The glycosylphosphatidylinositol-anchored form and the transmembrane form of CD58 are released from the cell surface upon antibody binding

1997 ◽  
Vol 56 ◽  
pp. 95
Author(s):  
D. Itzhaky ◽  
N. Hollander
Keyword(s):  
Cell Surface ◽  
Antibody Binding

Steric hindrance as a factor in the reaction of labeled antibody with cell surface antigenic determinants.

1978 ◽  
Vol 26 (8) ◽  
pp. 618-621 ◽  
Author(s):  
S P Kent ◽  
K H Ryan ◽  
A L Siegel
Keyword(s):  
Cell Surface ◽  
Surface Antigen ◽  
Steric Hindrance ◽  
Antibody Binding ◽  
Antigenic Determinants ◽  
Human Igg ◽  
Chromic Chloride

The binding of rabbit anti-human IgG labeled with 125I, shellfish glycogen or ferritin to human IgG attached to the surface of rabbit RBC with chromic chloride was studied. Maximum binding was noted with 125I labeled antibody. Slightly but consistently less binding was found with shellfish glycogen labeled antibody. The binding of ferritin labeled antibody was strikingly reduced--usually one-third or less of that found with 125I labeled antibody alone. This suggests that under the conditions of these experiments, the attachment of large labels to antibody molecules results in reduced antibody binding to surface antigen. Steric hindrance is probably at least in part responsible for this reduced binding.

scholarly journals Suramin inhibits antibody binding to cell surface antigens and disrupts complement-mediated mesangial cell lysis

2016 ◽  
Vol 132 (4) ◽  
pp. 224-234 ◽  
Author(s):  
Honglan Piao ◽  
Yuan Chi ◽  
Xiling Zhang ◽  
Zhen Zhang ◽  
Kun Gao ◽  
...  
Keyword(s):  
Cell Surface ◽  
Mesangial Cell ◽  
Surface Antigens ◽  
Cell Lysis ◽  
Antibody Binding ◽  
Cell Surface Antigens

scholarly journals Binding site localization on non-homogeneous cell surfaces using topological image averaging

2020 ◽  
Author(s):  
Vibha Kumra Ahnlide ◽  
Johannes Kumra Ahnlide ◽  
Jason P. Beech ◽  
Pontus Nordenfelt
Keyword(s):  
Cell Surface ◽  
Binding Site ◽  
Antibody Binding ◽  
Surface Proteins ◽  
High Throughput Analysis ◽  
Native Cell ◽  
Site Localization ◽  
Homogeneous Cell ◽  
Image Averaging ◽  
Therapeutic Monoclonal Antibodies

Antibody binding to cell surface proteins plays a crucial role in immunity and the location of an epitope can altogether determine the immunological outcome of a host-target interaction. Techniques available today for epitope identification are costly, time-consuming, and unsuited for high-throughput analysis. Fast and efficient screening of epitope location can be useful for the development of therapeutic monoclonal antibodies and vaccines. In the present work, we have developed a method for imaging-based localization of binding sites on cellular surface proteins. The cellular morphology typically varies, and antibodies often bind in a non-homogenous manner, making traditional particle-averaging strategies challenging for accurate native antibody localization. Nanometer-scale resolution is achieved through localization in one dimension, namely the distance from a bound ligand to a reference surface, by using topological image averaging. Our results show that this method is well suited for antibody binding site measurements on native cell surface morphology.

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