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 language | English (US) |
|---|---|
| Pages (from-to) | 211-222 |
| Number of pages | 12 |
| Journal | Journal of Experimental Medicine |
| Volume | 165 |
| Issue number | 1 |
| State | Published - 1987 |
| Externally published | Yes |
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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 journal › Article
}
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.
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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 -