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Characterization of a human monoclonal antibody obtained after immunization with plasma vaccine and a booster with recombinant-DNA hepatitis B vaccine

✍ Scribed by R.A. Heijtink; J. Kruining; P. van Bergen; S. de Rave; J. van Hattum; M. Schutten; A.D.M.E. Osterhaus

Publisher
John Wiley and Sons
Year
2002
Tongue
English
Weight
204 KB
Volume
66
Category
Article
ISSN
0146-6615

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✦ Synopsis

A human monoclonal antibody type IgG4, designated 1Ff4, was obtained by Epstein Barr virus transformation of peripheral blood lymphocytes from a hepatitis B vaccinee (HB-VAX: plasmaderived vaccine) after one boost of yeast recombinant DNA derived vaccine (Engerix-B). 1Ff4 binds preferentially to HBsAg/adw 2 and HBsAg/ ayw 1 . In binding experiments, it competes with antibodies induced by vaccination with HB-VAX-DNA (yeast recombinant) and HB-VAX (plasmaderived vaccine). 1Ff4 competes in part with a monoclonal antibody for the w/r region. Partial inhibition of binding of HBsAg/adw 2 to solid phase anti-HBs was detected, resembling inhibition obtained using other human monoclonal speci®c for the a''-loop. 1Ff4 does not bind to linear peptides covering the two a''-loops or to an adw 2 /G145R mutant, its binding to wild type HBsAg strongly depends on the presence of disulphide bonds. In a large series of HBsAgpositive samples from an endemic area, 1Ff4 antibodies were successfully used to discriminate between an adw 2 and an adrq strain. The characterisation of 1Ff4 and other human monoclonal anti-HBs antibodies may help to understand the ®ne speci®city of protective antibodies elicited by immunization.

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