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Functional hepatitis C virus envelope glycoproteins characterized.
2004 MAY 5 - (NewsRx.com & NewsRx.net) -- Scientists have characterized functional hepatitis C virus envelope glycoproteins.
According to published research from France and the United States, "Hepatitis C virus (HCV) encodes two envelope glycoproteins, E1 and E2, that assemble as a noncovalent heterodimer which is mainly retained in the endoplasmic reticulum. Because assembly into particles and secretion from the cell lead to structural changes in viral envelope proteins, characterization of the proteins associated with the virion is necessary in order to better understand how they mature to be functional in virus entry. There is currently no efficient and reliable cell culture system to amplify HCV, and the envelope glycoproteins associated with the virion have therefore not been characterized yet.
"Recently, infectious pseudotype particles that are assembled by displaying unmodified HCV envelope glycoproteins on retroviral core particles have been successfully generated," said Anne Op De Beeck and collaborators at the Institut Pasteur de Lille and INSERM U412 in France and Stanford University in the United States. "Because HCV pseudotype particles contain fully functional envelope glycoproteins, these envelope proteins, or at least a fraction of them, should be in a mature conformation similar to that on the native HCV particles. In this study, we used conformation-dependent monoclonal antibodies to characterize the envelope glycoproteins associated with HCV pseudotype particles.
"We showed that the ...
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