Condra J H, Sardana V V, Tomassini J E, Schlabach A J, Davies M E, Lineberger D W, Graham D J, Gotlib L, Colonno R J
Department of Virus and Cell Biology, Merck Sharp and Dohme Research Laboratories, West Point, Pennsylvania 19486.
J Biol Chem. 1990 Feb 5;265(4):2292-5.
Human rhinoviruses are the major causative agents of the common cold in humans and have been divided into major and minor groups based on receptor specificity. cDNAs encoding the light and heavy chains of a murine monoclonal antibody that recognizes the major group receptor were cloned, abundantly expressed in Escherichia coli, and renatured into Fab fragments that blocked virus binding and protected HeLa cell monolayers from rhinovirus infection. Elimination of the cysteines normally bridging the heavy and light chains yielded molecules indistinguishable from wild-type Fab fragments in virus binding assays. Single-chain antibodies with covalently linked light and heavy variable domains were also expressed and showed receptor binding and cell protection activities. These recombinant antibody fragments are potentially useful in preventing or treating common colds in humans.
人鼻病毒是人类普通感冒的主要病原体，根据受体特异性可分为主要组和次要组。编码识别主要组受体的鼠单克隆抗体轻链和重链的cDNA被克隆，在大肠杆菌中大量表达，并复性成能阻断病毒结合并保护HeLa细胞单层免受鼻病毒感染的Fab片段。去除通常连接重链和轻链的半胱氨酸后，在病毒结合试验中产生的分子与野生型Fab片段无法区分。具有共价连接的轻链和重链可变结构域的单链抗体也被表达，并显示出受体结合和细胞保护活性。这些重组抗体片段在预防或治疗人类普通感冒方面可能具有潜在用途。
