IMMUNE-RESPONSE TO HUMAN INFLUENZA-VIRUS HEMAGGLUTININ EXPRESSED IN ESCHERICHIA-COLI
IMMUNE-RESPONSE TO HUMAN INFLUENZA-VIRUS HEMAGGLUTININ EXPRESSED IN ESCHERICHIA-COLI
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DOI：
10.1016/0378-1119(83)90011-2
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发表时间：
1983-01-01
期刊：
影响因子：
3.5
通讯作者：
COMPANS, RW
中科院分区：
文献类型：
--
作者：
DAVIS, AR;BOS, T;COMPANS, RW
Cloned DNA fragments coding for parts of strain WSN (H1N1) influenza virus hemagglutinin (HA) were fused to a bacterial leader DNA derived from the Escherichia coli trp operon. Fusion proteins produced consisted of 190 amino acids of trpLE'' protein at the amino terminus, and HA amino acids, either 1-308, 1-396 or 1-548 (complete HA), at the carboxyl terminus. These proteins were expressed at high levels (10-20% of total protein) in E. coli starved for typtophan. A CNBr fragment (HA1-211) was derived from HA-308. Each of the proteins was purified and used for immunizing mice and rabbits. The antibody produced was shown to bind to the HA fusion proteins, detergent-treated viral HA, HA on intact virions, and the HA on the surface of cells infected with influenza virus. Evidently, the HA fusion proteins expressed in bacteria can elicit antibodies that recognize at least some determinants of the native viral HA, and probably could lead to development of an anti-influenza vaccine.
