Characterization of anti-idiotypic antibodies mimicking antibody- and receptor-binding sites on hepatitis A virus

Characterization of anti-idiotypic antibodies mimicking antibody- and receptor-binding sites on... Two anti-idiotypic monoclonal antibodies (mAb2s; named 94-2 and 94-7), were generated from a BALB/c mouse immunized with human monoclonal anti-hepatitis A virus (HAV) neutralizing antibody KF94. We characterized the properties of the mAb2s and determined interactions between mAb2s, KF94 and HAV using enzyme-linked immunosorbent assay, immunofluorescence assay and HAV infectivity assay. Inactivated HAV inhibited mAb2 binding to KF94, indicating that the mAb2s mimicked the HAV neutralization site that was complementary to the paratope of KF94. MAb2 94-7 competed with an anti-HAV cellular receptor antibody for binding to HAV-susceptible cells and partially blocked virus infection. We speculated that mAb2 94-7 mimicked a portion of the HAV receptor-binding site. The ability to generate mAb2 implies that HAV receptor-binding sites are exposed on the surface of HAV, permitting antibody access. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Characterization of anti-idiotypic antibodies mimicking antibody- and receptor-binding sites on hepatitis A virus

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Publisher
Springer Journals
Copyright
Copyright © 2009 by Springer-Verlag
Subject
Biomedicine; Infectious Diseases; Medical Microbiology ; Virology
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-009-0433-6
Publisher site
See Article on Publisher Site

Abstract

Two anti-idiotypic monoclonal antibodies (mAb2s; named 94-2 and 94-7), were generated from a BALB/c mouse immunized with human monoclonal anti-hepatitis A virus (HAV) neutralizing antibody KF94. We characterized the properties of the mAb2s and determined interactions between mAb2s, KF94 and HAV using enzyme-linked immunosorbent assay, immunofluorescence assay and HAV infectivity assay. Inactivated HAV inhibited mAb2 binding to KF94, indicating that the mAb2s mimicked the HAV neutralization site that was complementary to the paratope of KF94. MAb2 94-7 competed with an anti-HAV cellular receptor antibody for binding to HAV-susceptible cells and partially blocked virus infection. We speculated that mAb2 94-7 mimicked a portion of the HAV receptor-binding site. The ability to generate mAb2 implies that HAV receptor-binding sites are exposed on the surface of HAV, permitting antibody access.

Journal

Archives of VirologySpringer Journals

Published: Aug 1, 2009

References

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