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Journal of Bacteriology, July 2008, p. 4641-4647, Vol. 190, No. 13
0021-9193/08/$08.00+0     doi:10.1128/JB.00287-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Lipoprotein Signal Peptides Are Processed by Lsp and Eep of Streptococcus uberis{triangledown} ,{dagger}

E. L. Denham,1 P. N. Ward,2 and J. A. Leigh3*

Institute for Animal Health, Compton, Berkshire RG20 7NN, United Kingdom,1 Nuffield Department of Clinical Laboratory Sciences, Oxford University, John Radcliffe Hospital, Headington OX3 9DU, United Kingdom,2 School of Veterinary Medicine and Science, University of Nottingham, Sutton Bonington, Leicestershire LE12 5RD, United Kingdom3

Received 26 February 2008/ Accepted 27 April 2008

Lipoprotein signal peptidase (lsp) is responsible for cleaving the signal peptide sequence of lipoproteins in gram-positive bacteria. Investigation of the role of Lsp in Streptococcus uberis, a common cause of bovine mastitis, was undertaken using the lipoprotein MtuA (a protein essential for virulence) as a marker. The S. uberis lsp mutant phenotype displayed novel lipoprotein processing. Not only was full-length (uncleaved) MtuA detected by Western blotting, but during late log phase, a lower-molecular-weight derivative of MtuA was evident. Similar analysis of an S. uberis double mutant containing insertions disrupting both lsp and eep (a homologue of the Enterococcus faecalis "enhanced expression of pheromone" gene) indicated a role for eep in cleavage of lipoproteins in the absence of Lsp. Such a function may indicate a role for eep in maintenance of secretion pathways during disruption of normal lipoprotein processing.

* Corresponding author. Mailing address: School of Veterinary Medicine and Science, University of Nottingham, Sutton Bonington, Leicestershire LE12 5RD, United Kingdom. Phone: 44 7743 451 125. E-mail: james.leigh{at}nottingham.ac.uk

{triangledown} Published ahead of print on 9 May 2008.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, July 2008, p. 4641-4647, Vol. 190, No. 13
0021-9193/08/$08.00+0     doi:10.1128/JB.00287-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Das, S., Kanamoto, T., Ge, X., Xu, P., Unoki, T., Munro, C. L., Kitten, T. (2009). Contribution of Lipoproteins and Lipoprotein Processing to Endocarditis Virulence in Streptococcus sanguinis. J. Bacteriol. 191: 4166-4179 [Abstract] [Full Text]  
  • Bray, B. A., Sutcliffe, I. C., Harrington, D. J. (2009). Impact of lgt mutation on lipoprotein biosynthesis and in vitro phenotypes of Streptococcus agalactiae. Microbiology 155: 1451-1458 [Abstract] [Full Text]  
  • Denham, E. L., Ward, P. N., Leigh, J. A. (2009). In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp. Microbiology 155: 134-141 [Abstract] [Full Text]  


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