High-affinity rat anti-fluorescein monoclonal antibody with unique fine specificity properties including differntail recognition of dynamic ligand analogues

1995 ◽  
Vol 8 (4) ◽  
pp. 258-269 ◽  
Author(s):  
Steven D. Miklasz ◽  
Gene A. Gulliver ◽  
Edward W. Voss
Blood ◽  
2004 ◽  
Vol 104 (8) ◽  
pp. 2540-2542 ◽  
Author(s):  
Mark S. Cragg ◽  
Mike B. Bayne ◽  
Alison L. Tutt ◽  
Ruth R. French ◽  
Stephen Beers ◽  
...  

Abstract The chimeric anti-CD20 monoclonal antibody (mAb), rituximab, is an established part of the management of many non-Hodgkin lymphomas. The in vivo action of rituximab remains elusive, and this partially reflects a lack of highly specific reagents to detect rituximab binding at the cell surface. Here we report a new high-affinity mAb (MB2A4) with fine specificity for the idiotype of rituximab. It is able to detect rituximab in vitro, in the presence of high levels of human immunoglobulin G (IgG), in the serum of patients receiving rituximab therapy, and, surprisingly, when rituximab is bound to CD20 on the cell surface. We propose that the anti–idiotype (Id) binds to rituximab molecules bound univalently at the cell surface, facilitated by the relatively high off-rate of rituximab. This reagent provides new insights into the binding of rituximab at the cell surface and demonstrates a mode of binding that could be exploited for the surface detection of other mAbs with clinical and biologic applications.


2005 ◽  
Vol 296 (1-2) ◽  
pp. 45-62 ◽  
Author(s):  
Sotiris Missailidis ◽  
Despina Thomaidou ◽  
K. Eszter Borbas ◽  
Mike R. Price

Blood ◽  
2010 ◽  
Vol 116 (4) ◽  
pp. 617-624 ◽  
Author(s):  
Yoshihiro Kuwano ◽  
Oliver Spelten ◽  
Hong Zhang ◽  
Klaus Ley ◽  
Alexander Zarbock

Abstract Human blood neutrophils rolling on E- or P-selectin reduced their rolling velocity when intercellular adhesion molecule (ICAM)–1 was available. Similar to mouse neutrophils, this was dependent on P-selectin glycoprotein ligand 1 (PSGL1), αLβ2 integrin, the Src family tyrosine kinase FGR and spleen tyrosine kinase SYK. Blocking phospholipase C or p38 MAP kinase attenuated, but did not abolish the velocity reduction. To test expression of integrin activation epitopes, we adapted an immobilized reporter assay and developed a new homogeneous microfluidics-based reporter antibody binding assay. Rolling on E- or P-selectin induced the extension reporter epitopes KIM127 and NKI-L16, but not the high affinity reporter epitope monoclonal antibody (mAb) 24. This enabled rolling neutrophils to bind to immobilized extension reporter, but not activation reporter antibodies and allowed binding of soluble KIM127 during rolling. We conclude that human neutrophil rolling on E- or P-selectin induces the extended αLβ2 integrin conformation through signaling triggered by PSGL-1 engagement.


mAbs ◽  
2017 ◽  
Vol 10 (1) ◽  
pp. 104-117 ◽  
Author(s):  
Caroline S. Colley ◽  
Bojana Popovic ◽  
Sudharsan Sridharan ◽  
Judit E. Debreczeni ◽  
David Hargeaves ◽  
...  

2008 ◽  
Vol 76 (3) ◽  
pp. 340-352
Author(s):  
Ssucheng J. Hsu ◽  
Amita Patel ◽  
Paul D. Larsen ◽  
David J. Bohmann ◽  
Robert J. Bauer ◽  
...  

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Kasumi Tatsumi ◽  
Gyosuke Sakashita ◽  
Yuko Nariai ◽  
Kosuke Okazaki ◽  
Hiroaki Kato ◽  
...  

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