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Assay of preS epitopes and preS1 antibody in hepatitis B virus carriers and immune persons

✍ Scribed by R. Deepen; K. -H. Heermann; A. Uy; R. Thomssen; W. H. Gerlich

Publisher: Springer-Verlag
Year: 1990
Tongue: English
Weight: 664 KB
Volume: 179
Category: Article
ISSN: 0300-8584
DOI: 10.1007/bf00190150

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✦ Synopsis

The diagnostical significance of the large hepatitis B surface protein with its preS 1 attachment site and of anti-preS antibodies are not yet well known. We investigated the epitope of the preS1 attachment site to see whether it is a marker of viremia and whether antibodies against it occur in convalescents and vaccinees. For comparison, sera were also tested for the presence and relative amount of a preS2 epitope. The epitopes were detected by binding to specific monoclonal antibodies (mAb MA18/7 for the preS1 epitope and mAb Q19/10 for the preS2 epitope) at the solid phase of a sandwich enzyme-linked immunosorbent assay. Antibody against the preS1 epitope was detected by inhibition of binding to mAb MA18/7. This mAb inhibits attachment of preS 1 antigen to hepatocytes and reacts with a subtypeindependent sequential epitope at the surface of hepatitis B virus between amino acid 29-36. This preS1 epitope occurs in most hepatitis B surface antigen (HBsAg) carriers, irrespective of viremia. Free preS2 epitope Q 19/10 is present in samples with more than 8 pg/ml total HBsAg and it is masked in sera with less HBsAg. Antibodies which compete with mAb MA18/7 for its viral preS1 epitope occur in one third of HBsAg carriers who were negative for hepatitis B e antigen. It also occurs in one third of convalescents and in most good responders to plasma-derived vaccines.

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