ArticleNature microbiology2016
Conserved patterns hidden within group A Streptococcus M protein hypervariability recognize human C4b-binding protein.
Article in Nature microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 31 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 61 citations in OpenAlex.
- Structural basis for collagen recognition by theeLife · 2025Article
- Higher-order structure and proteoforms of co-occurring C4b-binding protein assemblies in human serum.The EMBO journal · 2024Article
- Conservation of C4BP-binding sequence patterns in Streptococcus pyogenes M and Enn proteins.The Journal of biological chemistry · 2024Article
- Two noncompeting human neutralizing antibodies targeting MPXV B6 show protective effects against orthopoxvirus infections.Nature communications · 2024Article
- Review
- Diverse Functions of C4b-Binding Protein in Health and Disease.Journal of immunology (Baltimore, Md. : 1950) · 2023Review
- SIgA structures bound to Streptococcus pyogenes M4 and human CD89 provide insights into host-pathogen interactions.Nature communications · 2023Article
- Article
- The Hidden Side of Complement Regulator C4BP: Dissection and Evaluation of Its Immunomodulatory Activity.Frontiers in immunology · 2022Article
- Binding of the kringle-2 domain of human plasminogen to streptococcal PAM-type M-protein causes dissociation of PAM dimers.MicrobiologyOpen · 2021Article
- Streptococcus pyogenes Forms Serotype- and Local Environment-Dependent Interspecies Protein Complexes.mSystems · 2021Article
- Design of Broadly Cross-Reactive M Protein-Based Group A Streptococcal Vaccines.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Article
- Single-Cell Expression Landscape of SARS-CoV-2 ReceptorCancers · 2021Article
- Nonimmune antibody interactions of Group A Streptococcus M and M-like proteins.PLoS pathogens · 2021Review
- Subdominance in Antibody Responses: Implications for Vaccine Development.Microbiology and molecular biology reviews : MMBR · 2020Review
- Novel structure of the N-terminal helical domain of BibA, a group B streptococcus immunogenic bacterial adhesin.Acta crystallographica. Section D, Structural biology · 2020Article
- Structural proteomics, electron cryo-microscopy and structural modeling approaches in bacteria-human protein interactions.Medical microbiology and immunology · 2020Review
- Structure-based group A streptococcal vaccine design: Helical wheel homology predicts antibody cross-reactivity among streptococcal M protein-derived peptides.The Journal of biological chemistry · 2020Article
- Group A Streptococcal S Protein Utilizes Red Blood Cells as Immune Camouflage and Is a Critical Determinant for Immune Evasion.Cell reports · 2019Article
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
No vaccine exists against group A Streptococcus (GAS), a leading cause of worldwide morbidity and mortality. A severe hurdle is the hypervariability of its major antigen, the M protein, with >200 different M types known. Neutralizing antibodies typically recognize M protein hypervariable regions (HVRs) and confer narrow protection. In stark contrast, human C4b-binding protein (C4BP), which is recruited to the GAS surface to block phagocytic killing, interacts with a remarkably large number of M protein HVRs (apparently ∼90%). Such broad recognition is rare, and we discovered a unique mechanism for this through the structure determination of four sequence-diverse M proteins in complexes with C4BP. The structures revealed a uniform and tolerant 'reading head' in C4BP, which detected conserved sequence patterns hidden within hypervariability. Our results open up possibilities for rational therapies that target the M-C4BP interaction, and also inform a path towards vaccine design.
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What OpenQuestion holds
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.