COMPLEMENT-DEPENDENT NEUTRALIZATION OF INFLUENZA-VIRUS BY A SERUM MANNOSE-BINDING LECTIN
COMPLEMENT-DEPENDENT NEUTRALIZATION OF INFLUENZA-VIRUS BY A SERUM MANNOSE-BINDING LECTIN
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DOI：
10.1099/0022-1317-75-3-615
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发表时间：
1994-03-01
影响因子：
3.8
通讯作者：
EZEKOWITZ, RAB
中科院分区：
文献类型：
--
作者：
ANDERS, EM;HARTLEY, CA;EZEKOWITZ, RAB
本文对豚鼠血清中P抑制剂的性质及其中和流感病毒的机制进行了研究。该抑制剂被证明是一种与人血清甘露糖结合蛋白有血清学相关性的甘露糖结合凝集素。ELISA法检测豚鼠凝集素与流感病毒或甘露糖结合蛋白的Ca2+依赖性结合。该单克隆抗体对豚鼠凝集素的血凝抑制和病毒中和活性均有抑制作用。凝集素对A型和b型流感病毒都有活性。在血凝抑制中，它独立于补体起作用，显然是通过凝集素与该位点附近的碳水化合物侧链结合，在空间上阻碍进入病毒血凝素的受体结合位点。然而，凝集素的中和作用需要激活经典的补体途径。据我们所知，血清凝集素加补体对流感病毒的中和作用代表了一种以前未被认识到的补体依赖性病毒失活机制，这可能在一线宿主防御各种包膜病毒中很重要。
The nature of the P inhibitor in guinea-pig serum and its mechanism of neutralization of influenza virus have been investigated. This inhibitor was shown to be a mannose-binding lectin serologically related to human serum mannose-binding protein. Ca2+-dependent binding of the guinea-pig lectin to influenza virus or to mannan could be detected with polyclonal or monoclonal antibodies against human mannose-binding protein in an ELISA. Furthermore, the monoclonal antibody inhibited both the haemagglutination-inhibiting and virus-neutralizing activities of the guinea-pig lectin. The lectin was active against influenza viruses of both type A and type B. In haemagglutination inhibition it acts independently of complement, apparently by sterically hindering access to the receptor-binding site on the viral haemagglutinin through binding of the lectin to carbohydrate side-chains in the vicinity of this site. Neutralization by the lectin, however, was shown to require activation of the classical complement pathway. To our knowledge, the neutralization of influenza virus by a serum lectin plus complement represents a previously unrecognized mechanism of complement-dependent viral inactivation that may be important in first-line host defence against a variety of enveloped viruses.