一种特异性分泌的人磷脂酶A2对1型人类免疫缺陷病毒的裂解作用。
Lysis of human immunodeficiency virus type 1 by a specific secreted human phospholipase A2.
作者信息
Kim Jae-Ouk, Chakrabarti Bimal K, Guha-Niyogi Anuradha, Louder Mark K, Mascola John R, Ganesh Lakshmanan, Nabel Gary J
机构信息
Vaccine Research Center, NIAID, National Institutes of Health, Room 4502, Bldg. 40, MSC-3005, 40 Convent Dr., Bethesda, MD 20892-3005, USA.
出版信息
J Virol. 2007 Feb;81(3):1444-50. doi: 10.1128/JVI.01790-06. Epub 2006 Nov 8.
Abstract
Phospholipase A2 (PLA2) proteins affect cellular activation, signal transduction, and possibly innate immunity. A specific secretory PLA2, sPLA2-X, is shown here to neutralize human immunodeficiency virus type 1 (HIV-1) through degradation of the viral membrane. Catalytic function was required for antiviral activity, and the target cells of infection were unaffected. sPLA2-X potently reduced gene transfer of HIV-1 Env-pseudotyped lentivirus vectors and inhibited the replication of both CCR5- and CXCR4-tropic HIV-1 in human CD4+ T cells. Virions resistant to damage by antibody and complement were sensitive to lysis by sPLA2-X, suggesting a novel mechanism of antiviral surveillance independent of the acquired immune system.
摘要
磷脂酶A2（PLA2）蛋白影响细胞活化、信号转导，可能还影响固有免疫。本文显示一种特定的分泌型PLA2，即sPLA2-X，可通过降解病毒膜来中和1型人类免疫缺陷病毒（HIV-1）。抗病毒活性需要催化功能，且感染的靶细胞不受影响。sPLA2-X能有效降低HIV-1包膜假型慢病毒载体的基因转移，并抑制CCR5嗜性和CXCR4嗜性HIV-1在人CD4+T细胞中的复制。对抗体和补体损伤具有抗性的病毒粒子对sPLA2-X介导的裂解敏感，提示存在一种独立于获得性免疫系统的新型抗病毒监测机制。
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