Reading P C, Hartley C A, Ezekowitz R A, Anders E M
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
Biochem Biophys Res Commun. 1995 Dec 26;217(3):1128-36. doi: 10.1006/bbrc.1995.2886.
The mechanism of lysis of influenza virus-infected BHK-21 cells by guinea pig serum (GPS) was investigated. Lysis was shown to involve activation of the classical complement pathway and was dependent on the presence of a mannose-binding lectin in GPS. FACS analysis demonstrated Ca(2+)-dependent binding of the lectin to influenza virus-infected, but not uninfected, cells. Cells infected with mutant strains of virus lacking a particular high-mannose oligosaccharide at the tip of the hemagglutinin molecule showed reduced binding of the lectin and were correspondingly less sensitive to lysis by GPS than cells infected with the parent viruses. The degree or pattern of glycosylation of influenza viruses thus influences susceptibility to this mechanism of viral clearance. By interfering with the infectious process, lectin-dependent complement-mediated lysis of infected cells may be an important component of innate immunity to influenza and other enveloped viruses.
研究了豚鼠血清（GPS）对感染流感病毒的BHK - 21细胞的裂解机制。结果表明，裂解过程涉及经典补体途径的激活，且依赖于GPS中甘露糖结合凝集素的存在。流式细胞术分析表明，该凝集素与感染流感病毒的细胞而非未感染细胞的结合依赖于Ca(2+)。感染了在血凝素分子顶端缺乏特定高甘露糖寡糖的病毒突变株的细胞，其凝集素结合减少，相应地，与感染亲本病毒的细胞相比，对GPS裂解的敏感性较低。因此，流感病毒的糖基化程度或模式会影响对这种病毒清除机制的敏感性。通过干扰感染过程，凝集素依赖性补体介导的感染细胞裂解可能是对流感和其他包膜病毒固有免疫的重要组成部分。
