000077269 001__ 77269
000077269 005__ 20220309092436.0
000077269 0247_ $$2doi$$a10.3389/fmicb.2019.00046
000077269 0248_ $$2sideral$$a110572
000077269 037__ $$aART-2019-110572
000077269 041__ $$aeng
000077269 100__ $$aSanz-García, F.
000077269 245__ $$aMycobacterial aminoglycoside acetyltransferases: a little of drug resistance, and a lot of other roles
000077269 260__ $$c2019
000077269 5060_ $$aAccess copy available to the general public$$fUnrestricted
000077269 5203_ $$aAminoglycoside acetyltransferases are important determinants of resistance to aminoglycoside antibiotics in most bacterial genera. In mycobacteria, however, aminoglycoside acetyltransferases contribute only partially to aminoglycoside susceptibility since they are related with low level resistance to these antibiotics (while high level aminoglycoside resistance is due to mutations in the ribosome). Instead, aminoglycoside acetyltransferases contribute to other bacterial functions, and this can explain its widespread presence along species of genus Mycobacterium. This review is focused on two mycobacterial aminoglycoside acetyltransferase enzymes. First, the aminoglycoside 2'-N-acetyltransferase [AAC(2')], which was identified as a determinant of weak aminoglycoside resistance in M. fortuitum, and later found to be widespread in most mycobacterial species; AAC(2') enzymes have been associated with resistance to cell wall degradative enzymes, and bactericidal mode of action of aminoglycosides. Second, the Eis aminoglycoside acetyltransferase, which was identified originally as a virulence determinant in M. tuberculosis (enhanced intracellular survival); Eis protein in fact controls production of pro-inflammatory cytokines and other pathways. The relation of Eis with aminoglycoside susceptibility was found after the years, and reaches clinical significance only in M. tuberculosis isolates resistant to the second-line drug kanamycin. Given the role of AAC(2') and Eis proteins in mycobacterial biology, inhibitory molecules have been identified, more abundantly in case of Eis. In conclusion, AAC(2') and Eis have evolved from a marginal role as potential drug resistance mechanisms into a promising future as drug targets.
000077269 536__ $$9info:eu-repo/grantAgreement/ES/MINECO/SAF2017-84839-C2-1-R$$9info:eu-repo/grantAgreement/ES/MINECO/SAF2013-48971-C2-2-R$$9info:eu-repo/grantAgreement/EC/FP7/260872/EU/More Medicines for Tuberculosis/MM4TB
000077269 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000077269 590__ $$a4.235$$b2019
000077269 591__ $$aMICROBIOLOGY$$b34 / 134 = 0.254$$c2019$$dQ2$$eT1
000077269 592__ $$a1.69$$b2019
000077269 593__ $$aMicrobiology (medical)$$c2019$$dQ1
000077269 593__ $$aMicrobiology$$c2019$$dQ1
000077269 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000077269 700__ $$0(orcid)0000-0002-6649-9153$$aAnoz-Carbonell, E.$$uUniversidad de Zaragoza
000077269 700__ $$aPérez-Herrán, E.
000077269 700__ $$0(orcid)0000-0003-2993-5478$$aMartín, C.$$uUniversidad de Zaragoza
000077269 700__ $$0(orcid)0000-0002-0111-4697$$aLucía, A.$$uUniversidad de Zaragoza
000077269 700__ $$aRodrigues, L.
000077269 700__ $$0(orcid)0000-0003-2076-844X$$aAínsa, J.A.$$uUniversidad de Zaragoza
000077269 7102_ $$11008$$2630$$aUniversidad de Zaragoza$$bDpto. Microb.Med.Pr.,Sal.Públ.$$cÁrea Microbiología
000077269 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000077269 773__ $$g10 (2019), 46 [11 pp.]$$pFront. microbiol.$$tFrontiers in Microbiology$$x1664-302X
000077269 8564_ $$s1266684$$uhttps://zaguan.unizar.es/record/77269/files/texto_completo.pdf$$yVersión publicada
000077269 8564_ $$s27864$$uhttps://zaguan.unizar.es/record/77269/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000077269 909CO $$ooai:zaguan.unizar.es:77269$$particulos$$pdriver
000077269 951__ $$a2022-03-09-09:17:23
000077269 980__ $$aARTICLE