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cDNA to a plant virus-monoclonal antibody gene was cloned and sequenced. The source of mRNAs was a hybridoma producing an IgG3 monoclonal antibody (42C07) which bound to a coat protein of potato virus Y. We have constructed cDNA libraries using a bacteriophage lambda ZAP II vector from the mRNA of the hybridomas. Screening of the libraries with polymerase chain reaction-mediated probes specific to variable and a part of constant regions of the heavy and light chain genes yielded clones of both chains. Numbers of the nucleotides encoding heavy and light chains were 1383 and 717, and numbers of the deduced amino acids were 461 and 239, respectively. Comparisons of the deduced amino acid sequences with those of other immunoglobulin (Ig) previously reported showed that they were full-length of the antibody gene. Furthermore, the heavy and light chains of 42C07 were successfully expressed separately in Escherichia coli as judged by reactivities with anti-mouse Ig antibody.

Molecular Cloning and Nucleotide Sequences of Heavy and Light Chain Genes of a Monoclonal Antibody to Potato Virus Y Coat Protein.