Enhanced anti-influenza activity of a surfactant protein D and serum conglutinin fusion protein
Enhanced anti-influenza activity of a surfactant protein D and serum conglutinin fusion protein
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DOI：
10.1152/ajplung.2000.278.1.l90
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发表时间：
2000-01-01
影响因子：
4.9
通讯作者：
Crouch, EC
中科院分区：
文献类型：
--
作者：
Hartshorn, KL;Sastry, KN;Crouch, EC
表面活性蛋白D和血清结合蛋白融合蛋白的增强的抗流感活性。Am.肺细胞生理学杂志梅尔. h生理学278：L90-L98，2000年。我们以前证明，牛血清凝聚素有显着更大的能力，抑制甲型流感病毒（IAV）的感染性比其他collectins。我们现在证明，重组的conglomerin和一个嵌合蛋白，该嵌合蛋白含有大鼠肺表面活性蛋白D（rSP-D）的NH 2末端和胶原结构域，融合到conglomerin的颈部区域和碳水化合物识别结构域（CRD）。（称为SP-D/Cong（neck+CRD））比野生型重组rSP-D具有明显更强的抑制IAV感染性的能力，证实了伴发蛋白的有效的IAV中和活性存在于其颈部、区域和CRD中。此外，由于SP-D的NH 2末端和胶原结构域的掺入，SP-D/Cong（颈+CRD）比重组Cong蛋白或重组rSP-D引起显著更大的IAV颗粒聚集和IAV的嗜中性粒细胞结合和H2 O2应答的增强。因此，SP-D/Cong（neck+CRD）结合了Cong蛋白和SP-D的有利的抗病毒和调理性质。这项研究表明，SP-D和连接蛋白的特定结构域与特定的功能特性的关联，并说明野生型胶原凝集素的抗微生物活性可以通过重组策略增强。
Enhanced anti-influenza activity of a surfactant protein D and serum conglutinin fusion protein. Am. J. Physiol. Lung Cell. Mel. Physiol. 278: L90-L98, 2000.--We previously demonstrated that bovine serum conglutinin has markedly greater ability to inhibit influenza A virus (IAV) infectivity than other collectins. We now show that recombinant conglutinin and a chimeric protein containing the NH2 terminus and collagen domain of rat pulmonary surfactant protein D (rSP-D) fused to the neck region and carbohydrate recognition domain (CRD) of conglutinin (termed SP-D/Cong(neck+CRD)) have markedly greater ability to inhibit infectivity of IAV than wild-type recombinant rSP-D, confirming that the potent IAV-neutralizing activity of conglutinin resides in its neck, region and CRD. Furthermore, by virtue of incorporation of the NH2 terminus and collagen domain of SP-D, SP-D/Cong(neck+CRD) caused substantially greater aggregation of IAV particles and enhancement of neutrophil binding of, and H2O2 responses to, IAV than recombinant conglutinin or recombinant rSP-D. Hence, SP-D/Cong(neck+CRD) combined favorable antiviral and opsonic properties of conglutinin and SP-D. This study demonstrates an association of specific structural domains of SP-D and conglutinin with specific functional properties and illustrates that antimicrobial activities of wild-type collectins can be enhanced through recombinant strategies.