Recognition of angiotensin II: Antibodies at different levels of an idiotypic network are superimposable

K. Christopher Garcia, Stephen Desiderio, Pierre M. Ronco, Pierre J. Verroust, Mario L Amzel

Research output: Contribution to journalArticle

Abstract

Genetic and sequence information are reported for an angiotensin II-reactive antibody (Ab1, MAb 110) and an anti-anti-idiotypic antibody (Ab3, MAb 131) that have identical antigen binding properties and that are related by an anti-idiotypic antibody (Ab2-β) that satisfies accepted biochemical criteria for an internal image-bearing antibody. The sequences of the variable regions of the Ab3 and of the Ab1 are nearly identical, even though the Ab1 is an antibody to a peptide and the Ab3 is an antibody to a globular protein. Significantly, amino acid residues that make critical contacts with antigen in the crystal structure of the Ab3-antigen complex are highly conserved in Ab1, suggesting that the epitopes of the Ab2-β recognized by the Ab3 do indeed resemble the bound structure of the antigen.

Original languageEnglish (US)
Pages (from-to)528-531
Number of pages4
JournalScience
Volume257
Issue number5069
StatePublished - 1992

Fingerprint

Angiotensin II
Antigens
Anti-Idiotypic Antibodies
Antibodies
Epitopes
Amino Acids
Peptides
Proteins

ASJC Scopus subject areas

  • General

Cite this

Recognition of angiotensin II : Antibodies at different levels of an idiotypic network are superimposable. / Christopher Garcia, K.; Desiderio, Stephen; Ronco, Pierre M.; Verroust, Pierre J.; Amzel, Mario L.

In: Science, Vol. 257, No. 5069, 1992, p. 528-531.

Research output: Contribution to journalArticle

Christopher Garcia, K. ; Desiderio, Stephen ; Ronco, Pierre M. ; Verroust, Pierre J. ; Amzel, Mario L. / Recognition of angiotensin II : Antibodies at different levels of an idiotypic network are superimposable. In: Science. 1992 ; Vol. 257, No. 5069. pp. 528-531.
@article{0fc1b3c2f3f246e0a35a94faa9ec62d9,
title = "Recognition of angiotensin II: Antibodies at different levels of an idiotypic network are superimposable",
abstract = "Genetic and sequence information are reported for an angiotensin II-reactive antibody (Ab1, MAb 110) and an anti-anti-idiotypic antibody (Ab3, MAb 131) that have identical antigen binding properties and that are related by an anti-idiotypic antibody (Ab2-β) that satisfies accepted biochemical criteria for an internal image-bearing antibody. The sequences of the variable regions of the Ab3 and of the Ab1 are nearly identical, even though the Ab1 is an antibody to a peptide and the Ab3 is an antibody to a globular protein. Significantly, amino acid residues that make critical contacts with antigen in the crystal structure of the Ab3-antigen complex are highly conserved in Ab1, suggesting that the epitopes of the Ab2-β recognized by the Ab3 do indeed resemble the bound structure of the antigen.",
author = "{Christopher Garcia}, K. and Stephen Desiderio and Ronco, {Pierre M.} and Verroust, {Pierre J.} and Amzel, {Mario L}",
year = "1992",
language = "English (US)",
volume = "257",
pages = "528--531",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5069",

}

TY - JOUR

T1 - Recognition of angiotensin II

T2 - Antibodies at different levels of an idiotypic network are superimposable

AU - Christopher Garcia, K.

AU - Desiderio, Stephen

AU - Ronco, Pierre M.

AU - Verroust, Pierre J.

AU - Amzel, Mario L

PY - 1992

Y1 - 1992

N2 - Genetic and sequence information are reported for an angiotensin II-reactive antibody (Ab1, MAb 110) and an anti-anti-idiotypic antibody (Ab3, MAb 131) that have identical antigen binding properties and that are related by an anti-idiotypic antibody (Ab2-β) that satisfies accepted biochemical criteria for an internal image-bearing antibody. The sequences of the variable regions of the Ab3 and of the Ab1 are nearly identical, even though the Ab1 is an antibody to a peptide and the Ab3 is an antibody to a globular protein. Significantly, amino acid residues that make critical contacts with antigen in the crystal structure of the Ab3-antigen complex are highly conserved in Ab1, suggesting that the epitopes of the Ab2-β recognized by the Ab3 do indeed resemble the bound structure of the antigen.

AB - Genetic and sequence information are reported for an angiotensin II-reactive antibody (Ab1, MAb 110) and an anti-anti-idiotypic antibody (Ab3, MAb 131) that have identical antigen binding properties and that are related by an anti-idiotypic antibody (Ab2-β) that satisfies accepted biochemical criteria for an internal image-bearing antibody. The sequences of the variable regions of the Ab3 and of the Ab1 are nearly identical, even though the Ab1 is an antibody to a peptide and the Ab3 is an antibody to a globular protein. Significantly, amino acid residues that make critical contacts with antigen in the crystal structure of the Ab3-antigen complex are highly conserved in Ab1, suggesting that the epitopes of the Ab2-β recognized by the Ab3 do indeed resemble the bound structure of the antigen.

UR - http://www.scopus.com/inward/record.url?scp=0026705594&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026705594&partnerID=8YFLogxK

M3 - Article

C2 - 1636087

AN - SCOPUS:0026705594

VL - 257

SP - 528

EP - 531

JO - Science

JF - Science

SN - 0036-8075

IS - 5069

ER -