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PMID: 2005389 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A V region mutation in a phosphocholine-binding monoclonal antibody results in loss of antigen binding.

Journal of immunology (Baltimore, Md. : 1950) ·Vol. 146 ·No. 6 ·1991-03-15 ·Pages 2017-20

Kobrin BJ, Buhl S, Shulman MJ, Scharff MD

Abstract

A V region mutant producing an antibody that had lost the ability to bind phosphocholine was isolated from a hybridoma producing a germline encoded T15 antibody. The mutation resulted in a single aspartic acid to asparagine substitution at residue 95 of the H chain V region. This confirms that the aspartic acid at residue 95 plays a major role in Ag binding. The results also suggest that somatic cell genetic techniques can be used to generate mAb with useful changes in Ag binding.

MeSH Terms

Amino Acids/physiology Animals Antibodies, Monoclonal/genetics Base Sequence Immunoglobulin Variable Region/chemistry,genetics Mice Mice, Inbred BALB C Molecular Sequence Data Mutation Phosphorylcholine/immunology Protein Conformation Structure-Activity Relationship

Chemicals

Amino Acids Antibodies, Monoclonal Immunoglobulin Variable Region Phosphorylcholine

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Kobrin B J

Department of Cell Biology, Albert Einstein College of Medicine, Bronx, NY 10461.

Buhl S

Shulman M J

Scharff M D

Article Info

Journal

Journal of immunology (Baltimore, Md. : 1950)

Abbr.

J Immunol

ISSN

0022-1767

Published

1991-03-15

Pages

2017-20

Language

English

Region

United States

NLM ID

2985117R

Subset

Grants

NCI NIH HHS · 5T32 CA 09173-15 · United States

NIAID NIH HHS · AI107072 · United States

NCI NIH HHS · CA39838 · United States

Databases

GENBANK

D10148, D10149, M58659, M58674, M58675, M60429, M60430, M60432, M60434, M60435

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PubMed source View journal details

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A V region mutation in a phosphocholine-binding monoclonal antibody results in loss of antigen binding.

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