ArticlePloS one2014
Structure and activity of Streptococcus pyogenes SipA: a signal peptidase-like protein essential for pilus polymerisation.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- The Role of the Omega Subzone in Determining the Membership of a Protein in One of the Two Families of the LexA/Signal Peptidase-like Superfamily.International journal of molecular sciences · 2026Article
- Structural and functional insights of sortases and their interactions with antivirulence compounds.Current research in structural biology · 2024Review
- Analysis of FctB3 crystal structure and insight into its structural stabilization and pilin linkage mechanisms.Archives of microbiology · 2023Article
- Genetics, Structure, and Function of Group A Streptococcal Pili.Frontiers in microbiology · 2021Review
- PilVax - a novel peptide delivery platform for the development of mucosal vaccines.Scientific reports · 2018Article
- Pilus biogenesis of Gram-positive bacteria: Roles of sortases and implications for assembly.Protein science : a publication of the Protein Society · 2017Review
- A Type I Signal Peptidase Is Required for Pilus Assembly in the Gram-Positive, Biofilm-Forming Bacterium Actinomyces oris.Journal of bacteriology · 2016Article
- The N-Terminal GYPSY Motif Is Required for Pilin-Specific Sortase SrtC1 Functionality in Lactobacillus rhamnosus Strain GG.PloS one · 2016Article
- A structural snapshot of type II pilus formation in Streptococcus pneumoniae.The Journal of biological chemistry · 2015Article
- The small regulatory RNA FasX enhances group A Streptococcus virulence and inhibits pilus expression via serotype-specific targets.Molecular microbiology · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pili expressed on the surface of the human pathogen Streptococcus pyogenes play an important role in host cell attachment, colonisation and pathogenesis. These pili are built from two or three components, an adhesin subunit at the tip, a major pilin that forms a polymeric shaft, and a basal pilin that is attached to the cell wall. Assembly is carried out by specific sortase (cysteine transpeptidase) enzyme. These components are encoded in a small gene cluster within the S. pyogenes genome, often together with another protein, SipA, whose function is unknown. We show through functional assays, carried out by expressing the S. pyogenes pilus components in Lactococcus lactis, SipA from the clinically important M1T1 strain is essential for pilus assembly, and that SipA function is likely to be conserved in all S. pyogenes. From the crystal structure of SipA we confirm that SipA belongs to the family of bacterial signal peptidases (SPases), which process the signal-peptides of secreted proteins. In contrast to a previous arm-swapped SipA dimer, this present structure shows that its principal domain closely resembles the catalytic domain of SPases and has a very similar peptide-binding cleft, but it lacks the catalytic Ser and Lys residues characteristic of SPases. In SipA these are replaced by Asp and Gly residues, which play no part in activity. We propose that SipA functions by binding a key component at the bacterial cell surface, in a conformation that facilitates pilus assembly.
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