[Preparation and identification of a single-chain antibody fragment against high pathogenic H5N1 avian influenza virus].
Previously, an mAb 10F7 was developed against H5N1 hemagglutinin, which was highly specific to 34 different H5N1 strains and showed good neutralizing activity. In the present study, the single-chain fragment of the antibody was cloned into a prokaryotic vector and then expressed in E. coli. The activity of the scFv was tested in hemagglution inhibition and neutralization experiment. Two H5N1 virus strains were inhibited to bind erythrocyte cells by the scFv while the H9 virus was not. Also, five H5N1 virus strains were neutralized during infecting MDCK cells. These results showed an approachable method for developing therapeutic antibody to H5N1 virus.
Fang
Zhong
Z
National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Key Laboratory of Education Minister for Cell Biology and Tumor Cell Engineering of Xiamen University, School of Life Sciences, Xiamen University, Xiamen 361005, China.
Luo
Wen-Xin
WX
Wang
Ming-Qiao
MQ
Chen
Ying-Wei
YW
Zhang
Jun
J
Chen
Hong-Lin
HL
Guan
Yi
Y
Xia
Ning-Shao
NS
D000595:Amino Acid Sequence; D000818:Animals; D000914:Antibodies, Viral / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D000918:Antibody Specificity / Q000276:immunology; D001717:Birds / Q000821:virology; D002460:Cell Line; D045744:Cell Line, Tumor; D004591:Electrophoresis, Polyacrylamide Gel; D053124:Influenza A Virus, H5N1 Subtype / Q000276:immunology*; D005585:Influenza in Birds / Q000821:virology; D009500:Neutralization Tests; D011994:Recombinant Proteins / Q000276:immunology / Q000378:metabolism; D057127:Single-Chain Antibodies / Q000235:genetics / Q000276:immunology* / Q000378:metabolism
D000914:Antibodies, Viral; D011994:Recombinant Proteins; D057127:Single-Chain Antibodies