A Mycobacterium leprae Hsp65 Mutant as a Candidate for Mitigating Lupus Aggravation in Mice 英文参考文献.docVIP

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A Mycobacterium leprae Hsp65 Mutant as a Candidate for Mitigating Lupus Aggravation in Mice 英文参考文献.doc

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A Mycobacterium leprae Hsp65 Mutant as a Candidate for Mitigating Lupus Aggravation in Mice 英文参考文献

AMycobacteriumlepraeHsp65MutantasaCandidate forMitigatingLupusAggravationinMice ElianaB.Marengo1,LucianaV.deMoraes2,RobsonL.Melo3,AndreaBalan4,BeatrizL.Fernandes3, DeniseV.Tambourgi5,LuizVicenteRizzo1,OsvaldoAugustoSant’Anna5* 1Hospital Israelita Albert Einstein, Sa?o Paulo, Brazil, 2Laborato′rio de Doenc?as Gene′ticas, Instituto Gulbenkian de Cie?ncia, Oeiras, Portugal, 3Centro de Toxinologia Aplicada-CAT/CEPID, Instituto Butantan, Sa?o Paulo, Brazil, 4Laborato′rio Nacional de Biocie?ncias LNBio, Centro de Pesquisa em Energia e Materiais, Po′lo II de Alta Tecnologia,Campinas,Brazil,5Laborato′riodeImunoqu?′mica,InstitutoButantan,Sa?o Paulo,Brazil Abstract Hsp60isanabundantandhighlyconservedfamilyofintracellularmolecules.Increasedlevelsofthisfamilyofproteinshave been observed in the extracellular compartment in chronic inflammation. Administration of M. leprae Hsp65 [WT] in [NZBxNZW]F1 mice accelerates the Systemic Lupus Erythematosus [SLE] progression whereas the point mutated K409A Hsp65 protein delays the disease. Here, the biological effects of M. leprae Hsp65 Leader pep and K409A pep synthetic peptides,whichcoverresidues352–371,arepresented.Peptideshadimmunomodulatoryeffectssimilartothatobserved withtheirrespectiveproteinsonsurvivalandthecombinedadministrationofK A LeaderpeporK409Apep WTshowed thatthemutantformswereabletoinhibitthedeleteriouseffectofWTonmortality,indicatingtheneutralizingpotentialof the mutant molecules in SLE progression. Molecular modeling showed that replacing Lysine by Alanine affects the electrostaticpotentialofthe352–371region.ThenumberofinteractionsobservedforWTismuchhigherthanforHsp65 K409AandmouseHsp60.Theimmunomodulatoryeffectsofthepoint-mutatedproteinandpeptideoccurredregardlessof thecatalytic activity.Thesefindings may be related tothelack of effect on survival whenF1 mice wereinoculated with Hsp60or K409Apep.Our findingsindicatetheuseofpoint-mutated Hsp65molecules,suchastheK409Aproteinandits corresponding peptide