Centro de Biotecnologia da Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil.
FEMS Microbiol Lett. 2010 Nov;312(2):101-9. doi: 10.1111/j.1574-6968.2010.02103.x. Epub 2010 Oct 7.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a classic glycolytic enzyme that plays important roles in various cellular processes. Here, we report the sequence and transcriptional analyses of a regulated gene (gpdh1) encoding GAPDH in the entomopathogenic fungus Metarhizium anisopliae, a well-characterized biocontrol agent of a wide range of arthropod pests. Transcript and protein analyses of the gpdh1 showed a carbohydrate-dependent expression pattern in response to different carbon sources. A demonstration that GAPDH is localized at the cell surface is presented, and assays with insect wings show that this protein has adhesion-like activity. These results imply that GAPDH adhesion to the wing surface is specific and may play a role in the binding of conidia to a host. Our observations indicate new roles for GAPDH both physiologically and during the entomopathogen-host interaction.
甘油醛-3-磷酸脱氢酶（GAPDH）是一种经典的糖酵解酶，在各种细胞过程中发挥重要作用。在这里，我们报告了在昆虫病原真菌金龟子绿僵菌中一种受调控的基因（gpdh1）的序列和转录分析，该基因编码 GAPDH，金龟子绿僵菌是一种广泛的节肢动物害虫的生物防治剂。gpdh1 的转录和蛋白分析显示出对不同碳源的碳水化合物依赖性表达模式。本文提出了 GAPDH 定位于细胞表面的观点，并通过昆虫翅膀进行了实验，表明该蛋白具有粘附样活性。这些结果表明 GAPDH 对翅膀表面的粘附是特异性的，可能在孢子与宿主结合中发挥作用。我们的观察结果表明 GAPDH 在生理和昆虫病原-宿主相互作用中具有新的作用。
