ArticleVeterinary research2025
Identification of the methionine transporter MetQ in Streptococcus suis and its contribution to virulence and biofilm formation.
Article in Veterinary research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers in PubMed.
- Pathogenicity and virulence ofVirulence · 2026Review
- Clinically relevant genomic and phenotypic differences in virulence, antimicrobial resistance, and biofilm-associated tolerance between Streptococcus suis lineages ST1 and ST123.Veterinary research · 2026Article
- Identification of immunostimulatory antigens in Group AProceedings of the National Academy of Sciences of the United States of America · 2026Article
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Authors and funding
7 authors.
Funding
Abstract
Streptococcus suis is a Gram-positive bacterium responsible for various infections in both pigs and humans. This study investigates the role of methionine acquisition in the growth and virulence of S. suis. The putative methionine transport system is organised as an operon comprising the metQ gene and genes encoding a transposase and an ATPase, forming a typical tripartite ABC transporter. This operon is conserved across multiple streptococcal species, including both animal and human pathogens. We examined whether MetQ functions as a methionine-binding protein and its role in bacterial infection. Using Western blotting and flow cytometry with a specific antiserum, we demonstrated that MetQ is produced in vitro by the S. suis reference strain P1/7 under methionine-limited conditions and is located on the bacterial cell surface. Growth assays in chemically defined media revealed that a metQ deletion mutant (P1/7∆metQ) exhibited impaired growth under methionine-restricted conditions but grew normally in a nutrient-rich medium, suggesting that MetQ primarily transports methionine. Isothermal Titration Calorimetry demonstrated that MetQ binds L-methionine with a dissociation constant (K
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