Monoclonal antibodies reveal the structural basis of antibody diversity

Jean Luc Teillaud, Catherine Desaymard, Angela M. Giusti, Barbara Haseltine, Roberta R. Pollock, Dale E. Yelton, Donald J. Zack, Matthew D. Scharff

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.

Original languageEnglish (US)
Pages (from-to)721-726
Number of pages6
JournalScience
Volume222
Issue number4625
StatePublished - Dec 1 1983

Fingerprint

Antibody Diversity
Monoclonal Antibodies
Immunoglobulin Genes
Antibody Affinity
Antibody Specificity
Antibodies
Hybridomas
Mutation Rate
Germ Cells
Dissection
Immunoglobulins
Technology
Antigens
Mutation
Genes

ASJC Scopus subject areas

  • General

Cite this

Teillaud, J. L., Desaymard, C., Giusti, A. M., Haseltine, B., Pollock, R. R., Yelton, D. E., ... Scharff, M. D. (1983). Monoclonal antibodies reveal the structural basis of antibody diversity. Science, 222(4625), 721-726.

Monoclonal antibodies reveal the structural basis of antibody diversity. / Teillaud, Jean Luc; Desaymard, Catherine; Giusti, Angela M.; Haseltine, Barbara; Pollock, Roberta R.; Yelton, Dale E.; Zack, Donald J.; Scharff, Matthew D.

In: Science, Vol. 222, No. 4625, 01.12.1983, p. 721-726.

Research output: Contribution to journalArticle

Teillaud, JL, Desaymard, C, Giusti, AM, Haseltine, B, Pollock, RR, Yelton, DE, Zack, DJ & Scharff, MD 1983, 'Monoclonal antibodies reveal the structural basis of antibody diversity', Science, vol. 222, no. 4625, pp. 721-726.
Teillaud JL, Desaymard C, Giusti AM, Haseltine B, Pollock RR, Yelton DE et al. Monoclonal antibodies reveal the structural basis of antibody diversity. Science. 1983 Dec 1;222(4625):721-726.
Teillaud, Jean Luc ; Desaymard, Catherine ; Giusti, Angela M. ; Haseltine, Barbara ; Pollock, Roberta R. ; Yelton, Dale E. ; Zack, Donald J. ; Scharff, Matthew D. / Monoclonal antibodies reveal the structural basis of antibody diversity. In: Science. 1983 ; Vol. 222, No. 4625. pp. 721-726.
@article{0092496fedfa49a5b6800f3936aaa5e0,
title = "Monoclonal antibodies reveal the structural basis of antibody diversity",
abstract = "Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.",
author = "Teillaud, {Jean Luc} and Catherine Desaymard and Giusti, {Angela M.} and Barbara Haseltine and Pollock, {Roberta R.} and Yelton, {Dale E.} and Zack, {Donald J.} and Scharff, {Matthew D.}",
year = "1983",
month = "12",
day = "1",
language = "English (US)",
volume = "222",
pages = "721--726",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "4625",

}

TY - JOUR

T1 - Monoclonal antibodies reveal the structural basis of antibody diversity

AU - Teillaud, Jean Luc

AU - Desaymard, Catherine

AU - Giusti, Angela M.

AU - Haseltine, Barbara

AU - Pollock, Roberta R.

AU - Yelton, Dale E.

AU - Zack, Donald J.

AU - Scharff, Matthew D.

PY - 1983/12/1

Y1 - 1983/12/1

N2 - Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.

AB - Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.

UR - http://www.scopus.com/inward/record.url?scp=0021016599&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021016599&partnerID=8YFLogxK

M3 - Article

VL - 222

SP - 721

EP - 726

JO - Science

JF - Science

SN - 0036-8075

IS - 4625

ER -