The macrophage galactose-type lectin can function as an attachment and entry receptor for influenza virus.
The macrophage galactose-type lectin can function as an attachment and entry receptor for influenza virus.
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巨噬细胞半乳糖型凝集素可以作为流感病毒的附着和进入受体。
DOI：
10.1128/jvi.02014-13
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
Reading PC.
中科院分区：
文献类型：
--
作者：
Ng WC;Liong S;Tate MD;Irimura T;Denda-Nagai K;Brooks AG;Londrigan SL;Reading PC.
介导甲型流感病毒（IAV）内化和进入的特异性蛋白受体尚未在任何细胞类型中被确定。唾液酸（SIA）是IAV血凝素的主要附着因子，由许多细胞表面糖蛋白和糖脂表达，混淆了识别参与病毒感染的特定受体的努力。中国仓鼠卵巢（CHO）上皮细胞Lec1表达细胞表面SIA并结合IAV，但具有较强的抗感染能力。在这里，我们证明了小鼠巨噬细胞半乳糖型凝集素1 （MGL1）在Lec1细胞中的表达增强了Ca2+依赖性IAV的结合，并恢复了对感染的容忍度。在细胞表面SIA存在或不存在的情况下，表达MGL1的Lec1细胞都被感染，这表明MGL1可以作为主要受体或作为SIA的辅助受体。表达内吞缺陷MGL1的Lec1细胞介导Ca2+依赖性IAV结合，但对IAV感染不太敏感，表明通过MGL1直接内化可导致细胞感染。总之，这些研究确定MGL1是一种细胞表面糖蛋白，可以作为IAV附着和感染进入的真实受体。
Specific protein receptors that mediate internalization and entry of influenza A virus (IAV) have not been identified for any cell type. Sialic acid (SIA), the primary attachment factor for IAV hemagglutinin, is expressed by numerous cell surface glycoproteins and glycolipids, confounding efforts to identify specific receptors involved in virus infection. Lec1 Chinese hamster ovary (CHO) epithelial cells express cell surface SIA and bind IAV yet are largely resistant to infection. Here, we demonstrate that expression of the murine macrophage galactose-type lectin 1 (MGL1) by Lec1 cells enhanced Ca2+-dependent IAV binding and restored permissivity to infection. Lec1 cells expressing MGL1 were infected in the presence or absence of cell surface SIA, indicating that MGL1 can act as a primary receptor or as a coreceptor with SIA. Lec1 cells expressing endocytosis-deficient MGL1 mediated Ca2+-dependent IAV binding but were less sensitive to IAV infection, indicating that direct internalization via MGL1 can result in cellular infection. Together, these studies identify MGL1 as a cell surface glycoprotein that can act as an authentic receptor for both attachment and infectious entry of IAV.