ArticleInfection and immunity2014
Structural conservation, variability, and immunogenicity of the T6 backbone pilin of serotype M6 Streptococcus pyogenes.
Article in Infection and immunity, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 37 citations in OpenAlex.
- Immunogenicity of Type IV Pilin Proteins fromMicroorganisms · 2025Article
- Group A Streptococcus Pili-Roles in Pathogenesis and Potential for Vaccine Development.Microorganisms · 2024Review
- The basal and major pilins in the Corynebacterium diphtheriae SpaA pilus adopt similar structures that competitively react with the pilin polymerase.Biopolymers · 2024Article
- Identification of an immunodominant region on a group AVirulence · 2023Article
- Analysis of FctB3 crystal structure and insight into its structural stabilization and pilin linkage mechanisms.Archives of microbiology · 2023Article
- Pilus proteins from Streptococcus pyogenes stimulate innate immune responses through Toll-like receptor 2.Immunology and cell biology · 2022Article
- A multivalent T-antigen-based vaccine for Group A Streptococcus.Scientific reports · 2021Article
- Review
- Genetics, Structure, and Function of Group A Streptococcal Pili.Frontiers in microbiology · 2021Review
- Group AInfection and immunity · 2019Article
- Vaccine Approaches To Protect against Group A Streptococcal Pharyngitis.Microbiology spectrum · 2019Review
- Identification and Characterization of Serotype-Specific Variation in Group A Streptococcus Pilus Expression.Infection and immunity · 2018Article
- Bent conformation of a backbone pilin N-terminal domain supports a three-stage pilus assembly mechanism.Communications biology · 2018Article
- Mucosal vaccination with pili from Group A Streptococcus expressed on Lactococcus lactis generates protective immune responses.Scientific reports · 2017Article
- The "Lid" in the Streptococcus pneumoniae SrtC1 Sortase Adopts a Rigid Structure that Regulates Substrate Access to the Active Site.The journal of physical chemistry. B · 2016Article
- Tissue tropisms in group A Streptococcus: what virulence factors distinguish pharyngitis from impetigo strains?Current opinion in infectious diseases · 2016Review
- Serological Evidence of Immune Priming by Group A Streptococci in Patients with Acute Rheumatic Fever.Frontiers in microbiology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Group A streptococcus (GAS; Streptococcus pyogenes) is a Gram-positive human pathogen that causes a broad range of diseases ranging from acute pharyngitis to the poststreptococcal sequelae of acute rheumatic fever. GAS pili are highly diverse, long protein polymers that extend from the cell surface. They have multiple roles in infection and are promising candidates for vaccine development. This study describes the structure of the T6 backbone pilin (BP; Lancefield T-antigen) from the important M6 serotype. The structure reveals a modular arrangement of three tandem immunoglobulin-like domains, two with internal isopeptide bonds. The T6 pilin lysine, essential for polymerization, is located in a novel VAKS motif that is structurally homologous to the canonical YPKN pilin lysine in other three- and four-domain Gram-positive pilins. The T6 structure also highlights a conserved pilin core whose surface is decorated with highly variable loops and extensions. Comparison to other Gram-positive BPs shows that many of the largest variable extensions are found in conserved locations. Studies with sera from patients diagnosed with GAS-associated acute rheumatic fever showed that each of the three T6 domains, and the largest of the variable extensions (V8), are targeted by IgG during infection in vivo. Although the GAS BP show large variations in size and sequence, the modular nature of the pilus proteins revealed by the T6 structure may aid the future design of a pilus-based vaccine.
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