scholarly journals Camelid‐derived single‐chain antibodies in hemostasis: Mechanistic, diagnostic, and therapeutic applications

2020 ◽  
Vol 4 (7) ◽  
pp. 1087-1110
Author(s):  
Ivan Peyron ◽  
Claire Kizlik‐Masson ◽  
Marie‐Daniéla Dubois ◽  
Sénadé Atsou ◽  
Stephen Ferrière ◽  
...  
Keyword(s):  
Single Chain ◽  
Therapeutic Applications ◽  
Single Chain Antibodies

scholarly journals Identification of single chain antibodies to breast cancer stem cells using phage display

2009 ◽  
pp. NA-NA ◽  
Author(s):  
Deniz Gur ◽  
Suling Liu ◽  
Anurag Shukla ◽  
Stephanie C Pero ◽  
Max S Wicha ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Stem Cells ◽  
Cancer Stem Cells ◽  
Phage Display ◽  
Breast Cancer Stem Cells ◽  
Single Chain ◽  
Single Chain Antibodies

Optimization of the expression of single-chain antibodies using different Escherichia coli systems

2007 ◽  
Vol 131 (2) ◽  
pp. S251-S252
Author(s):  
Symon Riedstra ◽  
Gonçalo Leite ◽  
Carolina Ferreira ◽  
Francisco Brás Gomes ◽  
Paulo M.P. Costa ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Single Chain ◽  
Single Chain Antibodies

scholarly journals Development and Characterization of Nanobodies Targeting the Kupffer Cell

2021 ◽  
Vol 12 ◽  
Author(s):  
Fang Zheng ◽  
Jinhong Zhou ◽  
Zhenlin Ouyang ◽  
Jiaxin Zhang ◽  
Xinyi Wang ◽  
...  
Keyword(s):  
Kupffer Cell ◽  
Cell Receptor ◽  
Therapeutic Agents ◽  
Membrane Receptors ◽  
Single Chain ◽  
Single Chain Antibodies ◽  
Functional Investigation ◽  
And Function ◽  
Distinct Features

Nanobodies that are derived from single-chain antibodies of camelids have served as powerful tools in diagnostics, therapeutics and investigation of membrane receptors' structure and function. In this study, we developed a series of nanobodies by a phage display screening building from lymphocytes isolated from an alpaca immunized with recombinant mouse Kupffer cell receptor Clec4F, which is involved in pathogen recognition by binding to galactose and N-acetylgalactosamine. Bio-panning selections retrieved 14 different nanobodies against Clec4F with an affinity ranging from 0.2 to 2 nM as determined by SPR. Those nanobodies mainly recognize 4 different epitopes as analyzed via competitive epitope binning. By analysis of the radioactivity in each organ after injection of 99mTc labeled Clec4F nanobodies in naïve mice, we found that these nanobodies are targeting the liver. Furthermore, we performed a structural characterization at atomic resolution of two of the Clec4F nanobodies from different epitope groups, which revealed distinct features within the CDR2 and CDR3 regions. Taken together, we developed a series of nanobodies targeting multiple distinct recognition epitopes of the Kupffer cell-specific receptor Clec4F which may be useful for its structural and functional investigation as well as for use as molecular imaging and therapeutic agents.

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