Secreted poxvirus chemokine binding proteins
Secreted poxvirus chemokine binding proteins
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分泌型痘病毒趋化因子结合蛋白
DOI：
10.1002/jlb.62.5.570
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发表时间：
1997
影响因子：
5.5
通讯作者：
G. McFadden
中科院分区：
文献类型：
--
作者：
A. Lalani;G. McFadden
痘病毒编码多种免疫调节蛋白，破坏感染宿主的细胞因子网络。粘液瘤病毒是一种兔痘病毒病原体，表达两种不同的35 - 40-kDa分泌糖蛋白，可结合广谱趋化因子。其中第一个，命名为M-T7，由T7基因编码，是这里称为I型趋化因子结合蛋白（CBP-I）的第一个例子。M-T7最初被发现是细胞干扰素-γ受体的分泌型病毒同源物，但结合研究表明，纯化的M-T7蛋白也通过保守的肝素结合结构域与CXC、CC和C趋化因子家族的成员相互作用。第二种粘液瘤蛋白，M-T1，也称为CBP-II，是痘病毒蛋白质的一个更大的超家族的成员，包括由各种各样的正痘病毒编码的相关分泌的35-kDa蛋白质。重组痘病毒构建体中CBP-I或CBP-II基因的缺失分析显示，浸润性白细胞向病毒感染病变中的运输发生了显著变化。有人提出，CBP-I与大多数趋化因子上发现的保守肝素结合结构域的相互作用代表了改变体内多种趋化因子功能的新机制。总之，CBP-I和CBP-II是分泌的病毒蛋白的第一个例子，其结合多种趋化因子家族成员，作为预防炎症细胞迁移到病毒感染组织的早期阶段的策略的一部分。J.利瓦克62：570-576; 1997.
Poxviruses encode a variety of immunomodulatory proteins that subvert the cytokine networks of infected hosts. Myxoma virus, a poxvirus pathogen of rabbits, expresses two distinct 35‐ to 40‐kDa secreted glycoproteins that bind a broad spectrum of chemokines. The first of these, designated M‐T7, is encoded by the T7 gene and is the first example of what is here referred to as type‐I chemokine binding protein (CBP‐I). M‐T7 was initially discovered as a secreted viral homologue of cellular interferon‐γ receptor but binding studies indicate that purified M‐T7 protein also interacts with members of the CXC, CC, and C chemokine families through the conserved heparin‐binding domains. The second myxoma protein, M‐T1, also called CBP‐II, is a member of a larger superfamily of poxvirus proteins that includes related secreted 35‐kDa proteins encoded by a wide variety of orthopoxviruses. Deletion analysis of either CBP‐I or ‐II genes within recombinant poxvirus constructs revealed profound alterations in the trafficking of infiltrating leukocytes into virus‐infected lesions. It is proposed that the interaction of CBP‐I with the conserved heparin‐binding domains found on most chemokines represents a novel mechanism for altering multiple chemokine functions in vivo. In summary, CBP‐I and CBP‐II are the first examples of secreted virus proteins that bind to multiple chemokine family members as part of a strategy to prevent the early phase of inflammatory cell migration into virus‐infected tissues. J. Leukoc. Biol.62: 570–576; 1997.