人甘露糖结合蛋白作为一种调理素发挥作用。
The human mannose-binding protein functions as an opsonin.
作者信息
Kuhlman M, Joiner K, Ezekowitz R A
机构信息
Harvard Department of Pediatrics, Children's Hospital, Boston, Massachusetts 02115.
出版信息
J Exp Med. 1989 May 1;169(5):1733-45. doi: 10.1084/jem.169.5.1733.
Abstract
The human mannose-binding protein (MBP) is a multimeric serum protein that is divided into three domains: a cysteine-rich NH2-terminal domain that stabilizes the alpha-helix of the second collagen-like domain, and a third COOH-terminal carbohydrate binding region. The function of MBP is unknown, although a role in host defense is suggested by its ability to bind yeast mannans. In this report we show that native and recombinant human MBP can serve in an opsonic role in serum and thereby enhance clearance of mannose rich pathogens by phagocytes. MBP binds to wild-type virulent Salmonella montevideo that express a mannose-rich O-polysaccharide. Interaction of MBP with these organisms results in attachment, uptake, and killing of the opsonized bacteria by phagocytes. These results demonstrate that MBP plays a role in first line host defense against certain pathogenic organisms.
摘要
人甘露糖结合蛋白（MBP）是一种多聚体血清蛋白，可分为三个结构域：富含半胱氨酸的NH2末端结构域，其可稳定第二个胶原样结构域的α螺旋；以及第三个COOH末端碳水化合物结合区域。尽管MBP结合酵母甘露聚糖的能力提示其在宿主防御中发挥作用，但其功能尚不清楚。在本报告中，我们表明天然和重组人MBP在血清中可发挥调理作用，从而增强吞噬细胞对富含甘露糖病原体的清除。MBP可结合表达富含甘露糖O-多糖的野生型有毒力的蒙得维的亚沙门氏菌。MBP与这些微生物的相互作用导致吞噬细胞对调理后的细菌进行附着、摄取和杀伤。这些结果表明MBP在宿主针对某些致病生物的一线防御中发挥作用。
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