ArticleActa crystallographica. Section D, Biological crystallography2013
Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- A novel pilus-associated gene cluster is implicated in Streptococcus agalactiae virulence.Veterinary research · 2025Article
- Determination of the Crystal Structure of the Cell Wall-Anchored Proteins and Pilins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Unmasking of the von Willebrand A-domain surface adhesin CglB at bacterial focal adhesions mediates myxobacterial gliding motility.Science advances · 2023Article
- Phylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins.Current research in microbial sciences · 2021Review
- LrpCBA pilus proteins of gut-dwelling Ligilactobacillus ruminis: crystallization and X-ray diffraction analysis.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Clostridium perfringens Produces an Adhesive Pilus Required for the Pathogenesis of Necrotic Enteritis in Poultry.Journal of bacteriology · 2021Article
- Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide.Communications biology · 2021Article
- Collagen Binding Proteins of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- Crystal structure of the atypically adhesive SpaB basal pilus subunit: Mechanistic insights about its incorporation in lactobacillar SpaCBA pili.Current research in structural biology · 2020Article
- The adhesive PitA pilus protein from the early dental plaque colonizer Streptococcus oralis: expression, purification, crystallization and X-ray diffraction analysis.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Sequence analysis and confirmation of the type IV pili-associated proteins PilY1, PilW and PilV in Acidithiobacillus thiooxidans.PloS one · 2019Article
- Discovery of a new Pro-Pro endopeptidase, PPEP-2, provides mechanistic insights into the differences in substrate specificity within the PPEP family.The Journal of biological chemistry · 2018Article
- Progress toward a group B streptococcal vaccine.Human vaccines & immunotherapeutics · 2018Article
- Pilus biogenesis of Gram-positive bacteria: Roles of sortases and implications for assembly.Protein science : a publication of the Protein Society · 2017Review
- Novel Molecular Insights about Lactobacillar Sortase-Dependent Piliation.International journal of molecular sciences · 2017Review
- Article
- Identification of a group B streptococcal fibronectin binding protein, SfbA, that contributes to invasion of brain endothelium and development of meningitis.Infection and immunity · 2014Article
- Structural model for covalent adhesion of the Streptococcus pyogenes pilus through a thioester bond.The Journal of biological chemistry · 2014Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
The crystal structure of a 75 kDa central fragment of GBS104, a tip pilin from the 2063V/R strain of Streptococcus agalactiae (group B streptococcus; GBS), is reported. In addition, a homology model of the remaining two domains of GBS104 was built and a model of full-length GBS104 was generated by combining the homology model (the N1 and N4 domains) and the crystal structure of the 75 kDa fragment (the N2 and N3 domains). This rod-shaped GBS104 model is constructed of three IgG-like domains (the N1, N2 and N4 domains) and one vWFA-like domain (the N3 domain). The N1 and N2 domains of GBS104 are assembled with distinct and remote segments contributed by the N- and C-termini. The metal-binding site in the N3 domain of GBS104 is in the closed/low-affinity conformation. Interestingly, this domain hosts two long arms that project away from the metal-binding site. Using site-directed mutagenesis, two cysteine residues that lock the N3 domain of GBS104 into the open/high-affinity conformation were introduced. Both wild-type and disulfide-locked recombinant proteins were tested for binding to extracellular matrix proteins such as collagen, fibronectin, fibrinogen and laminin, and an increase in fibronectin binding affinity was identified for the disulfide-locked N3 domain, suggesting that induced conformational changes may play a possible role in receptor binding.
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