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dc.contributor.authorMartín-Galiano, Antonio Javier 
dc.contributor.authorGorgojo, Begoña 
dc.contributor.authorKunin, Calvin M
dc.contributor.authorde la Campa, Adela G 
dc.date.accessioned2019-08-13T11:35:28Z
dc.date.available2019-08-13T11:35:28Z
dc.date.issued2002-06
dc.identifier.citationAntimicrob Agents Chemother. 2002 Jun;46(6):1680-7.es_ES
dc.identifier.issn0066-4804es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/8221
dc.description.abstractThe activities of mefloquine (MFL) and related compounds against previously characterized Streptococcus pneumoniae strains carrying defined amino acid substitutions in the c subunit of the F(0)F(1) H(+)-ATPase were studied. In addition, a series of MFL-resistant (Mfl(r)) strains were isolated and characterized. A good correlation was observed between inhibition of growth and inhibition of the membrane-associated F(0)F(1) H(+)-ATPase activity. MFL was about 10-fold more active than optochin and about 200-fold more active than quinine in inhibiting both the growth and the ATPase activities of laboratory pneumococcal strain R6. Mutant strains were inhibited by the different compounds to different degrees, depending on their specific mutations in the c subunit. The resistant strains studied had point mutations that changed amino acid residues in either the c subunit or the a subunit of the F(0) complex. Changes in the c subunit were located in one of the two transmembrane alpha helices: residues M13, G14, G20, M23, and N24 of helix 1 and residues M44, G47, V48, A49, and V57 of helix 2. Changes in the a subunit were also found in either of the transmembrane alpha helices, helix 5 or 6: residue L186 of helix 5 and residues W206, F209, and S214 of helix 6. These results suggest that the transmembrane helices of the c and a subunits interact and that the mutated residues are important for the structure of the F(0) complex and proton translocation.es_ES
dc.description.sponsorshipWe thank E. García for critical reading of the manuscript. The technical assistance of A. Rodríguez-Bernabé is acknowledged. A.J.M.-G. received a fellowship from Comunidad Autónoma de Madrid. This study was supported by grant 1274/01 from Instituto de Salud Carlos III.es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Microbiologyes_ES
dc.relation.isversionofPreprintes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAmino Acid Sequence es_ES
dc.subject.meshAmino Alcohols es_ES
dc.subject.meshAntimalarials es_ES
dc.subject.meshCell Membrane es_ES
dc.subject.meshDNA, Bacterial es_ES
dc.subject.meshMefloquine es_ES
dc.subject.meshMicrobial Sensitivity Tests es_ES
dc.subject.meshMolecular Sequence Data es_ES
dc.subject.meshMutation es_ES
dc.subject.meshProton-Translocating ATPases es_ES
dc.subject.meshReverse Transcriptase Polymerase Chain Reaction es_ES
dc.subject.meshStreptococcus pneumoniae es_ES
dc.titleMefloquine and new related compounds target the F(0) complex of the F(0)F(1) H(+)-ATPase of Streptococcus pneumoniaees_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución-NoComercial-CompartirIgual 4.0 Internacional*
dc.identifier.pubmedID12019076es_ES
dc.format.volume46es_ES
dc.format.number6es_ES
dc.format.page1680-7es_ES
dc.identifier.doi10.1128/aac.46.6.1680-1687.2002es_ES
dc.contributor.funderComunidad de Madrid
dc.contributor.funderInstituto de Salud Carlos III - ISCIII
dc.relation.publisherversionhttps://doi.org/10.1128/aac.46.6.1680-1687.2002es_ES
dc.identifier.journalAntimicrobial agents and chemotherapyes_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/1274/01es_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Atribución-NoComercial-CompartirIgual 4.0 Internacional
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