secretion for these proteins. Furthermore, in the absence of the pilus-polymerizing SrtC, pilin subunits also accumulate in single foci. Proteins that localized to single foci in E. faecalis were found to share a positively charged domain flanking a transmembrane helix. Mutation or deletion of this domain in SrtC abolished both its retention at single foci and its function in efficient pilus assembly. We conclude that this positively charged domain can act as a localization retention signal for the focal compartmentalization of membrane proteins.

* Corresponding authors. Mailing address: Department of Molecular Microbiology, Washington University School of Medicine, 660 S. Euclid Ave., Campus Box 8230, Saint Louis, MO 63110-1093. Phone: (314) 362-6772. Fax: (314) 362-1998. E-mail for Michael G. Caparon: caparon{at}borcim.wustl.edu. E-mail for Scott J. Hultgren: hultgren{at}borcim.wustl.edu

{triangledown} Published ahead of print on 13 March 2009.

{dagger} Supplemental material for this article is available at http://jb.asm.org/.

{ddagger} K.A.K. and A.L.K. contributed equally to this work.

§ Present address: Department of Allergy and Immunology, Washington University School of Medicine, St. Louis, MO 63110.

Present address: Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, TN 38105.

Journal of Bacteriology, May 2009, p. 3237-3247, Vol. 191, No. 10
0021-9193/09/$08.00+0     doi:10.1128/JB.01837-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Guttilla, I. K., Gaspar, A. H., Swierczynski, A., Swaminathan, A., Dwivedi, P., Das, A., Ton-That, H. (2009). Acyl Enzyme Intermediates in Sortase-Catalyzed Pilus Morphogenesis in Gram-Positive Bacteria. J. Bacteriol. 191: 5603-5612 [Abstract] [Full Text]  
  • Guiton, P. S., Hung, C. S., Kline, K. A., Roth, R., Kau, A. L., Hayes, E., Heuser, J., Dodson, K. W., Caparon, M. G., Hultgren, S. J. (2009). Contribution of Autolysin and Sortase A during Enterococcus faecalis DNA-Dependent Biofilm Development. Infect. Immun. 77: 3626-3638 [Abstract] [Full Text]  


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