Thielens Nicole M, Tacnet-Delorme Pascale, Arlaud Gérard J
Laboratoire d'Enzymologie Moléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France.
Immunobiology. 2002 Sep;205(4-5):563-74. doi: 10.1078/0171-2985-00155.
As soluble recognition molecules of innate immunity, C1q and MBL are able to bind directly to various viruses, including retroviruses and influenza viruses. Interaction of C1q with retroviruses and certain infected cells was shown to involve the globular region of C1q and viral envelope glycoproteins, such as p15E of MuLV, gp41 and gp120 of HIV-1, gp21 of HTLV-1. C1q binding was found to trigger antibody-independent activation of the classical pathway of complement, but did not lead to virus destruction and had even an adverse effect on infection in humans, because of subversion of the complement system by the virus. Binding of MBL or of the pulmonary collectin SP-D to influenza A virus was shown to involve the carbohydrate recognition domain of the molecule and high-mannose oligosaccharides of the viral proteins haemagglutinin and neuraminidase. These interactions lead to virus inactivation, are independent of complement activation and are influenced by the oligomerization state of the collectin.
作为天然免疫的可溶性识别分子，C1q和甘露聚糖结合凝集素（MBL）能够直接结合多种病毒，包括逆转录病毒和流感病毒。已表明C1q与逆转录病毒及某些受感染细胞的相互作用涉及C1q的球状区域和病毒包膜糖蛋白，如莫洛尼氏鼠白血病病毒（MuLV）的p15E、人类免疫缺陷病毒1型（HIV-1）的gp41和gp120、人类嗜T淋巴细胞病毒1型（HTLV-1）的gp21。发现C1q结合可触发补体经典途径的抗体非依赖性激活，但不会导致病毒破坏，甚至对人类感染有不利影响，因为病毒会破坏补体系统。已表明MBL或肺凝集素表面活性蛋白-D（SP-D）与甲型流感病毒的结合涉及该分子的碳水化合物识别结构域以及病毒蛋白血凝素和神经氨酸酶的高甘露糖寡糖。这些相互作用导致病毒失活，独立于补体激活，并受凝集素寡聚化状态的影响。
