Title |
A single-domain antibody-linked Fab bispecific antibody Her2-S-Fab has potent cytotoxicity against Her2-expressing tumor cells
|
---|---|
Published in |
AMB Express, April 2016
|
DOI | 10.1186/s13568-016-0201-4 |
Pubmed ID | |
Authors |
Aifen Li, Jieyu Xing, Li Li, Changhua Zhou, Bin Dong, Ping He, Qing Li, Zhong Wang |
Abstract |
Her2, which is frequently overexpressed in breast cancer, is one of the most studied tumor-associated antigens for cancer therapy. Anti-HER2 monoclonal antibody, trastuzumab, has achieved significant clinical benefits in metastatic breast cancer. In this study, we describe a novel bispecific antibody Her2-S-Fab targeting Her2 by linking a single domain anti-CD16 VHH to the trastuzumab Fab. The Her2-S-Fab antibody can be efficiently expressed and purified from Escherichia coli, and drive potent cancer cell killing in HER2-overexpressing cancer cells. In xenograft model, the Her2-S-Fab suppresses tumor growth in the presence of human immune cells. Our results suggest that the bispecific Her2-S-Fab may provide a valid alternative to Her2 positive cancer therapy. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 2 | 100% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Members of the public | 2 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Denmark | 1 | 2% |
Unknown | 44 | 98% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Researcher | 11 | 24% |
Student > Ph. D. Student | 9 | 20% |
Student > Bachelor | 7 | 16% |
Student > Master | 4 | 9% |
Other | 2 | 4% |
Other | 5 | 11% |
Unknown | 7 | 16% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 12 | 27% |
Agricultural and Biological Sciences | 8 | 18% |
Pharmacology, Toxicology and Pharmaceutical Science | 4 | 9% |
Medicine and Dentistry | 3 | 7% |
Engineering | 3 | 7% |
Other | 8 | 18% |
Unknown | 7 | 16% |