000160898 001__ 160898
000160898 005__ 20251017144611.0
000160898 0247_ $$2doi$$a10.1186/s13567-025-01522-y
000160898 0248_ $$2sideral$$a144061
000160898 037__ $$aART-2025-144061
000160898 041__ $$aeng
000160898 100__ $$aBosch, Camila
000160898 245__ $$aIdentification of the methionine transporter MetQ in Streptococcus suis and its contribution to virulence and biofilm formation
000160898 260__ $$c2025
000160898 5060_ $$aAccess copy available to the general public$$fUnrestricted
000160898 5203_ $$aStreptococcus 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 (KD) of 7.1 µM. In a murine infection model, the metQ mutant showed reduced dissemination to internal organs compared to the wild type. Furthermore, the mutant showed decreased intracellular survival in murine macrophages and increased sensitivity to oxidative stress, while exhibited enhanced biofilm formation compared to the wild type. Our findings indicate that MetQ is essential for methionine uptake under methionine-restricted conditions, which is critical for bacterial nutrition, immune evasion, and pathogenicity during infection.
000160898 536__ $$9info:eu-repo/grantAgreement/ES/MICINN AEI PID2020-114617RB-100AEI-10.13039-501100011033
000160898 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttps://creativecommons.org/licenses/by/4.0/deed.es
000160898 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000160898 700__ $$aGarcía, Carla$$uUniversidad de Zaragoza
000160898 700__ $$aSaralegui, Luis$$uUniversidad de Zaragoza
000160898 700__ $$avan Beek, Lucille
000160898 700__ $$ade Jonge, Marien I.
000160898 700__ $$0(orcid)0000-0002-1974-9025$$aMarín, Clara
000160898 700__ $$0(orcid)0000-0002-8134-0693$$aArenas, Jesús$$uUniversidad de Zaragoza
000160898 7102_ $$11009$$2773$$aUniversidad de Zaragoza$$bDpto. Patología Animal$$cÁrea Sanidad Animal
000160898 773__ $$g56 (2025), 99 [16 pp.]$$pVet. res.$$tVeterinary Research$$x0928-4249
000160898 8564_ $$s3678411$$uhttps://zaguan.unizar.es/record/160898/files/texto_completo.pdf$$yVersión publicada
000160898 8564_ $$s2513436$$uhttps://zaguan.unizar.es/record/160898/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000160898 909CO $$ooai:zaguan.unizar.es:160898$$particulos$$pdriver
000160898 951__ $$a2025-10-17-14:17:26
000160898 980__ $$aARTICLE