ArticleInfection and immunity2014
SpyAD, a moonlighting protein of group A Streptococcus contributing to bacterial division and host cell adhesion.
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 23 papers.
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Who cites it
23 citing papers in PubMed, 28 citations in OpenAlex.
- A staged clinical development and evidence-generation framework for Group A Streptococcus vaccines.NPJ vaccines · 2026Review
- Rational selection of antigenic targets for Group A Streptococcus vaccine: updates, challenges and opportunities.NPJ vaccines · 2026Review
- Group A Streptococcal Virulence Factors and Vaccine Development-An Update.Microorganisms · 2026Review
- Comparative genomics andFrontiers in microbiology · 2026Article
- Article
- Current Progress in the Development of mRNA Vaccines Against Bacterial Infections.International journal of molecular sciences · 2024Review
- Proteomic approach to identify host cell attachment proteins provides protective Pseudomonas aeruginosa vaccine antigen FtsZ.NPJ vaccines · 2024Article
- Genomic analysis of conjugative and chromosomally integrated mobile genetic elements in oral streptococci.Applied and environmental microbiology · 2024Article
- Serological Responses toOpen forum infectious diseases · 2024Article
- Article
- The Streptococcus pyogenes vaccine landscape.NPJ vaccines · 2023Review
- Development and Characterisation of a Four-Plex Assay to MeasureMethods and protocols · 2022Article
- XRE family transcriptional regulator XtrSs modulates Streptococcus suis fitness under hydrogen peroxide stress.Archives of microbiology · 2022Article
- Site-Specific Conjugation of Cell Wall Polyrhamnose to Protein SpyAD Envisioning a Safe Universal Group A Streptococcal Vaccine.Infectious microbes & diseases · 2021Article
- Rational Design of a Glycoconjugate Vaccine against Group AInternational journal of molecular sciences · 2020Article
- Streptococcus pyogenes genes that promote pharyngitis in primates.JCI insight · 2020Article
- Genome-Wide Screens Identify Group A Streptococcus Surface Proteins Promoting Female Genital Tract Colonization and Virulence.The American journal of pathology · 2020Article
- Article
- The N-terminal domain of the R28 protein promotesThe Journal of biological chemistry · 2018Article
- Prospective Longitudinal Analysis of Immune Responses in Pediatric Subjects After Pharyngeal Acquisition of Group A Streptococci.Journal of the Pediatric Infectious Diseases Society · 2017Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Group A streptococcus (GAS) is a human pathogen causing a wide repertoire of mild and severe diseases for which no vaccine is yet available. We recently reported the identification of three protein antigens that in combination conferred wide protection against GAS infection in mice. Here we focused our attention on the characterization of one of these three antigens, Spy0269, a highly conserved, surface-exposed, and immunogenic protein of unknown function. Deletion of the spy0269 gene in a GAS M1 isolate resulted in very long bacterial chains, which is indicative of an impaired capacity of the knockout mutant to properly divide. Confocal microscopy and immunoprecipitation experiments demonstrated that the protein was mainly localized at the cell septum and could interact in vitro with the cell division protein FtsZ, leading us to hypothesize that Spy0269 is a member of the GAS divisome machinery. Predicted structural domains and sequence homologies with known streptococcal adhesins suggested that this antigen could also play a role in mediating GAS interaction with host cells. This hypothesis was confirmed by showing that recombinant Spy0269 could bind to mammalian epithelial cells in vitro and that Lactococcus lactis expressing Spy0269 on its cell surface could adhere to mammalian cells in vitro and to mice nasal mucosa in vivo. On the basis of these data, we believe that Spy0269 is involved both in bacterial cell division and in adhesion to host cells and we propose to rename this multifunctional moonlighting protein as SpyAD (Streptococcus pyogenes Adhesion and Division protein).
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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.