Anti-human HB-EGF monoclonal antibodies inhibiting ectodomain shedding of HB-EGF and diphtheria toxin binding

2010 ◽  
Vol 148 (1) ◽  
pp. 55-69 ◽  
Author(s):  
M. Hamaoka ◽  
I. Chinen ◽  
T. Murata ◽  
S. Takashima ◽  
R. Iwamoto ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Diphtheria Toxin ◽  
Ectodomain Shedding ◽  
Toxin Binding

Localization of an N-Domain Region of Angiotensin-Converting Enzyme Involved in the Regulation of Ectodomain Shedding Using Monoclonal Antibodies

2005 ◽  
Vol 4 (2) ◽  
pp. 258-267 ◽  
Author(s):  
Irina V. Balyasnikova ◽  
Zenda L. Woodman ◽  
Ronald F. Albrecht ◽  
Ramanathan Natesh ◽  
K. Ravi Acharya ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Angiotensin Converting Enzyme ◽  
Ectodomain Shedding ◽  
Converting Enzyme

scholarly journals Improved Specificity of a Multiplex Immunoassay for Quantitation of Anti-Diphtheria Toxin Antibodies with the Use of Diphtheria Toxoid

2011 ◽  
Vol 18 (7) ◽  
pp. 1183-1186 ◽  
Author(s):  
Pieter G. M. van Gageldonk ◽  
Christina von Hunolstein ◽  
Fiona R. M. van der Klis ◽  
Guy A. M. Berbers
Keyword(s):  
Diphtheria Toxin ◽  
Neutralization Test ◽  
Diphtheria Toxoid ◽  
Inhibition Assay ◽  
Nonspecific Binding ◽  
Serum Samples ◽  
Multiplex Immunoassay ◽  
Toxin Binding ◽  
Binding Inhibition ◽  
Binding Inhibition Assay

ABSTRACTA nonspecific binding of antibodies to diphtheria toxin, especially in adult serum samples, was observed in our diphtheria-tetanus-pertussis multiplex immunoassay (DTaP4 MIA). This can be significantly reduced by the use of diphtheria toxoid, achieving a good correlation with the Vero cell neutralization test and the toxin binding inhibition assay.

Anti-glycoprotein VI monoclonal antibodies directly aggregate platelets independently of FcγRIIa and induce GPVI ectodomain shedding

Platelets ◽  
2009 ◽  
Vol 20 (2) ◽  
pp. 75-82 ◽  
Author(s):  
Mohammad Al-Tamimi ◽  
Fi-Tjen Mu ◽  
Jane F. Arthur ◽  
Yang Shen ◽  
Masaaki Moroi ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Ectodomain Shedding ◽  
Glycoprotein Vi

Production and characteristics of monoclonal antibodies to the diphtheria toxin

2009 ◽  
Vol 35 (5) ◽  
pp. 556-565
Author(s):  
T. I. Valyakina ◽  
O. E. Lakhtina ◽  
R. L. Komaleva ◽  
M. A. Simonova ◽  
L. V. Samokhvalova ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Diphtheria Toxin

scholarly journals A Mixture of Functionally Oligoclonal Humanized Monoclonal Antibodies That Neutralize Clostridium difficile TcdA and TcdB with High Levels ofIn VitroPotency ShowsIn VivoProtection in a Hamster Infection Model

2013 ◽  
Vol 20 (3) ◽  
pp. 377-390 ◽  
Author(s):  
Nicola L. Davies ◽  
Joanne E. Compson ◽  
Brendon MacKenzie ◽  
Victoria L. O'Dowd ◽  
Amanda K. F. Oxbrow ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Clostridium Difficile ◽  
Neutralizing Antibodies ◽  
Disease Process ◽  
Care Facility ◽  
Infection Model ◽  
Hamster Model ◽  
Content Type ◽  
Toxin Binding

ABSTRACTClostridium difficileinfections are a major cause of antibiotic-associated diarrhea in hospital and care facility patients. In spite of the availability of effective antibiotic treatments,C. difficileinfection (CDI) is still a major cause of patient suffering, death, and substantial health care costs.Clostridium difficileexerts its major pathological effects through the actions of two protein exotoxins, TcdA and TcdB, which bind to and disrupt gut tissue. Antibiotics target the infecting bacteria but not the exotoxins. Administering neutralizing antibodies against TcdA and TcdB to patients receiving antibiotic treatment might modulate the effects of the exotoxins directly. We have developed a mixture of three humanized IgG1 monoclonal antibodies (MAbs) which neutralize TcdA and TcdB to address three clinical needs: reduction of the severity and duration of diarrhea, reduction of death rates, and reduction of the rate of recurrence. The UCB MAb mixture showed higher potency in a variety ofin vitrobinding and neutralization assays (∼10-fold improvements), higher levels of protection in a hamster model of CDI (82% versus 18% at 28 days), and higher valencies of toxin binding (12 versus 2 for TcdA and 3 versus 2 for TcdB) than other agents in clinical development. Comparisons of the MAb properties also offered some insight into the potential relative importance of TcdA and TcdB in the disease process.

scholarly journals Structure-Function Analysis of the Diphtheria Toxin Receptor Toxin Binding Site by Site-directed Mutagenesis

1997 ◽  
Vol 272 (43) ◽  
pp. 27084-27090 ◽  
Author(s):  
Toshihide Mitamura ◽  
Toshiyuki Umata ◽  
Fumie Nakano ◽  
Yuji Shishido ◽  
Tetsuro Toyoda ◽  
...  
Keyword(s):  
Structure Function ◽  
Binding Site ◽  
Diphtheria Toxin ◽  
Function Analysis ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Toxin Binding ◽  
Diphtheria Toxin Receptor ◽  
Toxin Receptor
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