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用截短的黏附素卡他莫拉菌免疫球蛋白D结合蛋白(MID764 - 913)进行免疫接种,在肺部清除的小鼠模型中对卡他莫拉菌具有保护作用。

Immunization with the truncated adhesin moraxella catarrhalis immunoglobulin D-binding protein (MID764-913) is protective against M. catarrhalis in a mouse model of pulmonary clearance.

作者信息

Forsgren Arne, Brant Marta, Riesbeck Kristian

机构信息

Department of Medical Microbiology, Malmo University Hospital, Lund University, Malmo, Sweden.

出版信息

J Infect Dis. 2004 Jul 15;190(2):352-5. doi: 10.1086/422155. Epub 2004 Jun 9.

Abstract

Most Moraxella catarrhalis isolates express the outer membrane protein MID. In addition to its specific affinity for immunoglobulin D, MID functions as an adhesin and binds to human epithelium. The adhesive part is localized within MID(764-913). Two mid-deficient M. catarrhalis isolates were constructed and examined in a mouse model of pulmonary clearance. M. catarrhalis devoid of MID was cleared more efficiently, compared with the wild-type counterparts. Furthermore, mice immunized with MID(764-913) cleared M. catarrhalis much more efficiently, compared with mice immunized with bovine serum albumin. MID(764-913) is suggested as a promising candidate in a future M. catarrhalis vaccine.

摘要

大多数卡他莫拉菌分离株表达外膜蛋白MID。除了对免疫球蛋白D具有特异性亲和力外,MID还作为一种粘附素发挥作用,并与人上皮细胞结合。粘附部分定位于MID(764 - 913)内。构建了两个缺失mid的卡他莫拉菌分离株,并在肺部清除的小鼠模型中进行了检测。与野生型菌株相比,缺失MID的卡他莫拉菌被清除得更有效。此外,与用牛血清白蛋白免疫的小鼠相比,用MID(764 - 913)免疫的小鼠清除卡他莫拉菌的效率要高得多。MID(764 - 913)被认为是未来卡他莫拉菌疫苗的一个有前景的候选物。

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