The molecular and biochemical characterization of mutant monoclonal antibodies with increased antigen binding

Deborah L. French, Roberta R. Pollock, Hector L. Aguila, Matthew D. Scharff

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Mutant mAb with increased Ag binding were generated from a hybridoma cell line, 36-65, that secretes an IgG1,κ anti-p-azophenylarsonate-(Ars) specific antibody. The mutant antibodies were identified using an Ars-specific ELISA and sib selection so that approximately 106 cells could be analyzed. The ELISA used as Ag a low ratio of Ars coupled to BSA and was set up so that only those antibodies that had higher binding than the parent would be detected. Seven mutant producing cell lines were isolated from five independent clones of 36-65. The mutant antibodies bind Ag 20 to more than 200-fold better than the parent and have wild type V region sequences. All have C region mutations that result in an increased avidity. At least five different genetic events are responsible for the C region mutations.

Original languageEnglish (US)
Pages (from-to)2010-2016
Number of pages7
JournalJournal of Immunology
Volume146
Issue number6
StatePublished - Mar 15 1991

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Monoclonal Antibodies
Antigens
Antibodies
p-Azobenzenearsonate
Enzyme-Linked Immunosorbent Assay
Cell Line
Mutation
Hybridomas
Clone Cells
Immunoglobulin G

ASJC Scopus subject areas

  • Immunology

Cite this

The molecular and biochemical characterization of mutant monoclonal antibodies with increased antigen binding. / French, Deborah L.; Pollock, Roberta R.; Aguila, Hector L.; Scharff, Matthew D.

In: Journal of Immunology, Vol. 146, No. 6, 15.03.1991, p. 2010-2016.

Research output: Contribution to journalArticle

French, Deborah L. ; Pollock, Roberta R. ; Aguila, Hector L. ; Scharff, Matthew D. / The molecular and biochemical characterization of mutant monoclonal antibodies with increased antigen binding. In: Journal of Immunology. 1991 ; Vol. 146, No. 6. pp. 2010-2016.
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