ArticleProceedings of the National Academy of Sciences of the United States of America2010
Elongated fibrillar structure of a streptococcal adhesin assembled by the high-affinity association of alpha- and PPII-helices.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 95 citations in OpenAlex.
- TargetingACS medicinal chemistry letters · 2026Article
- PolyProline Predictor: A web server for empirical sequence-based prediction of polyproline II helices.Protein science : a publication of the Protein Society · 2026Article
- The structure ofInfection and immunity · 2026Article
- Normoxic stress enhance the secretion of adhesion-promoting membrane vesicles byJournal of oral microbiology · 2026Article
- Backbone NMR resonance assignments for the C2 domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2025Article
- Antibacterial and Antibiofilm Potential of Chlorophyllin AgainstAntibiotics (Basel, Switzerland) · 2024Article
- Proline, a unique amino acid whose polymer, polyproline II helix, and its analogues are involved in many biological processes: a review.Amino acids · 2024Review
- Virtual Screening of Inhibitors ofACS medicinal chemistry letters · 2024Article
- Refolding, Crystallization, and Crystal Structure Analysis of a Scavenger Receptor Cysteine-Rich Domain of Human Salivary Agglutinin Expressed in Escherichia coli.The protein journal · 2024Article
- Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1.Biomolecular NMR assignments · 2023Article
- Domain shuffling of a highly mutable ligand-binding fold drives adhesin generation across the bacterial kingdom.Proteins · 2023Article
- Article
- Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.Microbiology spectrum · 2022Article
- Targeting the BspC-vimentin interaction to develop anti-virulence therapies during Group B streptococcal meningitis.PLoS pathogens · 2022Article
- Structure-Function Characterization of Streptococcus intermedius Surface Antigen Pas.Journal of bacteriology · 2021Article
- Structural and functional analysis of the C-terminal region of Streptococcus gordonii SspB.Acta crystallographica. Section D, Structural biology · 2021Article
- Collagen Binding Proteins of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- In Silico Selection and In Vitro Evaluation of New Molecules That Inhibit the Adhesion ofInternational journal of molecular sciences · 2020Article
- Characterization of an intermolecular quaternary interaction between discrete segments of the Streptococcus mutans adhesin P1 by NMR spectroscopy.The FEBS journal · 2020Article
- The streptococcal multidomain fibrillar adhesin CshA has an elongated polymeric architecture.The Journal of biological chemistry · 2020Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Streptococcus mutans antigen I/II (AgI/II) is a cell surface-localized protein adhesin that interacts with salivary components within the salivary pellicle. AgI/II contributes to virulence and has been studied as an immunological and structural target, but a fundamental understanding of its underlying architecture has been lacking. Here we report a high-resolution (1.8 A) crystal structure of the A(3)VP(1) fragment of S. mutans AgI/II that demonstrates a unique fibrillar form (155 A) through the interaction of two noncontiguous regions in the primary sequence. The A(3) repeat of the alanine-rich domain adopts an extended alpha-helix that intertwines with the P(1) repeat polyproline type II (PPII) helix to form a highly extended stalk-like structure heretofore unseen in prokaryotic or eukaryotic protein structures. Velocity sedimentation studies indicate that full-length AgI/II that contains three A/P repeats extends over 50 nanometers in length. Isothermal titration calorimetry revealed that the high-affinity association between the A(3) and P(1) helices is enthalpically driven. Two distinct binding sites on AgI/II to the host receptor salivary agglutinin (SAG) were identified by surface plasmon resonance (SPR). The current crystal structure reveals that AgI/II family proteins are extended fibrillar structures with the number of alanine- and proline-rich repeats determining their length.
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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.