Pentapeptide Identified as a Monoclonal Antibody Binding Site in the Serine-Protease Domain of t-PA

1994 ◽  
Vol 375 (7) ◽  
pp. 471-480 ◽  
Author(s):  
Frank O. Gombert ◽  
William Werz ◽  
Michael Schlüter ◽  
Anja Bayer ◽  
Rolf G. Werner ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Binding Site ◽  
Serine Protease ◽  
Antibody Binding ◽  
Protease Domain ◽  
Serine Protease Domain ◽  
Antibody Binding Site ◽  
Monoclonal Antibody Binding

Monoclonal antibody binding-site diversity assessment with a cell-based clustering assay

2014 ◽  
Vol 405 ◽  
pp. 1-14 ◽  
Author(s):  
Sindy Liao-Chan ◽  
Joseph Zachwieja ◽  
Steven Gomez ◽  
Dana Duey ◽  
John Lippincott ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Binding Site ◽  
Antibody Binding ◽  
Antibody Binding Site ◽  
Diversity Assessment ◽  
A Cell ◽  
Site Diversity ◽  
Monoclonal Antibody Binding

S-antigen: identification of the MAbA9-C6 monoclonal antibody binding site and the uveitopathogenic sites

1986 ◽  
Vol 5 (12) ◽  
pp. 995-1004 ◽  
Author(s):  
Larry A. Donoso ◽  
Carmen F. Merryman ◽  
Toshimichi Shinohara ◽  
Bernard Dietzschold ◽  
Grame Wistow ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Binding Site ◽  
Antibody Binding ◽  
Antibody Binding Site ◽  
Monoclonal Antibody Binding

scholarly journals Crystal Structure of the Conserved Amino Terminus of the Extracellular Domain of Matrix Protein 2 of Influenza A Virus Gripped by an Antibody

2015 ◽  
Vol 90 (1) ◽  
pp. 611-615 ◽  
Author(s):  
Ki Joon Cho ◽  
Bert Schepens ◽  
Kristof Moonens ◽  
Lei Deng ◽  
Walter Fiers ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Monoclonal Antibody ◽  
Binding Site ◽  
Influenza A Virus ◽  
Influenza A ◽  
Matrix Protein ◽  
Antibody Binding ◽  
Amino Terminus ◽  
Antibody Binding Site ◽  
Protective Antibodies

We report the crystal structure of the M2 ectodomain (M2e) in complex with a monoclonal antibody that binds the amino terminus of M2. M2e extends into the antibody binding site to form an N-terminal β-turn near the bottom of the paratope. This M2e folding differs significantly from that of M2e in complex with an antibody that binds another part of M2e. This suggests that M2e can adopt at least two conformations that can elicit protective antibodies.

Oligosaccharide recognition by antibodies: Synthesis and evaluation of talose oligosaccharide analogues

2002 ◽  
Vol 80 (8) ◽  
pp. 1112-1130 ◽  
Author(s):  
T L Lowary ◽  
E Eichler ◽  
D R Bundle
Keyword(s):  
Monoclonal Antibody ◽  
Molecular Recognition ◽  
Binding Site ◽  
Antibody Binding ◽  
Solution Phase ◽  
O Antigen ◽  
Antibody Binding Site ◽  
Alkyl Groups ◽  
Galactose Residue ◽  
Native Ligand

A series of monosaccharide (4–6), disaccharide (3,7–12), and trisaccharide (13–15) analogs of the native ligand 2, which fills the binding site of monoclonal antibody Se 155.4, have been synthesized and their bioactivity measured by solid- and solution-phase assays. The syntheses of disaccharide analogs sought to replace galactose by various alkyl groups at the O-2 position of mannose. The activity of one of these O-2 alkyl analogs was 75% of that observed for the trisaccharide and points to only weak net bonding between the solvent exposed galactose residue and the antibody binding site. The synthesis of talose analogs 13 and 14, where the mannose or galactose residues of 2 were replaced by talose produced ligands with activities from one-third to one-half of that seen for the native ligand 2. These activity changes did not exhibit discernable correlations with the ability of talose to disrupt water of solvation.Key words: abequose, 3,6-dideoxy-D-xylo-hexose, talose disaccharide and trisaccharide, antibody oligosaccharide interactions, molecular recognition of carbohydrates, water in antibody complexes, Salmonella LPS, monoclonal antibody Se 155.4, bacterial O-antigen.

IgE and monoclonal antibody binding by the mite allergen Der p 7

1996 ◽  
Vol 26 (3) ◽  
pp. 308-315 ◽  
Author(s):  
H.-D. SHEN ◽  
K. Y. CHUA ◽  
W. L. LIN ◽  
H. L. CHEN ◽  
K.-H. HSIEH ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Mite Allergen ◽  
Antibody Binding ◽  
Monoclonal Antibody Binding

An Enzyme-Linked Immunosorbent Assay for Urokinase-Type Plasminogen Activator (u-PA) and Mutants and Chimeras Containing the Serine Protease Domain of u-PA

1992 ◽  
Vol 67 (01) ◽  
pp. 095-100 ◽  
Author(s):  
Paul J Declerck ◽  
Leen Van Keer ◽  
Maria Verstreken ◽  
Désiré Collen
Keyword(s):  
Serine Protease ◽  
Plasminogen Activator ◽  
Active Site ◽  
Enzyme Linked Immunosorbent Assay ◽  
Single Chain ◽  
Protease Domain ◽  
Serine Protease Domain ◽  
Type Plasminogen Activator ◽  
Urokinase Type Plasminogen Activator ◽  
Normal Human

SummaryAn enzyme-linked immunosorbent assay (ELISA) for quantitation of natural and recombinant plasminogen activators containing the serine protease domain (B-chain) of urokinase-type plasminogen activator (u-PA) was developed, based on two murine monoclonal antibodies, MA-4D1E8 and MA-2L3, raised against u-PA and reacting with non-overlapping epitopes in the B-chain. MA-4D1E8 was coated on microtiter plates and bound antigen was quantitated with MA-2L3 conjugated with horseradish peroxidase. The intra-assay, inter-assay and inter-dilution coefficients of variation of the assay were 6%, 15% and 9%, respectively. Using recombinant single-chain u-PA (rscu-PA) as a standard, the u-PA-related antigen level in normal human plasma was 1.4 ± 0.6 ng/ml (mean ± SD, n = 27).The ELISA recognized the following compounds with comparable sensitivity: intact scu-PA (amino acids, AA, 1 to 411), scu-PA-32k (AA 144 to 411), a truncated (thrombin-derived) scu-PA comprising A A 157 to 411, and chimeric t-PA/u-PA molecules including t-PA(AA1-263)/scu-PA(AA144-411), t-PA(AA1-274)/scu-PA(AA138-411) and t-PA(AA87-274)/scu-PA(AA138-411). Conversion of single-chain to two-chain forms of u-PA or inhibition of active two-chain forms with plasminogen activator inhibitor-1 or with the active site serine inhibitor phenyl-methyl-sulfonyl fluoride, did not alter the reactivity in the assay. In contrast, inactivation with α2-antiplasmin or with the active site histidine inhibitor Glu-Gly-Arg-CH2Cl resulted in a 3- to 5-fold reduction of the reactivity. When purified scu-PA-32k was added to pooled normal human plasma at final concentrations ranging from 20 to 1,000 ng/ml, recoveries in the ELISA were between 84 and 110%.The assay was successfully applied for the quantitation of pharmacological levels of scu-PA and t-PA(AA87_274)/scu-PA(AA138-411) in plasma during experimental thrombolysis in baboons.Thus the present ELISA, which is specifically dependent on the presence of the serine protease part of u-PA, is useful for measurement of a wide variety of variants and chimeras of u-PA which are presently being developed for improved thrombolytic therapy.

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