Characterization of monoclonal antibodies recognizing HLA-G or HLA-E: new tools to analyze the expression of nonclassical HLA class I molecules

2003 ◽  
Vol 64 (3) ◽  
pp. 315-326 ◽  
Author(s):  
Catherine Menier ◽  
Berta Saez ◽  
Vaclav Horejsi ◽  
Silvia Martinozzi ◽  
Irene Krawice-Radanne ◽  
...  
1989 ◽  
Vol 26 ◽  
pp. 16
Author(s):  
D Geraghty ◽  
S Orcutt ◽  
T Staggs ◽  
J Hansen

Blood ◽  
1992 ◽  
Vol 79 (11) ◽  
pp. 2901-2908 ◽  
Author(s):  
E Rubinstein ◽  
I Urso ◽  
C Boucheix ◽  
RC Carroll

Abstract The effect on platelet activation of monoclonal antibodies directed against common determinants of the HLA class I heavy chain molecule was studied. Cross-linking W6/32, an anti-HLA class I of IgG2a subclass, led to platelet activation. Two other antibodies of the same subclass did not have this effect on platelets. The lack of activity of the F(ab')2 fragments suggests that the activation signal is mediated by the platelet Fc receptor (Fc gamma RII). Indeed, except for a higher sensitivity of W6/32 to aspirin and apyrase, activations by cross- linking IV-3 (an anti-Fc gamma RII) and W6/32 are similar at the level of InsP3 formation, calcium mobilization, pH modifications, and activation of protein kinase C and myosin kinase. When HLA class I molecules and Fc gamma RII are cross-linked together, platelet activation occurs. This is not observed when a control IgG2a is substituted for W6/32 or when CD9 and Fc receptor are cross-linked together. This suggests that HLA class I molecules and Fc gamma RII synergize to activate platelets.


1990 ◽  
Vol 172 (3) ◽  
pp. 827-834 ◽  
Author(s):  
J A Frelinger ◽  
F M Gotch ◽  
H Zweerink ◽  
E Wain ◽  
A J McMichael

We have tested the binding of HLA class I proteins to peptides using a solid-phase binding assay. We tested 102 peptides, mostly derived from the HIV gag and HIV pol sequences. Most peptides did not bind to any class I protein tested. The pattern of binding among the three class I proteins tested, HLA-A2, -B27, and -B8, was approximately 85% concordant. Further, all five of the known HIV-1 gag T cell epitopes detected by human CTL bound at least one class I protein. Binding of class I to the peptides could be detected either by directly iodinated class I proteins, or indirectly using monoclonal antibodies specific for class I. The binding to the plates could be blocked with MA2.1, which binds in the alpha 1 region of A2, but not by W6/32, which binds elsewhere. The data presented here show that binding of class I to peptides is specific, but that many peptides bind to more than a single class I protein.


Blood ◽  
1992 ◽  
Vol 79 (11) ◽  
pp. 2901-2908
Author(s):  
E Rubinstein ◽  
I Urso ◽  
C Boucheix ◽  
RC Carroll

The effect on platelet activation of monoclonal antibodies directed against common determinants of the HLA class I heavy chain molecule was studied. Cross-linking W6/32, an anti-HLA class I of IgG2a subclass, led to platelet activation. Two other antibodies of the same subclass did not have this effect on platelets. The lack of activity of the F(ab')2 fragments suggests that the activation signal is mediated by the platelet Fc receptor (Fc gamma RII). Indeed, except for a higher sensitivity of W6/32 to aspirin and apyrase, activations by cross- linking IV-3 (an anti-Fc gamma RII) and W6/32 are similar at the level of InsP3 formation, calcium mobilization, pH modifications, and activation of protein kinase C and myosin kinase. When HLA class I molecules and Fc gamma RII are cross-linked together, platelet activation occurs. This is not observed when a control IgG2a is substituted for W6/32 or when CD9 and Fc receptor are cross-linked together. This suggests that HLA class I molecules and Fc gamma RII synergize to activate platelets.


2010 ◽  
Vol 103 (2) ◽  
pp. 197-206 ◽  
Author(s):  
Courtney Smith ◽  
Mariarita Santi ◽  
Elisabeth J. Rushing ◽  
Robert Cornelison ◽  
Tobey J. MacDonald ◽  
...  

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