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1、Proc.Nati.Acad.Sci.USAVol.81,pp.1421-1425,March1984CellBiologyAssemblyinvitroofaspanningmembraneproteinoftheendoplasmicreticulum:TheElglycoproteinofcoronavirusmousehepatitisvirusA59(cell-freeproteinsynthesis/envelopedanimalviruses)PETERROTTIER*,DOROTHEEBRANDENBURG*,JOHNARMSTRONGt,
2、BENVANDERZEUST*,ANDGRAHAMWARRENt*InstituteofVirology,VeterinaryFaculty,StateUniversityofUtrecht,3508TDUtrecht,TheNetherlands;andtTheEuropeanMolecularBiologyLaboratory,Postfach10.2209,6900Heidelberg,FederalRepublicofGermanyCommunicatedbyJohnKendrew,November16,1983ABSTRACTTheElglyco
3、proteinofcoronavirusmouseinfectivitybutnotforvirusmaturationandrelease(12,17).hepatitisvirusA59wassynthesizedinvitrobytranslationofSomepassestothecellsurfacewhereitfusesadjacentcellsviralmRNAinthepresenceofdogpancreaticmicrosomes.Itstogether,therebyspreadingtheinfection.Insomeresp
4、ects,dispositioninthemembranewasinvestigatedbydigestionwithE2issimilartothespikeglycoproteinsofthosevirusesthatproteasesandbyselectiveNH2-terminallabeling.TheproteinbudatthePM.Itappearstotakethesameroutethroughthespansthemembrane,butonlysmallportionsfromtheNH2cell,passingthroughth
5、eGolgicomplex,tobefatty-acylat-andCOOHterminusareexposedrespectivelyinthelumenaled,andtohavenormalN-linkedoligosaccharides(18).Inandcytoplasmicdomains;thebulkofthemoleculeisappar-contrast,theElproteinhasneitherfattyacidgroupsnorN-entlyburiedinthemembrane.Theproteinlacksacleavablel
6、inkedoligosaccharides;instead,ithas0-linkedoligosaccha-leadersequenceanddoesnotacquireitscharacteristic0-rides(12,17,18),whichareprobablyacquiredintheGolgilinkedoligosaccharidesinroughmicrosomes.Itmayenterthecomplex(14,19)asthevirionspassthroughthestacksofmembraneatanystagedurings
7、ynthesisofthefirst150aminoGolgicisternae.Thispatternofpost-translationalmodifica-acidresidues.Theseunusualfeaturesoftheproteinmighthelptionisuniqueamongviralglycoproteinssofarcharacter-toexplainwhyitisnottransportedtothecellsurfaceinvivoized.butremainsinintracellularmembranes,caus
8、ingthevirustoThebuddingsiteofthec
