New family of exon-shuffled recombinant genes reveals extensive interdomain interactions in class I histocompatibility antigens and identifies residues involved

M. J. Darsley, H. Takahashi, M. J. Macchi, Jeffrey A Frelinger, K. Ozato, E. Appella

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The specificities of an extensive panel of anti-H-2D(d) monoclonal antibodies, which had been previously characterized using exon-shuffled H-δ(d)/H-2L(d) molecules and a number of anti-H-2D(p) antibodies, were examined using H-2D(d)/H-2D(p) recombinants. The use of this new family of recombinant antigens revealed extensive interaction between the membrane-distal (N and C1) domains of class I molecules, 20 out of 48 mAbs recognize complex epitopes formed by the interaction of these two domains. These antibodies exhibit a number of distinct patterns of crossreactivity with other class I proteins, revealing the presence of multiple epitopes within the region of domain interaction. Comparison of the data presented here with those from previous work allowed the identification of a small number of residues in the C1 domain that participate in the generation of complex epitopes involving both the N and C1 domains. The results are discussed in terms of the structural information available for these two domains.

Original languageEnglish (US)
Pages (from-to)211-222
Number of pages12
JournalJournal of Experimental Medicine
Volume165
Issue number1
StatePublished - 1987
Externally publishedYes

Fingerprint

Histocompatibility Antigens Class I
Epitopes
Exons
Genes
Antibodies
Monoclonal Antibodies
Antigens
Membranes
Proteins

ASJC Scopus subject areas

  • Immunology

Cite this

New family of exon-shuffled recombinant genes reveals extensive interdomain interactions in class I histocompatibility antigens and identifies residues involved. / Darsley, M. J.; Takahashi, H.; Macchi, M. J.; Frelinger, Jeffrey A; Ozato, K.; Appella, E.

In: Journal of Experimental Medicine, Vol. 165, No. 1, 1987, p. 211-222.

Research output: Contribution to journalArticle

@article{c9ee517b4a304bc8af25c60b4d6c7ff2,
title = "New family of exon-shuffled recombinant genes reveals extensive interdomain interactions in class I histocompatibility antigens and identifies residues involved",
abstract = "The specificities of an extensive panel of anti-H-2D(d) monoclonal antibodies, which had been previously characterized using exon-shuffled H-δ(d)/H-2L(d) molecules and a number of anti-H-2D(p) antibodies, were examined using H-2D(d)/H-2D(p) recombinants. The use of this new family of recombinant antigens revealed extensive interaction between the membrane-distal (N and C1) domains of class I molecules, 20 out of 48 mAbs recognize complex epitopes formed by the interaction of these two domains. These antibodies exhibit a number of distinct patterns of crossreactivity with other class I proteins, revealing the presence of multiple epitopes within the region of domain interaction. Comparison of the data presented here with those from previous work allowed the identification of a small number of residues in the C1 domain that participate in the generation of complex epitopes involving both the N and C1 domains. The results are discussed in terms of the structural information available for these two domains.",
author = "Darsley, {M. J.} and H. Takahashi and Macchi, {M. J.} and Frelinger, {Jeffrey A} and K. Ozato and E. Appella",
year = "1987",
language = "English (US)",
volume = "165",
pages = "211--222",
journal = "Journal of Experimental Medicine",
issn = "0022-1007",
publisher = "Rockefeller University Press",
number = "1",

}

TY - JOUR

T1 - New family of exon-shuffled recombinant genes reveals extensive interdomain interactions in class I histocompatibility antigens and identifies residues involved

AU - Darsley, M. J.

AU - Takahashi, H.

AU - Macchi, M. J.

AU - Frelinger, Jeffrey A

AU - Ozato, K.

AU - Appella, E.

PY - 1987

Y1 - 1987

N2 - The specificities of an extensive panel of anti-H-2D(d) monoclonal antibodies, which had been previously characterized using exon-shuffled H-δ(d)/H-2L(d) molecules and a number of anti-H-2D(p) antibodies, were examined using H-2D(d)/H-2D(p) recombinants. The use of this new family of recombinant antigens revealed extensive interaction between the membrane-distal (N and C1) domains of class I molecules, 20 out of 48 mAbs recognize complex epitopes formed by the interaction of these two domains. These antibodies exhibit a number of distinct patterns of crossreactivity with other class I proteins, revealing the presence of multiple epitopes within the region of domain interaction. Comparison of the data presented here with those from previous work allowed the identification of a small number of residues in the C1 domain that participate in the generation of complex epitopes involving both the N and C1 domains. The results are discussed in terms of the structural information available for these two domains.

AB - The specificities of an extensive panel of anti-H-2D(d) monoclonal antibodies, which had been previously characterized using exon-shuffled H-δ(d)/H-2L(d) molecules and a number of anti-H-2D(p) antibodies, were examined using H-2D(d)/H-2D(p) recombinants. The use of this new family of recombinant antigens revealed extensive interaction between the membrane-distal (N and C1) domains of class I molecules, 20 out of 48 mAbs recognize complex epitopes formed by the interaction of these two domains. These antibodies exhibit a number of distinct patterns of crossreactivity with other class I proteins, revealing the presence of multiple epitopes within the region of domain interaction. Comparison of the data presented here with those from previous work allowed the identification of a small number of residues in the C1 domain that participate in the generation of complex epitopes involving both the N and C1 domains. The results are discussed in terms of the structural information available for these two domains.

UR - http://www.scopus.com/inward/record.url?scp=0023104686&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023104686&partnerID=8YFLogxK

M3 - Article

C2 - 2432149

AN - SCOPUS:0023104686

VL - 165

SP - 211

EP - 222

JO - Journal of Experimental Medicine

JF - Journal of Experimental Medicine

SN - 0022-1007

IS - 1

ER -