Sharon A. Egan
Identification of sortase A (SrtA) substrates in Streptococcus uberis: evidence for an additional hexapeptide (LPXXXD) sorting motif
Egan, Sharon A.; Kurian, Dominic; Ward, Philip N.; Hunt, Lawrence; Leigh, James A.
Philip N. Ward
James A. Leigh
Sortase (a transamidase) has been shown to be responsible for the covalent attachment of proteins to the bacterial cell wall. Anchoring is effected on secreted proteins containing a specific cell wall motif toward their C-terminus; that for sortase A (SrtA) in Gram-positive bacteria often incorporates the sequence LPXTG. Such surface proteins are often characterized as virulence determinants and play important roles during the establishment and persistence of infection. Intramammary infection with Streptococcus uberis is a common cause of bovine mastitis, which impacts on animal health and welfare and the economics of milk production. Comparison of stringently produced cell wall fractions from S. uberis and an isogenic mutant strain lacking SrtA permitted identification of 9 proteins likely to be covalently anchored at the cell surface. Analysis of these sequences implied the presence of two anchoring motifs for S. uberis, the classical LPXTG motif and an additional LPXXXD motif.
|Journal Article Type||Article|
|Publication Date||Dec 29, 2009|
|Journal||Journal of Proteome Research|
|Publisher||American Chemical Society|
|Peer Reviewed||Peer Reviewed|
|APA6 Citation||Egan, S. A., Kurian, D., Ward, P. N., Hunt, L., & Leigh, J. A. (2009). Identification of sortase A (SrtA) substrates in Streptococcus uberis: evidence for an additional hexapeptide (LPXXXD) sorting motif. Journal of Proteome Research, 9(2), doi:10.1021/pr901025w|
|Keywords||Sortase A, LPXTG, Cell wall proteins, Mastitis, Streptococcus uberis|
|Copyright Statement||Copyright information regarding this work can be found at the following address: http://eprints.nottingh.../end_user_agreement.pdf|
|Additional Information||This document is the unedited author's version of a submitted work that was subsequently accepted for publication in the Journal of Proteome Research, copyright American Chemical Society. To access the final edited and published work see http://pubs.acs.org/doi/abs/10.1021/pr901025w|
Copyright information regarding this work can be found at the following address: http://eprints.nottingham.ac.uk/end_user_agreement.pdf