Characterization of a human monoclonal antibody obtained after immunization with plasma vaccine and a booster with recombinant‐DNA hepatitis B vaccine
Identifieur interne : 000584 ( Istex/Corpus ); précédent : 000583; suivant : 000585Characterization of a human monoclonal antibody obtained after immunization with plasma vaccine and a booster with recombinant‐DNA hepatitis B vaccine
Auteurs : R. A. Heijtink ; J. Kruining ; P. Van Bergen ; S. De Rave ; J. Van Hattum ; M. Schutten ; A. D. M. E. OsterhausSource :
- Journal of Medical Virology [ 0146-6615 ] ; 2002-03.
Abstract
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: plasma‐derived vaccine) after one boost of yeast recombinant DNA derived vaccine (Engerix‐B). 1Ff4 binds preferentially to HBsAg/adw2 and HBsAg/ayw1. In binding experiments, it competes with antibodies induced by vaccination with HB‐VAX‐DNA (yeast recombinant) and HB‐VAX (plasma‐derived vaccine). 1Ff4 competes in part with a monoclonal antibody for the w/r region. Partial inhibition of binding of HBsAg/adw2 to solid phase anti‐HBs was detected, resembling inhibition obtained using other human monoclonal specific for the “a”‐loop. 1Ff4 does not bind to linear peptides covering the two “a”‐loops or to an adw2/G145R mutant, its binding to wild type HBsAg strongly depends on the presence of disulphide bonds. In a large series of HBsAg‐positive samples from an endemic area, 1Ff4 antibodies were successfully used to discriminate between an adw2 and an adrq+ strain. The characterisation of 1Ff4 and other human monoclonal anti‐HBs antibodies may help to understand the fine specificity of protective antibodies elicited by immunization. J. Med. Virol. 66:304‐311, 2002. © 2002 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/jmv.2146
Links to Exploration step
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<front><div type="abstract" xml:lang="en">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: plasma‐derived vaccine) after one boost of yeast recombinant DNA derived vaccine (Engerix‐B). 1Ff4 binds preferentially to HBsAg/adw2 and HBsAg/ayw1. In binding experiments, it competes with antibodies induced by vaccination with HB‐VAX‐DNA (yeast recombinant) and HB‐VAX (plasma‐derived vaccine). 1Ff4 competes in part with a monoclonal antibody for the w/r region. Partial inhibition of binding of HBsAg/adw2 to solid phase anti‐HBs was detected, resembling inhibition obtained using other human monoclonal specific for the “a”‐loop. 1Ff4 does not bind to linear peptides covering the two “a”‐loops or to an adw2/G145R mutant, its binding to wild type HBsAg strongly depends on the presence of disulphide bonds. In a large series of HBsAg‐positive samples from an endemic area, 1Ff4 antibodies were successfully used to discriminate between an adw2 and an adrq+ strain. The characterisation of 1Ff4 and other human monoclonal anti‐HBs antibodies may help to understand the fine specificity of protective antibodies elicited by immunization. J. Med. Virol. 66:304‐311, 2002. © 2002 Wiley‐Liss, Inc.</div>
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<p>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: plasma‐derived vaccine) after one boost of yeast recombinant DNA derived vaccine (Engerix‐B). 1Ff4 binds preferentially to HBsAg/<hi rend="italic">adw</hi>
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<p>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: plasma‐derived vaccine) after one boost of yeast recombinant DNA derived vaccine (Engerix‐B). 1Ff4 binds preferentially to HBsAg/<i>adw</i>
<sub>2</sub>
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<sub>2</sub>
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<sub>2</sub>
/G145R mutant, its binding to wild type HBsAg strongly depends on the presence of disulphide bonds. In a large series of HBsAg‐positive samples from an endemic area, 1Ff4 antibodies were successfully used to discriminate between an <i>adw</i>
<sub>2</sub>
and an adrq+ strain. The characterisation of 1Ff4 and other human monoclonal anti‐HBs antibodies may help to understand the fine specificity of protective antibodies elicited by immunization. J. Med. Virol. 66:304‐311, 2002. © 2002 Wiley‐Liss, Inc.</p>
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<abstract lang="en">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: plasma‐derived vaccine) after one boost of yeast recombinant DNA derived vaccine (Engerix‐B). 1Ff4 binds preferentially to HBsAg/adw2 and HBsAg/ayw1. In binding experiments, it competes with antibodies induced by vaccination with HB‐VAX‐DNA (yeast recombinant) and HB‐VAX (plasma‐derived vaccine). 1Ff4 competes in part with a monoclonal antibody for the w/r region. Partial inhibition of binding of HBsAg/adw2 to solid phase anti‐HBs was detected, resembling inhibition obtained using other human monoclonal specific for the “a”‐loop. 1Ff4 does not bind to linear peptides covering the two “a”‐loops or to an adw2/G145R mutant, its binding to wild type HBsAg strongly depends on the presence of disulphide bonds. In a large series of HBsAg‐positive samples from an endemic area, 1Ff4 antibodies were successfully used to discriminate between an adw2 and an adrq+ strain. The characterisation of 1Ff4 and other human monoclonal anti‐HBs antibodies may help to understand the fine specificity of protective antibodies elicited by immunization. J. Med. Virol. 66:304‐311, 2002. © 2002 Wiley‐Liss, Inc.</abstract>
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