title: Characterization of aggregates of hepatitis C virus glycoproteins.
abstract: Hepatitis C virus (HCV) encodes two glycoproteins, E1 and E2, which assemble in oligomeric structures. Studies of HCV glycoprotein assembly using heterologous expression systems have shown that these glycoproteins can follow two pathways: a productive pathway leading to the formation of a non-covalent heterodimer; and a non-productive pathway leading to the formation of large disulfide-linked aggregates. The non-covalent HCV glycoprotein complex is probably the functional complex which plays an active role in the entry process in host cells. The aggregates are believed to be waste products; however, one can imagine that, in infected cells, they could provide HCV glycoproteins with additional functions. To further understand the potential role played by HCV glycoprotein aggregates in HCV infection, a MAb (H14) was produced which specifically recognizes these aggregates but not the non-covalent E1E2 heterodimer. The H14 epitope was shown to be present on both HCV glycoproteins and was sensitive to deglycosylation. An additional characterization of HCV glycoprotein aggregates, with the help of MAb H14, indicates that they share an epitope with a cellular protein called Mac-2 binding protein. The presence of such an epitope on HCV glycoprotein aggregates could potentially lead to the production of autoantibodies recognizing Mac-2 binding protein in HCV-infected patients.
authors.affiliation: CNRS-UMR 85261 and CNRS-UMR 85252, Institut de Biologie de Lille/Institut Pasteur de Lille, BP447, 59021 Lille cedex, France.
authors.forename: Amélie
authors.initials: A
authors.lastname: Choukhi
authors.affiliation: CNRS-UMR 85261 and CNRS-UMR 85252, Institut de Biologie de Lille/Institut Pasteur de Lille, BP447, 59021 Lille cedex, France.
authors.forename: André
authors.initials: A
authors.lastname: Pillez
authors.affiliation: CNRS-UMR 85261 and CNRS-UMR 85252, Institut de Biologie de Lille/Institut Pasteur de Lille, BP447, 59021 Lille cedex, France.
authors.forename: Hervé
authors.initials: H
authors.lastname: Drobecq
authors.affiliation: CNRS-UMR 85261 and CNRS-UMR 85252, Institut de Biologie de Lille/Institut Pasteur de Lille, BP447, 59021 Lille cedex, France.
authors.forename: Christian
authors.initials: C
authors.lastname: Sergheraert
authors.affiliation: CNRS-UMR 85261 and CNRS-UMR 85252, Institut de Biologie de Lille/Institut Pasteur de Lille, BP447, 59021 Lille cedex, France.
authors.forename: Czeslaw
authors.initials: C
authors.lastname: Wychowski
authors.affiliation: CNRS-UMR 85261 and CNRS-UMR 85252, Institut de Biologie de Lille/Institut Pasteur de Lille, BP447, 59021 Lille cedex, France.
authors.forename: Jean
authors.initials: J
authors.lastname: Dubuisson
mesh_terms: D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000951:Antigens, Neoplasm; D014408:Biomarkers, Tumor; D015153:Blotting, Western; D002352:Carrier Proteins / Q000276:immunology*; D002460:Cell Line; D000939:Epitopes; D005455:Fluorescent Antibody Technique; D006023:Glycoproteins / Q000276:immunology*; D016174:Hepacivirus / Q000235:genetics / Q000276:immunology / Q000472:pathogenicity; D006801:Humans; D011233:Precipitin Tests; D017510:Protein Folding; D014407:Tumor Cells, Cultured; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000276:immunology* / Q000378:metabolism; D016326:Extracellular Matrix Proteins
chemical_list: D000469:Alkaline Phosphatase; D000911:Antibodies, Monoclonal; D000951:Antigens, Neoplasm; D014408:Biomarkers, Tumor; D002352:Carrier Proteins; D000939:Epitopes; D006023:Glycoproteins; D014759:Viral Envelope Proteins; C087035:E1 protein, Hepatitis C virus; C081856:LGALS3BP protein, human; D016326:Extracellular Matrix Proteins; C091015:glycoprotein E2, Hepatitis C virus