ABSTRACT
A humanized monoclonal antibody that binds to the 86-kDa glycoprotein, gpUL75 (gH), of human cytomegalovirus (CMV) has been developed. The six complementarity determining regions of the heavy and light chains of the mouse antibody HCMV16 were transferred to human antibody framework sequences and combined with human antibody constant regions to produce a complete antibody. The reshaped antibody recognized cells infected with a variety of virus strains and neutralized clinical isolates of CMV as efficiently as laboratory strains in a conventional plaque reduction assay. This antibody provides a potential agent for the prevention or treatment of CMV infections in humans.
Subject(s)
Antibodies, Viral/immunology , Cytomegalovirus Infections/prevention & control , Viral Envelope Proteins/immunology , Amino Acid Sequence , Animals , Antibodies, Viral/chemistry , Base Sequence , Cell Line , Cytomegalovirus Infections/drug therapy , Humans , Immunoglobulin Variable Region/chemistry , Mice , Molecular Sequence Data , Recombinant Fusion Proteins/immunologyABSTRACT
Oligodeoxyribonucleotide primers based on the 5' ends of bovine IgG1/2 and lambda constant (C) region genes, together with primers encoding conserved amino acids at the N-terminus of mature variable (V) regions from other species, have been used in cDNA and polymerase chain reactions (PCRs) to amplify heavy and light chain V region cDNA from bovine heterohybridomas. The amino acid sequences of VH and V lambda from four bovine immunoglobulins of different specificities are presented.
