ArticlePloS one2015
Structure and assembly of group B streptococcus pilus 2b backbone protein.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- A novel pilus-associated gene cluster is implicated in Streptococcus agalactiae virulence.Veterinary research · 2025Article
- Immunization with Multiple Virulence Factors Provides Maternal and Neonatal Protection against Group B Streptococcus Serotypes.Vaccines · 2023Article
- Using Dried Blood Spots for a Sero-Surveillance Study of Maternally Derived Antibody against Group B Streptococcus.Vaccines · 2023Article
- Strategies to Prevent Early and Late-Onset Group BPathogens (Basel, Switzerland) · 2023Review
- Group B Streptococcal Colonization, Molecular Characteristics, and Epidemiology.Frontiers in microbiology · 2018Review
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- Bent conformation of a backbone pilin N-terminal domain supports a three-stage pilus assembly mechanism.Communications biology · 2018Article
- Pilus biogenesis of Gram-positive bacteria: Roles of sortases and implications for assembly.Protein science : a publication of the Protein Society · 2017Review
- Regulation of PI-2b Pilus Expression in Hypervirulent Streptococcus agalactiae ST-17 BM110.PloS one · 2017Article
- CnaA domains in bacterial pili are efficient dissipaters of large mechanical shocks.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Nanomechanical Properties of Lactococcus lactis Pili Are Conditioned by the Polymerized Backbone Pilin.PloS one · 2016Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Group B Streptococcus (GBS) is a major cause of invasive disease in infants. Like other Gram-positive bacteria, GBS uses a sortase C-catalyzed transpeptidation mechanism to generate cell surface pili from backbone and ancillary pilin precursor substrates. The three pilus types identified in GBS contain structural subunits that are highly immunogenic and are promising candidates for the development of a broadly-protective vaccine. Here we report the X-ray crystal structure of the backbone protein of pilus 2b (BP-2b) at 1.06Å resolution. The structure reveals a classical IgG-like fold typical of the pilin subunits of other Gram-positive bacteria. The crystallized portion of the protein (residues 185-468) encompasses domains D2 and D3 that together confer high stability to the protein due to the presence of an internal isopeptide bond within each domain. The D2+D3 region, lacking the N-terminal D1 domain, was as potent as the entire protein in conferring protection against GBS challenge in a well-established mouse model. By site-directed mutagenesis and complementation studies in GBS knock-out strains we identified the residues and motives essential for assembly of the BP-2b monomers into high-molecular weight complexes, thus providing new insights into pilus 2b polymerization.
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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.