Funk Jana, Schaarschmidt Barbara, Slesiona Silvia, Hallström Teresia, Horn Uwe, Brock Matthias
Bio Pilot Plant, Leibniz-Institute for Natural Product Research and Infection Biology-Hans-Knöll-Institute (HKI), Beutenbergstr. 11a, 07745, Jena, Germany.
Microbial Immunology, Leibniz-Institute for Natural Product Research and Infection Biology-Hans-Knöll-Institute (HKI), Beutenbergstr. 11a, 07745, Jena, Germany.
Int J Med Microbiol. 2016 Jan;306(1):59-68. doi: 10.1016/j.ijmm.2015.11.005. Epub 2015 Dec 3.
Allergies are an increasing issue in human health and can, eventually, cause severe anaphylactic shock. Aspergillus fumigatus and Candida albicans are leading causes of life-threatening invasive fungal infections in immunocompromised patients, but can also cause severe allergic responses in otherwise healthy individuals. The glycolytic enzyme enolase is known as a major allergen despite its function in intracellular metabolism. Therefore, its presentation on surfaces of different fungal species was investigated by using antibodies raised against recombinant enolases from A. fumigatus and C. albicans. Examination of antibody specificity revealed cross-reactivity to cell-free extracts from Aspergillus terreus, Aspergillus flavus, Aspergillus nidulans and Candida glabrata, but not against any of the three human enolases. Antibody specificity was further confirmed by hybridization with other recombinant fungal enolases, where the antibodies recognized different subsets of fungal enolases. When surface presentation of enolase was tested on intact fungal cells, a positive staining was obtained with those antibodies that also recognized the enzyme from the respective cell-free extract. This implies a general surface presentation of this glycolytic enzyme among fungal species and provides hints for its predominant recognition as an allergen. Additionally, A. fumigatus and C. albicans enolase bound to human plasminogen, which remained accessible for the plasminogen activator uPA. This implies a potential role of enolase in the invasion and dissemination process during fungal infections.
过敏在人类健康中是一个日益严重的问题，最终可能导致严重的过敏性休克。烟曲霉和白色念珠菌是免疫功能低下患者危及生命的侵袭性真菌感染的主要原因，但在其他健康个体中也可引起严重的过敏反应。糖酵解酶烯醇化酶尽管在细胞内代谢中发挥作用，但仍被认为是一种主要过敏原。因此，通过使用针对烟曲霉和白色念珠菌重组烯醇化酶产生的抗体，研究了其在不同真菌物种表面的呈现情况。抗体特异性检测显示，这些抗体与土曲霉、黄曲霉、构巢曲霉和光滑念珠菌的无细胞提取物存在交叉反应，但与三种人类烯醇化酶均无反应。通过与其他重组真菌烯醇化酶杂交进一步证实了抗体特异性，这些抗体识别不同的真菌烯醇化酶亚群。当在完整的真菌细胞上测试烯醇化酶的表面呈现时，那些能识别相应无细胞提取物中该酶的抗体获得了阳性染色。这意味着这种糖酵解酶在真菌物种中普遍存在表面呈现，并为其作为主要过敏原的识别提供了线索。此外，烟曲霉和白色念珠菌烯醇化酶与人类纤溶酶原结合，纤溶酶原激活剂uPA仍可作用于该结合物。这意味着烯醇化酶在真菌感染的侵袭和传播过程中可能发挥作用。
