Mode of Expression and Functional Characterization of FCT-3 Pilus Region-Encoded Proteins in Streptococcus pyogenes Serotype M49

  title={Mode of Expression and Functional Characterization of FCT-3 Pilus Region-Encoded Proteins in Streptococcus pyogenes Serotype M49},
  author={Masanobu Nakata and Thomas Köller and Karin Moritz and Deborah A. Ribardo and Ludwig Jonas and Kevin S. McIver and Tomoko Sumitomo and Yutaka Terao and Shigetada Kawabata and Andreas Podbielski and Bernd Kreikemeyer},
  journal={Infection and Immunity},
  pages={32 - 44}
ABSTRACT The human pathogen Streptococcus pyogenes (group A streptococcus [GAS]) pilus components, suggested to play a role in pathogenesis, are encoded in the variable FCT (fibronectin- and collagen-binding T-antigen) region. We investigated the functions of sortase A (SrtA), sortase C2 (SrtC2), and the FctA protein of the most prevalent type 3 FCT region from a serotype M49 strain. Although it is considered a housekeeping sortase, SrtA's activity is involved in pilus formation in addition to… 
Assembly Mechanism of FCT Region Type 1 Pili in Serotype M6 Streptococcus pyogenes*
Investigation of the assembly mechanism of FCT type 1 pili in a serotype M6 strain found that T6 encompasses the novel VAKS pilin motif conserved in streptococcal T6 homologues and that the lysine residue (Lys-175) within the motif and cell wall sorting signal of T6 are prerequisites for isopeptide linkage of T 6 molecules.
Involvement of T6 Pili in Biofilm Formation by Serotype M6 Streptococcus pyogenes
Findings indicate that assembled FCT type 1 pili contribute to biofilm formation and also function as attenuators of bacterial aggregation in serotype M1 strain SF370.
Structure and Activity of Streptococcus pyogenes SipA: A Signal Peptidase-Like Protein Essential for Pilus Polymerisation
It is proposed that SipA functions by binding a key component at the bacterial cell surface, in a conformation that facilitates pilus assembly, and that SIPA function is likely to be conserved in all S. pyogenes strains.
The Group A Streptococcus serotype M2 pilus plays a role in host cell adhesion and immune evasion
It is shown that, unlike other GAS pili, the FCT‐6 pilus also contributes to immune evasion and was demonstrated by a delay in blood clotting, increased intracellular survival of the bacteria in macrophages, higher bacterial survival rates in human whole blood and greater virulence in a Galleria mellonella infection model in the presence of fully assembled F CT‐6 pili.
An arm-swapped dimer of the Streptococcus pyogenes pilin specific assembly factor SipA.
Genetics, Structure, and Function of Group A Streptococcal Pili
The current state of the art regarding GAS pili is summarized, including a new mode of host-GAS interaction mediated by pili, along with insights into pilus expression in terms of tissue tropism.
Mutations in the Gene Encoding the Ancillary Pilin Subunit of the Streptococcus suis srtF Cluster Result in Pili Formed by the Major Subunit Only
Since the highly virulent strains under investigation are unlikely to produce other pili, the results suggest that pili might be dispensable for critical steps of the S. suis pathogenesis of infection.
Structural Conservation, Variability, and Immunogenicity of the T6 Backbone Pilin of Serotype M6 Streptococcus pyogenes
Although the GAS BP show large variations in size and sequence, the modular nature of the pilus proteins revealed by the T6 structure may aid the future design of a pilus-based vaccine.
Linkage of T3 and Cpa pilins in the Streptococcus pyogenes M3 pilus
The residues involved in their linkage are investigated and it is shown that linkage of Cpa to T3 by the sortase family transpeptidase SrtC2 requires the VPPTG motif in the cell wall‐sorting signal of CPA, suggesting that Cpa is located exclusively at the pilus tip, a location supported by immunogold electron microscopy.


Molecular Characterization of a Novel Fibronectin-binding Protein of Streptococcus pyogenesStrains Isolated from Toxic Shock-like Syndrome Patients*
A novel Fn-binding protein of group A streptococcus serotype M3 and M18 strains isolated from patients with toxic shock-like syndrome (TSLS) is presented, and it is suggested that FbaB is etiologically involved in the development of invasive Streptococcal diseases.
Assembly and role of pili in group B streptococci
This study provides the first evidence that adhesive pili are also present in Gram‐positive pathogens.
Differential Recognition of Surface Proteins in Streptococcus pyogenes by Two Sortase Gene Homologs
It is concluded that srtA and srtB encode sortase enzymes required for anchoring different subsets of proteins to the cell wall, and it seems likely that the multiple sortase homologs in the genomes of other gram-positive bacteria have a similar substrate-specific role.
A Novel Sortase, SrtC2, from Streptococcus pyogenes Anchors a Surface Protein Containing a QVPTGV Motif to the Cell Wall
It is concluded that srtC encodes a novel sortase that anchors a protein containing a QVPTGV motif to the surface of GAS.
Genomic Localization of a T Serotype Locus to a Recombinatorial Zone Encoding Extracellular Matrix-Binding Proteins in Streptococcus pyogenes
The data provide evidence that the highly recombinatorial FCT region of the S. pyogenes genome is under strong selection for change in response to the host environment.
Role of Streptococcal T Antigens in Superficial Skin Infection
The findings suggest that both FctA and Cpa are required for pilus formation, but importantly, an intact pilus is not essential for Cpa-mediated virulence, and reveal that a pilus-like structure is notessential for the most common form of streptococcal skin disease.
The intracellular status of Streptococcus pyogenes: role of extracellular matrix-binding proteins and their regulation.
Heterogeneity in the Polarity of Nra Regulatory Effects on Streptococcal Pilus Gene Transcription and Virulence
Key strain-specific differences in the transcriptional circuitry governing virulence gene expression in S. pyogenes are demonstrated and a lack of detectable Nra effects on M protein- and SpeB-dependent phenotypes is supported.
PlyC, a novel bacteriophage lysin for compartment‐ dependent proteomics of group A streptococci
PlyC is superior for cell wall protein extraction compared to mutanolysin due to its higher activity and specificity as an N‐acetylmuramoyl‐L‐alanine amidase and the experimental design allowed the actual localization of the proteins despite contamination with intracellular proteins.
Group A Streptococcus produce pilus-like structures containing protective antigens and Lancefield T antigens
  • M. MoraG. Bensi J. Telford
  • Biology, Medicine
    Proceedings of the National Academy of Sciences of the United States of America
  • 2005
It is reported that Group A Streptococcus, a Gram-positive human-specific pathogen that causes pharyngitis, impetigo, invasive disease, necrotizing fasciitis, and autoimmune sequelae has long, surface-exposed, pilus-like structures composed of members of a family of extracellular matrix-binding proteins.