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1、LETTERdoi:10.1038/nature12328MolecularbasisofbindingbetweennovelhumancoronavirusMERS-CoVanditsreceptorCD2612113,411,511,6GuangwenLu*,YaweiHu*,QihuiWang*,JianxunQi*,FengGao*,YanLi,YanfangZhang,WeiZhang,YuanYuan,42711,5,6,7,8JinkuBao,BuchangZhang,YiShi,JinghuaYan&GeorgeF.
2、Gao13–15ThenewlyemergentMiddleEastrespiratorysyndromecoronavirusviruses,shouldmediatemembranefusion.Theexploitationofthe1,2(MERS-CoV)cancauseseverepulmonarydiseaseinhumans,repre-virus–receptorinteractionandthusoftheinterventionstrategiessentingthesecondexampleofahighlyp
3、athogeniccoronavirus,therequiresanatomicdelineationofthereceptor-bindingpropertiesof3firstbeingSARS-CoV.CD26(alsoknownasdipeptidylpeptidaseS1.Onthebasisofpreviousstudies,thereceptorattachmentsitesof4,DPP4)wasrecentlyidentifiedasthecellularreceptorforMERS-coronavirusS1su
4、bunitsmightlocatetoeithertheamino-terminal416CoV.TheengagementoftheMERS-CoVspikeproteinwithCD26(suchasinmurinehepatitisvirus)orthecarboxy-terminal(suchas17mediatesviralattachmenttohostcellsandvirus–cellfusion,therebyin,forexample,SARS-CoVandhumancoronavirusNL63(ref.18))
5、initiatinginfection.Herewedelineatethemolecularbasisofthisdomain.WethereforetestedindividuallythebindingofMERS-CoVS1specificinteractionbypresentingthefirstcrystalstructuresofbothanditsN-andC-terminal-domainproteinstocell-surface-expressedthefreereceptorbindingdomain(RBD
6、)oftheMERS-CoVspikeCD26molecules.Thereceptor-bindingcapacitywasattributedtotheproteinanditscomplexwithCD26.Furthermore,bindingbetweenC-terminalaminoacids367–606ofMERS-CoVS1(Fig.1b).WeherebytheRBDandCD26ismeasuredusingreal-timesurfaceplasmonreferredtothisdomainasRBD.Thep
7、otentinteractionbetweenMERS-resonancewithadissociationconstantof16.7nM.TheviralRBDCoVRBDandCD26wasfurtherdemonstratedbysurfaceplasmoniscomposedofacoresubdomainhomologoustothatoftheSARS-resonanceassays,inwhichCD26bindstoMERS-CoVRBDwitha52121CoVspikeprotein,andauniquestra
8、nd-dominatedexternalreceptordissociationconstant(Kd)ofabout16.7nM(Kon,1.79310Ms;2321bindingmotifthatrecognizes
