Development of human antibody fragments directed towards synaptic acetylcholinesterase using a semi-synthetic phage display library

2002 ◽  
pp. 165-179 ◽  
Author(s):  
C. Flores-Flores ◽  
A. Nissim ◽  
S. Shochat ◽  
H. Soreq
Keyword(s):  
Phage Display ◽  
Phage Display Library ◽  
Antibody Fragments ◽  
Human Antibody

Human Antibody Fragments Specific for Human Blood Group Antigens from a Phage Display Library

1993 ◽  
Vol 11 (10) ◽  
pp. 1145-1149 ◽  
Author(s):  
James D. Marks ◽  
Willem H. Ouwehand ◽  
Jacqueline M. Bye ◽  
Ricarda Finnern ◽  
Barbara D. Gorick ◽  
...  
Keyword(s):  
Phage Display ◽  
Blood Group ◽  
Human Blood ◽  
Phage Display Library ◽  
Antibody Fragments ◽  
Human Antibody ◽  
Blood Group Antigens ◽  
Human Blood Group

scholarly journals A novel and effective approach to generate germline-like monoclonal antibodies by integration of phage and mammalian cell display platforms

2021 ◽  
Author(s):  
Yu-jia Jin ◽  
Diao Yu ◽  
Xiao-long Tian ◽  
Hui-xian Li ◽  
Xiao-chao Zhou ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Phage Display ◽  
Mammalian Cell ◽  
Phage Display Library ◽  
Antibody Fragments ◽  
Human Antibody ◽  
Phage Display Technology ◽  
Mammalian Cell Display

AbstractPhage display technology allows for rapid selection of antibodies from the large repertoire of human antibody fragments displayed on phages. However, antibody fragments should be converted to IgG for biological characterizations and affinity of antibodies obtained from phage display library is frequently not sufficient for efficient use in clinical settings. Here, we describe a new approach that combines phage and mammalian cell display, enabling simultaneous affinity screening of full-length IgG antibodies. Using this strategy, we successfully obtained a novel germline-like anti-TIM-3 monoclonal antibody named m101, which was revealed to be a potent anti-TIM-3 therapeutic monoclonal antibody via in vitro and in vivo experiments, indicating its effectiveness and power. Thus, this platform can help develop new monoclonal antibody therapeutics with high affinity and low immunogenicity.

1278 Targeting anti-fibrogenic therapeutics to hepatic stellate cells — generating human antibody fragments by phage display

Hepatology ◽  
2003 ◽  
Vol 38 ◽  
pp. 775-775
Author(s):  
L ELRICK ◽  
V LEEL ◽  
C MAREK ◽  
N KORUTH ◽  
K CHARLTON ◽  
...  
Keyword(s):  
Phage Display ◽  
Hepatic Stellate Cells ◽  
Stellate Cells ◽  
Antibody Fragments ◽  
Human Antibody

Single chain variable fragment antibodies against Shiga toxins isolated from a human antibody phage display library

Vaccine ◽  
2011 ◽  
Vol 29 (33) ◽  
pp. 5340-5346 ◽  
Author(s):  
Paola Neri ◽  
Naoko Shigemori ◽  
Susumu Hamada-Tsutsumi ◽  
Kentaro Tsukamoto ◽  
Hideyuki Arimitsu ◽  
...  
Keyword(s):  
Phage Display ◽  
Phage Display Library ◽  
Human Antibody ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Shiga Toxins ◽  
Antibody Phage ◽  
Antibody Phage Display

scholarly journals Neutralizing Antibodies of Botulinum Neurotoxin Serotype A Screened from a Fully Synthetic Human Antibody Phage Display Library

2009 ◽  
Vol 14 (8) ◽  
pp. 991-998 ◽  
Author(s):  
Rui Yu ◽  
Shuang Wang ◽  
Yun-zhou Yu ◽  
Wei-shi Du ◽  
Fang Yang ◽  
...  
Keyword(s):  
Phage Display ◽  
Neutralizing Antibodies ◽  
Botulinum Neurotoxin ◽  
Phage Display Library ◽  
Human Antibody ◽  
Serotype A ◽  
Antibody Phage ◽  
Antibody Phage Display ◽  
Botulinum Neurotoxin Serotype A

The botulinum neurotoxins (BoNTs) produced by Clostridium botulinum are the most poisonous protein substances known. The neutralizing antibodies against botulinum neurotoxin can effectively prevent and cure the toxicosis. Using purified Hc fragments of botulinum neurotoxin serotype A (BoNT/A-Hc) as antigen, 2 specific neutralizing antibodies mapping different epitopes were selected from a fully synthetic human antibody library. The 2 antibodies can effectively inhibit the binding between BoNT/A-Hc and differentiated PC-12 cells in vitro, and the neutralization was evaluated in vivo. Although no single mAb completely protected mice from toxin, they both could prolong time to death when challenged with 20 LD 50s (50% lethal doses) of BoNT/A. When used together, the mAbs completely neutralized 1000 LD50s/mg Ab, suggesting their high neutralizing potency in vivo . The results would lead to further production of neutralizing antibody drugs against BoNT/A. It also proved that it was a quick method to obtain human therapeutic antibodies by selecting from the fully synthetic human antibody phage display library. ( Journal of Biomolecular Screening 2009:991-998)

Sign in / Sign up

Export Citation Format

Share Document