Hyperimmunised bovine milk and whey: influence of pH and enzymatic treatments on the antigen-binding capacity of immunoglobulin G

2015 ◽  
Vol 96 (5) ◽  
pp. 1814-1820
Author(s):  
Julia Dugnol ◽  
Francisco A Riera
AMB Express ◽  
2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Sinead T. Morrin ◽  
Geoffrey McCarthy ◽  
Deirdre Kennedy ◽  
Mariarosaria Marotta ◽  
Jane A. Irwin ◽  
...  

Genes ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 38
Author(s):  
Takehiro Mukae ◽  
Sho Okumura ◽  
Takuma Watanobe ◽  
Kyoko Yoshii ◽  
Takahiro Tagami ◽  
...  

Increased commercial demand for monoclonal antibodies (mAbs) has resulted in the urgent need to establish efficient production systems. We previously developed a transgenic chicken bioreactor system that effectively produced human cytokines in egg whites using genome-edited transgenic chickens. Here, we describe the application of this system to mAb production. The genes encoding the heavy and light chains of humanized anti-HER2 mAb, linked by a 2A peptide sequence, were integrated into the chicken ovalbumin gene locus using a CRISPR/Cas9 protocol. The knock-in hens produced a fully assembled humanized mAb in their eggs. The mAb expression level in the egg white was 1.4–1.9 mg/mL, as determined by ELISA. Furthermore, the antigen binding affinity of the anti-HER2 mAb obtained was estimated to be equal to that of the therapeutic anti-HER2 mAb (trastuzumab). In addition, antigen-specific binding by the egg white mAb was demonstrated by immunofluorescence against HER2-positive and -negative cells. These results indicate that the chicken bioreactor system can efficiently produce mAbs with antigen binding capacity and can serve as an alternative production system for commercial mAbs.


Toxicon ◽  
2002 ◽  
Vol 40 (7) ◽  
pp. 857-861 ◽  
Author(s):  
C Maya Devi ◽  
M Vasantha Bai ◽  
L.K Krishnan

2016 ◽  
Vol 1466 ◽  
pp. 105-112 ◽  
Author(s):  
Hyo Jin Kang ◽  
Weonu Choe ◽  
Jeong-Ki Min ◽  
Young-mi Lee ◽  
B. Moon Kim ◽  
...  

1973 ◽  
Vol 59 (5) ◽  
pp. 927 ◽  
Author(s):  
Bernard Halpern ◽  
Richard A. Albach ◽  
James G. Shaffer ◽  
Ralph E. Dolkart

2006 ◽  
Vol 72 (11) ◽  
pp. 7394-7397 ◽  
Author(s):  
Jane A. Brockelbank ◽  
Verena Peters ◽  
Bernd H. A. Rehm

ABSTRACT The immunoglobulin G (IgG) binding ZZ domain of protein A from Staphylococcus aureus was fused to the N terminus of the polyhydroxyalkanoate (PHA) synthase from Cupriavidus necator. The fusion protein was confirmed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry and mediated formation of ZZ domain-displaying PHA granules in recombinant Escherichia coli. The IgG binding capacity of isolated granules was assessed using enzyme-linked immunosorbent assay and could be enhanced by the overproduction of the ZZ-PHA synthase. ZZ-PHA granules enabled efficient purification of IgG from human serum.


2013 ◽  
Vol 36 (15) ◽  
pp. 2387-2393 ◽  
Author(s):  
Shasha Dong ◽  
Liang Chen ◽  
Bin Dai ◽  
Wilfred Johnson ◽  
Jialei Ye ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document