RrgA and RrgB Are Components of a Multisubunit Pilus Encoded by the Streptococcus pneumoniae rlrA Pathogenicity Islet

The rlrA pathogenicity islet in Streptococcus pneumoniae TIGR4 encodes three surface proteins, RrgA, RrgB, and RrgC, and three sortase enzymes. Using transmission electron microscopy, cell fractionation, cell wall sorting signal domain swapping, and Western blotting, we show that RrgA and RrgB are i...

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Published inInfection and Immunity Vol. 74; no. 4; pp. 2453 - 2456
Main Authors LeMieux, Julianna, Hava, David L, Basset, Alan, Camilli, Andrew
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.04.2006
Subjects
Aminoacyltransferases - genetics
Aminoacyltransferases - physiology
Bacterial Proteins - genetics
Bacterial Proteins - physiology
Bacteriology
Biological and medical sciences
Cysteine Endopeptidases - genetics
Cysteine Endopeptidases - physiology
Fimbriae Proteins - chemistry
Fimbriae Proteins - genetics
Fimbriae Proteins - immunology
Fimbriae, Bacterial - enzymology
Fimbriae, Bacterial - genetics
Fimbriae, Bacterial - ultrastructure
Fundamental and applied biological sciences. Psychology
Genomic Islands - genetics
Genomic Islands - immunology
Microbiology
Microscopy, Electron, Transmission
Miscellaneous
Molecular Pathogenesis
Protein Structure, Tertiary - genetics
Streptococcus pneumoniae
Streptococcus pneumoniae - enzymology
Streptococcus pneumoniae - genetics
Streptococcus pneumoniae - immunology
Streptococcus pneumoniae - pathogenicity
Virulence Factors - chemistry
Virulence Factors - genetics
Virulence Factors - immunology
Pathogenicity
Streptococcaceae
Microbiology
Bacteria
Micrococcales
Pilus
Immunity
Streptococcus pneumoniae
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Summary:The rlrA pathogenicity islet in Streptococcus pneumoniae TIGR4 encodes three surface proteins, RrgA, RrgB, and RrgC, and three sortase enzymes. Using transmission electron microscopy, cell fractionation, cell wall sorting signal domain swapping, and Western blotting, we show that RrgA and RrgB are incorporated into a multisubunit pilus in S. pneumoniae.
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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@tufts.edu.
Editor: V. J. DiRita
Present address: Lymphocyte Biology Section, Brigham and Women's Hospital, Harvard Medical School, 1 Jimmy Fund Way, Boston, MA 02115.
Present address: Department of Infectious Disease, Children's Hospital, 300 Longwood Avenue, Boston, MA 02115.
ISSN:0019-9567
1098-5522
DOI:10.1128/IAI.74.4.2453-2456.2006