Secretion of Hepatitis C Virus Envelope Glycoproteins Depends on Assembly of Apolipoprotein B Positive Lipoproteins 英文参考文献.docVIP

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Secretion of Hepatitis C Virus Envelope Glycoproteins Depends on Assembly of Apolipoprotein B Positive Lipoproteins 英文参考文献.doc

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Secretion of Hepatitis C Virus Envelope Glycoproteins Depends on Assembly of Apolipoprotein B Positive Lipoproteins 英文参考文献

SecretionofHepatitisCVirusEnvelopeGlycoproteins DependsonAssemblyofApolipoproteinBPositive Lipoproteins VincaIcard1,2,3,4.,OlivierDiaz1,2,3.,CarolineScholtes1,2,3,4,LaurePerrin-Cocon1,2,3 ,Christophe Ramie`re1,2,3,4,RalfBartenschlager5,FrancoisPenin6,VincentLotteau1,2,3,4,PatriceAndre′1,2,3,4 * 1Universite′ de Lyon, Lyon, France, 2Inserm, U851, Lyon, France, 3Universite′ de Lyon1, IFR128 BioSciences Lyon-Gerland, Lyon, France, 4Hospices Civils de Lyon, LaboratoiredeVirologieNord,Lyon,France,5DepartmentofMolecularVirology,UniversityofHeidelberg,Heidelberg,Germany,6CNRS,UMR5086,InstitutdeBiologieet ChimiedesProte′ines,Lyon,France Abstract The density of circulating hepatitis C virus (HCV) particles in the blood of chronically infected patients is very heterogeneous. The very low density of some particles has been attributed to an association of the virus with apolipoproteinB(apoB)positiveandtriglyceriderichlipoproteins(TRL)likelyresultinginhybridlipoproteinsknownaslipo- viro-particles(LVP)containingtheviralenvelopeglycoproteinsE1andE2,capsidandviralRNA.Thespecificinfectivityof theseparticleshasbeenshowntobehigherthantheinfectivityofparticlesofhigherdensity.Thenatureoftheassociation ofHCVparticleswithlipoproteinsremainselusiveandtheroleofapolipoproteinsinthesynthesisandassemblyoftheviral particles is unknown. The human intestinal Caco-2 cell line differentiates in vitro into polarized and apoB secreting cells duringasymmetriccultureonporousfilters.Byusingthiscellculturesystem,cellsstablyexpressingE1andE2secretedthe glycoproteinsintothebasalculturemediumafteroneweekofdifferentiationconcomitantlywithTRLsecretion.Secreted glycoproteins were only detected in apoB containing density fractions. The E1–E2 and apoB containing particles were uniquecomplexesbearingtheenvelopeglycoproteinsattheirsurfacesinceapoBcouldbeco-immunoprecipitatedwithE2- specific antibodies. Envelope proteinsecretion wasreduced by inhibitingthelipidation of apoBwith aninhibitor of the microsomaltrigly