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1、JournalofGeneralVirology(1992),73,2731-2736.PrintedinGreatBritain2731Sequenceanalysisofthemembraneproteingeneofhumancoronavirus0C43andevidenceforO-glycosylationSamirMounirandPierreJ.Talbot*VirologyResearchCenter,InstitutArmand-Frappier,Universit~duQu
2、ebec,531boulevarddesPrairies,LavaLQukbec,CanadaH7N4Z3Thegeneencodingthemembrane(M)proteinofthehydrophobictransmembranedomains.TheaminoacidOC43strainofhumancoronavirus(HCV-OC43)wassequenceoftheMproteinofHCV-OC43has94%amplifiedbyareversetranscription-p
3、olymerasechainidentitywiththatoftheMebusstrainofBCV,andalsoreactionofviralRNAwithHCV-OC43-andbovinecontainssixpotentialO-glycosylationsitesinthecoronavirus(BCV)-specificprimers.ThenucleotideexposedN-terminaldomain.Indeed,theglycosylationsequenceofthe
4、cloned1-5kbfragmentrevealedanoftheMproteinwasnotinhibitedinthepresenceofopenreadingframe(ORF)of690nucleotideswhichtunicamycin,whichisindicativeofO-glycosylation,aswasidentifiedastheMproteingenefromitshomologypreviouslyreportedforBCVandmurinehepatitis
5、toBCV.ThisORFencodesaproteinof230aminovirus.Virionsreleasedfromtunicamycin-treatedcellsacidswithanMrof26416.ThegeneisprecededbythecontainedtheMglycoproteinbutweredevoidofbothmotifUCCAAAC,analogoustotheconsensuscorona-peplomer(S)andhaemagglutinin-este
6、rase(HE)pro-virustranscriptioninitiationsequence.TheMproteinteins.Thus,inhibitionoftheN-glycosylationoftheSofHCV-OC43showsfeaturestypicalofallcoronavirusandHEstructuralproteinspreventedtheirincorpora-Mproteinsstudied:ahydrophilic,presumablyexternalti
7、onintoprogenyvirions,anindicationthattheyareNterminusincludingabout10%oftheprotein,andadispensableforvirionmorphogenesis,unliketheMpotentialN-glycosylationsitefollowedbythreemajorprotein.Humancoronaviruses(HCVs)aregroupedintotwoMHVsshowdiversetropism
8、s,andsomeMHVstrainsinmajorantigenicclusters,representedbytheprototyperodentshavebeenusedasamodelsystemtostudystrains229EandOC43(Siddelletal.,1983).HCV-OC43chronicandacutehepaticandneurologicaldiseases.sharesantigenicrelationshipswithothercoronaviruse
