glycoprotein-e2--hepatitis-c-virus and Lymphoma--Non-Hodgkin

Hepatitis C virus (HCV) infection is associated with extrahepatic B-cell lymphoproliferative disorders. To determine whether a viral antigen drives this B-cell expansion, the B-cell receptors were cloned from HCV-associated lymphomas and were expressed as soluble immunoglobulins. The rescued immunoglobulins were then tested for their ability to bind the HCV-E2 envelope glycoprotein, an antigen that was previously implicated in the pathogenesis of HCV-associated B-cell diseases. One of 2 lymphoma immunoglobulin test cases bound the E2 protein in a manner identical to a bona fide human anti-E2 antibody. Moreover, it bound E2 from multiple viral genotypes, suggesting reactivity with a conserved E2 epitope. These findings support the hypothesis that some HCV-associated lymphomas originate from B cells that were initially activated by the HCV-E2 protein and might explain the association between HCV infection and some B-cell lymphoproliferative disorders.

Topics: Amino Acid Sequence; B-Lymphocytes; Cloning, Molecular; Epitopes; Gene Expression; Genotype; Hepacivirus; Hepatitis C; Humans; Immunoglobulin Heavy Chains; Immunoglobulin Light Chains; Immunoglobulin Variable Region; Immunoglobulins; Lymphoma, Non-Hodgkin; Molecular Sequence Data; Mutation; Protein Conformation; Receptors, Antigen, B-Cell; Viral Envelope Proteins