ArticleThe Journal of biological chemistry2015
A structural snapshot of type II pilus formation in Streptococcus pneumoniae.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Pilus ofFrontiers in cellular and infection microbiology · 2023Review
- The prevalence of pilus islets inAccess microbiology · 2021Article
- 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
- A comprehensive in silico analysis of sortase superfamily.Journal of microbiology (Seoul, Korea) · 2019Article
- Bent conformation of a backbone pilin N-terminal domain supports a three-stage pilus assembly mechanism.Communications biology · 2018Article
- A plasmid from an Antarctic haloarchaeon uses specialized membrane vesicles to disseminate and infect plasmid-free cells.Nature microbiology · 2017Article
- Molecular characterization of Streptococcus pneumoniae, particularly serotype19A/ST320, which emerged in Krasnoyarsk, Russia.Microbiology and immunology · 2017Article
- Pilus biogenesis of Gram-positive bacteria: Roles of sortases and implications for assembly.Protein science : a publication of the Protein Society · 2017Review
- Sortase Transpeptidases: Structural Biology and Catalytic Mechanism.Advances in protein chemistry and structural biology · 2017Review
- Discovery of Novel Leptospirosis Vaccine Candidates Using Reverse and Structural Vaccinology.Frontiers in immunology · 2017Article
- New insights about pilus formation in gut-adapted Lactobacillus rhamnosus GG from the crystal structure of the SpaA backbone-pilin subunit.Scientific reports · 2016Article
- Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pili are fibrous appendages expressed on the surface of a vast number of bacterial species, and their role in surface adhesion is important for processes such as infection, colonization, andbiofilm formation. The human pathogen Streptococcus pneumoniae expresses two different types of pili, PI-1 and PI-2, both of which require the concerted action of structural proteins and sortases for their polymerization. The type PI-1 streptococcal pilus is a complex, well studied structure, but the PI-2 type, present in a number of invasive pneumococcal serotypes, has to date remained less well understood. The PI-2 pilus consists of repeated units of a single protein, PitB, whose covalent association is catalyzed by cognate sortase SrtG-1 and partner protein SipA. Here we report the high resolution crystal structures of PitB and SrtG1 and use molecular modeling to visualize a "trapped" 1:1 complex between the two molecules. X-ray crystallography and electron microscopy reveal that the pneumococcal PI-2 backbone fiber is formed by PitB monomers associated in head-to-tail fashion and that short, flexible fibers can be formed even in the absence of coadjuvant proteins. These observations, obtained with a simple pilus biosynthetic system, are likely to be applicable to other fiber formation processes in a variety of Gram-positive organisms.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.