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Functional surface proteomic profiling reveals the host heat-shock protein A8 as a mediator of Lichtheimia corymbifera recognition by murine alveolar macrophages.
Environmental Microbiology ( IF 5.1 ) Pub Date : 2020-06-24 , DOI: 10.1111/1462-2920.15140
Mohamed I Abdelwahab Hassan 1, 2, 3 , Janis M Kruse 4 , Thomas Krüger 4 , Hans-Martin Dahse 5 , Zoltán Cseresnyés 6 , Matthew G Blango 4 , Hortense Slevogt 7 , Franziska Hörhold 8 , Volker Ast 8 , Rainer König 8 , Marc Thilo Figge 2, 6 , Olaf Kniemeyer 4 , Axel A Brakhage 2, 4 , Kerstin Voigt 1, 2
Affiliation  

Mucormycosis is an emergent, fatal fungal infection of humans and warm‐blooded animals caused by species of the order Mucorales. Immune cells of the innate immune system serve as the first line of defence against inhaled spores. Alveolar macrophages were challenged with the mucoralean fungus Lichtheimia corymbifera and subjected to biotinylation and streptavidin enrichment procedures followed by LC–MS/MS analyses. A total of 28 host proteins enriched for binding to macrophage–L. corymbifera interaction. Among those, the HSP70‐family protein Hspa8 was found to be predominantly responsive to living and heat‐killed spores of a virulent and an attenuated strain of L. corymbifera. Confocal scanning laser microscopy of infected macrophages revealed colocalization of Hspa8 with phagocytosed spores of L. corymbifera. The amount of detectable Hspa8 was dependent on the multiplicity of infection. Incubation of alveolar macrophages with an anti‐Hspa8 antibody prior to infection reduced their capability to phagocytose spores of L. corymbifera. In contrast, anti‐Hspa8 antibodies did not abrogate the phagocytosis of Aspergillus fumigatus conidia by macrophages. These results suggest an important contribution of the heat‐shock family protein Hspa8 in the recognition of spores of the mucoralean fungus L. corymbifera by host alveolar macrophages and define a potential immunomodulatory therapeutic target.

中文翻译:

功能性表面蛋白质组学分析揭示了宿主热休克蛋白A8是鼠肺泡巨噬细胞识别钴酸锂的媒介。

毛霉菌病是由毛霉菌属引起的人类和温血动物的一种紧急致命真菌感染。先天免疫系统的免疫细胞是抵抗吸入孢子的第一道防线。肺泡巨噬细胞受到黏膜粘菌Lichtheimia corymbifera的攻击,并经过生物素化和链霉亲和素富集程序,然后进行LC-MS / MS分析。总共富集了28种与巨噬细胞L结合的宿主蛋白。伞形科互动。其中,HSP70家族蛋白Hspa8主要对强毒和减毒的L菌株活和热杀死的孢子有反应。鳞翅目。共聚焦扫描激光显微镜观察感染的巨噬细胞显示Hspa8与L的吞噬孢子共定位。伞形科。可检测的Hspa8的量取决于感染的多样性。在感染前将肺泡巨噬细胞与抗Hspa8抗体一起孵育会降低其吞噬L孢子的能力。伞形科。相比之下,抗Hspa8抗体不会消除巨噬细胞对烟曲霉分生孢子的吞噬作用。这些结果表明,热休克家族蛋白Hspa8在识别粘多糖真菌L的孢子中具有重要作用。伞形科 通过宿主肺泡巨噬细胞来确定潜在的免疫调节治疗靶点。
更新日期:2020-06-24
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