Please use this identifier to cite or link to this item: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/9028
Title: InsilicoAnalysisRevealedHigh-riskSingleNucleotidePolymorphismsinHumanPentraxin-3GeneandtheirImpactonInnateImmuneResponseagainstMicrobialPathogens
Authors: Thakur, Raman
Shankar, Jata
Keywords: PTX-3
In silico
Aspergillusfumigatus
lipopolysaccharide
Issue Date: 2016
Publisher: Jaypee University of Information Technology, Solan, H.P.
Abstract: Pentraxin-3(PTX-3)proteinisanevolutionaryconservedproteinthatactsasasolublepattern-recognitionreceptorforpathogensandplaysimportantroleininnateimmuneresponse.Itrecognizesvariouspathogensbyinteractingwithextracellularmoietiessuchasglactomannanofconidia(Aspergillusfumigatus),lipopolysaccharideofPseudomonasaeruginosa,StreptococcuspneumoniaandSalmonellatyphimurium.Thus,PTX-3proteinhelpstoclearthesepathogensbyactivatingdownstreaminnateimmuneprocess.Inthisstudy,computationalmethodswereusedtoanalyzevariousnon-synonymoussinglenucleotidepolymorphisms(nsSNPs)inPTX-3gene.ThreedifferentdatabaseswereusedtoretrieveSNPdatasetsfollowedbysevendifferentinsilicoalgorithmstoscreennsSNPsinPTX-3gene.SequencehomologybasedapproachwasusedtoidentifynsSNPs.ConservationprofileofPTX-3proteinaminoacidresidueswerepredictedbyConSurfwebserver.Intotal,10high-risknsSNPswereidentifiedinpentraxin-domainofPTX-3gene.Outofthese10high-risknsSNPs,4werepresentintheconservedstructuralandfunctionalresiduesofthepentraxin-domain,hence,selectedforstructuralanalyses.Theresultsshowedalterationintheputativestructureofpentraxin-domain.Predictionofprotein–proteininteractionsanalysisshowedassociationofPTX-3proteinwithC1qcomponentofcomplementpathway.DifferentfunctionalandstructuralresiduesalongwithvariousputativephosphorylationsitesandevolutionaryrelationshipwerealsopredicteforPTX-3protein.ThisisthefirstextensivecomputationalanalysesofpentraxinproteinfamilywithnsSNPsandwillserveasavaluableresourceforfuturepopulatiobasedstudies.
URI: http://ir.juit.ac.in:8080/jspui/jspui/handle/123456789/9028
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