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1、ArchVirol(1989)106:221-237VrologyArchives(¢)bySpringer-Verlag1989Identificationandlocationofthestructuralglycoproteinsofatissueculture-adaptedturkeyentericcoronavirusS.Dea1,S.Garzon2,andP.TijssenIiCentredeRechercheenM6decineCompar~eUniversit6duQuebec,InstitutArmand-Frappier,Laval
2、-des-Rapides,Qu6bec,and2Facult6deM6decine,Universit6deMontr6al,Montreal,Qu6bec,CanadaAcceptedMarch27,1989Summary.TheMinnesotastrainofturkeyentericcoronavirus(TCV)wasgrownonahumanrectaltumor(HRT-18)celllineinthepresenceofradiolabeledaminoacidsandglucosaminetoanalysevifionstructura
3、lproteins.Inadditiontothe52,000unglycosylatednucleocapsidprotein,threemajorglycoproteinspecieswerefoundtobeassociatedwiththeviralenvelope.Apredominantglycosylatedproteinwithamolecularweightof22-24,000representedthetransmembranematrixprotein.Largerglycoproteinswithapparentmolecula
4、rweightsof180-200,000(gp200),120-125,000(gp120)and95-100,000(gp100)wereassociatedtothecharacteristiclargebulbousprojections(peplomers)lo-catedatthesurfaceofthevirion.Thegp100andgp120speciesapparentlyarosefromaproteolyticcleavageofgp200,assuggestedbydigestionstudieswithtrypsinandc
5、hymotrypsin.Anadditionallargeglycoproteinwithmol.wt.of140,000(gp140),thatbehavedasadisulfide-linkeddimerofa66,000mol-ecule,wasfoundtobeassociatedtogranularprojectionslocatednearthebaseofthelargepeplomers.Digestionstudieswithtrypsin,bromelainandpronasedemonstratedthatgp140wasrelat
6、edtothehemagglutinatingactivityofthevirus.Aninnermembranoussacortongue-shapedstructurecouldbevisualizedintheinterioroftheviralparticlesfollowingtreatmentwithpronase.Incontrast,trypsinorchymotrypsintreatmentsresultedinevaginafions("budding")onthevirussurface.Progenyviralparticlesp
7、roducedinTCV-infectedcellculturesinthepresenceoftunicamycinlackedbothtypesofsurfaceprojections,asdemonstratedbyelectronmicroscopyandelectrophoresis.Thematrixproteinalsoappearedtobereducedtoitsunglycosylatedform,concomitantwithaconsiderablelossofitsantigenicity.Thus,withrespecttoi
8、tsmorphologicalandbiochemicalcharacteris
