Increased antiviral and opsonic activity of a highly multimerized collectin chimera.
Increased antiviral and opsonic activity of a highly multimerized collectin chimera.
复制标题
高度多聚化的集合素嵌合体的抗病毒和调理活性增加。
DOI：
10.1006/bbrc.2001.5373
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发表时间：
2001
期刊：
影响因子：
--
通讯作者：
Hartshorn,KL
中科院分区：
文献类型：
--
作者：
White,MR;Crouch,E;Chang,D;Hartshorn,KL
Altering the carbohydrate binding properties of surfactant protein D (SP-D) [e.g., by replacing its carbohydrate recognition domain (CRD) with that of either mannose binding lectin (MBL) or conglutinin] can increase its activity against influenza A virus (IAV). The current study demonstrates that the degree of multimerization of SP-D is another independent determinant of antiviral activity. A chimeric collectin containing the N-terminus and collagen domain of human SP-D and the CRD of MBL formed high-molecular-weight multimers similar to those previously described for human SP-D. Using several complementary assays, and diverse viral strains, the chimeric multimers showed greater anti-IAV activity than similarly multimerized preparations of SP-D or incompletely oligomerized preparations of the chimera. More highly multimerized preparations of the chimera also caused greater increases in uptake of IAV by neutrophils. These studies may have implications for development of collectins as therapeutic agents and understanding of natural variations in susceptibility to IAV infection.
