Natural auto- and polyreactive antibodies differing from antigen-induced antibodies in the H chain CDR3

Ching Chen, Mary Stenzel-Poore, Marvin Rittenberg

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

We describe three sets of natural (preimmune) polyreactive antibodies and Ag-induced antibodies that share the same VH-VL combinations. The amino acid homology in the VH and VL segments averaged 92%. These sets were found among 49 neonatal and adult natural mAb that were compared with 35 Ag-induced monoclonals produced during the memory response to phosphocholine (PC)-keyhole limpet hemocyanin. Both groups of monoclonals had been selected on the basis of a restricted fine specificity pattern, namely the ability to recognize PC-protein and p-nitrophenyl phosphocholine but not PC. All of the antibodies were tested for reactivity against a panel of 15 self and foreign Ag. Despite their common fine specificity as the basis for selection, 33/49 natural antibodies were poly/auto reactive whereas 0/35 Ag-induced antibodies had such poly/auto reactive properties. The natural antibodies were encoded by genes representing nine different VH families and several Vκ and Vλ families. There were a few replacement substitutions distinguishing the Ag-induced antibodies from the natural antibodies in each set; however, the most noteworthy difference was the extreme variability of CDR3 in the natural antibodies that differed in both length and amino acid sequence from each other and from Ag-induced antibodies. The results suggest that CDR3 of the H chain may play a critical role in distinguishing poly- from monospecific combining sites in natural and Ag-induced antibodies.

Original languageEnglish (US)
Pages (from-to)2359-2367
Number of pages9
JournalJournal of Immunology
Volume147
Issue number7
StatePublished - Oct 1 1991

Fingerprint

Antigens
Antibodies
Phosphorylcholine
Aptitude
Amino Acid Sequence
Binding Sites
Amino Acids
Genes
Proteins

ASJC Scopus subject areas

  • Immunology

Cite this

Natural auto- and polyreactive antibodies differing from antigen-induced antibodies in the H chain CDR3. / Chen, Ching; Stenzel-Poore, Mary; Rittenberg, Marvin.

In: Journal of Immunology, Vol. 147, No. 7, 01.10.1991, p. 2359-2367.

Research output: Contribution to journalArticle

@article{05b9763a93ce42b580f1946d3a7095b7,
title = "Natural auto- and polyreactive antibodies differing from antigen-induced antibodies in the H chain CDR3",
abstract = "We describe three sets of natural (preimmune) polyreactive antibodies and Ag-induced antibodies that share the same VH-VL combinations. The amino acid homology in the VH and VL segments averaged 92{\%}. These sets were found among 49 neonatal and adult natural mAb that were compared with 35 Ag-induced monoclonals produced during the memory response to phosphocholine (PC)-keyhole limpet hemocyanin. Both groups of monoclonals had been selected on the basis of a restricted fine specificity pattern, namely the ability to recognize PC-protein and p-nitrophenyl phosphocholine but not PC. All of the antibodies were tested for reactivity against a panel of 15 self and foreign Ag. Despite their common fine specificity as the basis for selection, 33/49 natural antibodies were poly/auto reactive whereas 0/35 Ag-induced antibodies had such poly/auto reactive properties. The natural antibodies were encoded by genes representing nine different VH families and several Vκ and Vλ families. There were a few replacement substitutions distinguishing the Ag-induced antibodies from the natural antibodies in each set; however, the most noteworthy difference was the extreme variability of CDR3 in the natural antibodies that differed in both length and amino acid sequence from each other and from Ag-induced antibodies. The results suggest that CDR3 of the H chain may play a critical role in distinguishing poly- from monospecific combining sites in natural and Ag-induced antibodies.",
author = "Ching Chen and Mary Stenzel-Poore and Marvin Rittenberg",
year = "1991",
month = "10",
day = "1",
language = "English (US)",
volume = "147",
pages = "2359--2367",
journal = "Journal of Immunology",
issn = "0022-1767",
publisher = "American Association of Immunologists",
number = "7",

}

TY - JOUR

T1 - Natural auto- and polyreactive antibodies differing from antigen-induced antibodies in the H chain CDR3

AU - Chen, Ching

AU - Stenzel-Poore, Mary

AU - Rittenberg, Marvin

PY - 1991/10/1

Y1 - 1991/10/1

N2 - We describe three sets of natural (preimmune) polyreactive antibodies and Ag-induced antibodies that share the same VH-VL combinations. The amino acid homology in the VH and VL segments averaged 92%. These sets were found among 49 neonatal and adult natural mAb that were compared with 35 Ag-induced monoclonals produced during the memory response to phosphocholine (PC)-keyhole limpet hemocyanin. Both groups of monoclonals had been selected on the basis of a restricted fine specificity pattern, namely the ability to recognize PC-protein and p-nitrophenyl phosphocholine but not PC. All of the antibodies were tested for reactivity against a panel of 15 self and foreign Ag. Despite their common fine specificity as the basis for selection, 33/49 natural antibodies were poly/auto reactive whereas 0/35 Ag-induced antibodies had such poly/auto reactive properties. The natural antibodies were encoded by genes representing nine different VH families and several Vκ and Vλ families. There were a few replacement substitutions distinguishing the Ag-induced antibodies from the natural antibodies in each set; however, the most noteworthy difference was the extreme variability of CDR3 in the natural antibodies that differed in both length and amino acid sequence from each other and from Ag-induced antibodies. The results suggest that CDR3 of the H chain may play a critical role in distinguishing poly- from monospecific combining sites in natural and Ag-induced antibodies.

AB - We describe three sets of natural (preimmune) polyreactive antibodies and Ag-induced antibodies that share the same VH-VL combinations. The amino acid homology in the VH and VL segments averaged 92%. These sets were found among 49 neonatal and adult natural mAb that were compared with 35 Ag-induced monoclonals produced during the memory response to phosphocholine (PC)-keyhole limpet hemocyanin. Both groups of monoclonals had been selected on the basis of a restricted fine specificity pattern, namely the ability to recognize PC-protein and p-nitrophenyl phosphocholine but not PC. All of the antibodies were tested for reactivity against a panel of 15 self and foreign Ag. Despite their common fine specificity as the basis for selection, 33/49 natural antibodies were poly/auto reactive whereas 0/35 Ag-induced antibodies had such poly/auto reactive properties. The natural antibodies were encoded by genes representing nine different VH families and several Vκ and Vλ families. There were a few replacement substitutions distinguishing the Ag-induced antibodies from the natural antibodies in each set; however, the most noteworthy difference was the extreme variability of CDR3 in the natural antibodies that differed in both length and amino acid sequence from each other and from Ag-induced antibodies. The results suggest that CDR3 of the H chain may play a critical role in distinguishing poly- from monospecific combining sites in natural and Ag-induced antibodies.

UR - http://www.scopus.com/inward/record.url?scp=0026040197&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026040197&partnerID=8YFLogxK

M3 - Article

C2 - 1918968

AN - SCOPUS:0026040197

VL - 147

SP - 2359

EP - 2367

JO - Journal of Immunology

JF - Journal of Immunology

SN - 0022-1767

IS - 7

ER -