INTRACELLULAR NEUTRALIZATION OF VIRUS BY IMMUNOGLOBULIN-A ANTIBODIES
INTRACELLULAR NEUTRALIZATION OF VIRUS BY IMMUNOGLOBULIN-A ANTIBODIES
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DOI：
10.1073/pnas.89.15.6901
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发表时间：
1992-08-01
影响因子：
11.1
通讯作者：
NEDRUD, JG
中科院分区：
文献类型：
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作者：
MAZANEC, MB;KAETZEL, CS;NEDRUD, JG
IgA被认为可通过阻止病毒附着从而在黏膜上皮表面中和病毒。由于IgA是一种多聚免疫球蛋白，它通过多聚免疫球蛋白受体穿过上皮细胞的内层进行转运，并且由于病毒是专性细胞内寄生物，我们假设IgA抗体也可能通过与受感染细胞内新合成的病毒蛋白结合来干扰病毒复制。表达多聚免疫球蛋白受体的马丁 - 达比犬肾上皮细胞的极化单层在顶端表面被仙台病毒感染。从基底外侧表面递送的抗仙台病毒IgA单克隆抗体与细胞内的病毒蛋白共定位，这通过免疫荧光得以证实。更重要的是，抗病毒IgA使病毒滴度降低>1000倍（P<0.001），而IgG单克隆抗体仅使病毒滴度降低约10倍（P<0.05）。这些结果表明，IgA抗体可以在细胞内发挥作用来抑制病毒复制。
IgA is thought to neutralize viruses at the epithelial surface of mucous membranes by preventing their attachment. Since IgA, a polymeric immunoglobulin, is transported through the lining of epithelial cells by the polymeric-immunoglobulin receptor and since viruses are obligate intracellular parasites, we hypothesized that IgA antibodies may also interfere with viral replication by binding to newly synthesized viral proteins within infected cells. Polarized monolayers of Madin-Darby canine kidney epithelial cells expressing the polymeric-immunoglobulin receptor were infected on the apical surface with Sendai virus. Anti-Sendai virus IgA monoclonal antibody delivered from the basolateral surface colocalized with viral protein within the cell, as documented by immunofluorescence. More importantly, anti-viral IgA reduced virus titers >1000-fold (P10-fold (P