000164076 001__ 164076
000164076 005__ 20251121161351.0
000164076 0247_ $$2doi$$a10.1016/j.micres.2025.128354
000164076 0248_ $$2sideral$$a146205
000164076 037__ $$aART-2025-146205
000164076 041__ $$aeng
000164076 100__ $$aGarcía, Carla$$uUniversidad de Zaragoza
000164076 245__ $$aIdentification of ShgH as a dual histidine/glutamine transporter component essential for Streptococcus suis virulence and biofilm modulation
000164076 260__ $$c2025
000164076 5060_ $$aAccess copy available to the general public$$fUnrestricted
000164076 5203_ $$aStreptococcus suis is a zoonotic pathogen that affects pigs and humans. In this study, we characterised ShgH, a predicted substrate-binding component of an ABC transporter. Immunoassays confirmed that ShgH is expressed, secreted and surface-exposed in S. suis, in agreement with its proposed transporter function. Isothermal titration calorimetry demonstrated that ShgH binds glutamine and histidine, with a higher affinity for histidine. Deletion of the shgH gene significantly impaired uptake of both radiolabelled amino acids confirming its role as part of a transporter. Functional analysis revealed that shgH deletion results in a marked reduction in virulence in a murine infection model, while host colonization remained unaffected. ShgH contributes to infection by facilitating evasion of phagocytosis and resistance to oxidative stress through impaired nutrient acquisition and reduced capsule production. In addition, ShgH regulates biofilm formation and architecture. Notably, ShgH is highly conserved among pathogenic streptococci, suggesting a broader functional relevance. Altogether, our findings identify ShgH as a dual glutamine/histidine- binding protein essential for nutrient uptake and virulence in S. suis, and a promising target for future therapeutic interventions.
000164076 536__ $$9info:eu-repo/grantAgreement/ES/MICINN AEI PID2020-114617RB-100
000164076 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttps://creativecommons.org/licenses/by/4.0/deed.es
000164076 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000164076 700__ $$aSaralegui, Luis$$uUniversidad de Zaragoza
000164076 700__ $$aMorales, Beatriz
000164076 700__ $$aJurado, Paula
000164076 700__ $$0(orcid)0000-0002-8181-2689$$aBes, M. Teresa$$uUniversidad de Zaragoza
000164076 700__ $$0(orcid)0000-0002-1974-9025$$aMarín, Clara
000164076 700__ $$0(orcid)0000-0002-8134-0693$$aArenas, Jesús$$uUniversidad de Zaragoza
000164076 7102_ $$11009$$2773$$aUniversidad de Zaragoza$$bDpto. Patología Animal$$cÁrea Sanidad Animal
000164076 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000164076 773__ $$g302 (2025), 128354$$pMicrobiol. res.$$tMICROBIOLOGICAL RESEARCH$$x0944-5013
000164076 8564_ $$s7162522$$uhttps://zaguan.unizar.es/record/164076/files/texto_completo.pdf$$yVersión publicada
000164076 8564_ $$s2592956$$uhttps://zaguan.unizar.es/record/164076/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000164076 909CO $$ooai:zaguan.unizar.es:164076$$particulos$$pdriver
000164076 951__ $$a2025-11-21-14:26:00
000164076 980__ $$aARTICLE