title: The antigen/antibody specificity exchanger: a new peptide based tool for re-directing antibodies of other specificities to recognize the V3 domain of HIV-1 gp120.
abstract: We recently showed that a synthetic peptide corresponding to the third complementary determining region of the heavy chain (CDRH3) of a monoclonal antibody (mAb) directed to the V3 domain of HIV-1 gp120 neutralizes HIV-1 in vitro. From the CDRH3 sequence we have now produced bifunctional antigen/antibody specificity exchanger (A/ASE) peptides containing both the HIV-1 mAb derived CDRH3 sequence and antigenic region sequences from the hepatitis B virus core/e antigen (HBc/eAg) and the poliovirus VP1. These A/ASE peptides were able to re-direct HBc/eAg and enteroviral VP1 specific mAbs, as well as polyclonal human HIV-1 negative sera to recognize the V3 domain of HIV-1. Furthermore, two out of three A/ASE peptides were able to neutralize HIV-1 in vitro. These bifunctional A/ASE peptides have a potential to be used as tools in research, diagnostics and maybe even therapeutics.
authors: Department of Immunology, Microbiology, Pathology, and Infectious Diseases, Karolinska Institutet, Huddinge University Hosptial, Sweden.
authors: M
authors: M
authors: Sällberg
authors: K
authors: K
authors: Sherefa
authors: Z X
authors: ZX
authors: Zhang
mesh_terms: D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D000937:Antigen-Antibody Reactions; D000956:Antigens, Viral / Q000276:immunology*; D015699:HIV Envelope Protein gp120 / Q000276:immunology*; D015497:HIV-1 / Q000276:immunology*; D007124:Immunoenzyme Techniques; D007143:Immunoglobulin Heavy Chains; D008969:Molecular Sequence Data; D009500:Neutralization Tests; D010455:Peptides / Q000138:chemical synthesis / Q000276:immunology
chemical_list: D000911:Antibodies, Monoclonal; D000956:Antigens, Viral; D015699:HIV Envelope Protein gp120; D007143:Immunoglobulin Heavy Chains; D010455:Peptides