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Journal of Bacteriology, September 2008, p. 6002-6013, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00379-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Roles of the Sortases of Streptococcus pneumoniae in Assembly of the RlrA Pilus{triangledown}

Julianna LeMieux, Shauna Woody, and Andrew Camilli*

Howard Hughes Medical Institute and Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, Massachusetts 02111

Received 15 March 2008/ Accepted 27 June 2008

Pili have been observed on the surface of several gram-positive bacteria, including Streptococcus pneumoniae. The S. pneumoniae strain TIGR4 pilus is composed of three structural subunit proteins encoded in the rlrA pathogenicity islet, RrgA, RrgB, and RrgC. RrgB comprises the pilus backbone, RrgA is observed at intervals along surface pili, while RrgC is found in a loosely defined relationship with RrgA. We investigated the incorporation of each subunit into pili and the reliance of such placement on each of the other subunits. Both accessory subunits RrgA and RrgC are present in similar quantities in pili of all sizes. However, neither protein is required for the polymerization of RrgB, suggesting a nonessential role for RrgA and RrgC in the initiation of pilus assembly. Additionally, the rlrA islet encodes three sortases, SrtC-1, SrtC-2, and SrtC-3 (formerly SrtB, SrtC, and SrtD), which are divergent in sequence from the housekeeping sortase, SrtA. We determined the contributions of these four sortases to pilus assembly and found that SrtA is dispensable for pilus assembly and localization to the cell wall. Instead, SrtC-1, SrtC-2, and SrtC-3 are responsible for pilus assembly and exhibit functional redundancy with respect to backbone assembly and cell wall localization. A level of specificity and coordination among the class C sortases was revealed by the finding that SrtC-1 and SrtC-3 are required for the incorporation of the accessory subunits and by showing a deleterious effect on pilus assembly upon alteration of the cell wall sorting signals of the accessory subunit proteins.

* Corresponding author. Mailing address: Howard Hughes Medical Institute and Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Avenue, Boston, MA 02111. Phone: (617) 636-2144. Fax: (617) 636-2175. E-mail: andrew.camilli{at}tufts.edu

{triangledown} Published ahead of print on 7 July 2008.

Journal of Bacteriology, September 2008, p. 6002-6013, Vol. 190, No. 17
0021-9193/08/$08.00+0     doi:10.1128/JB.00379-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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