Shi Ping, Lu Zenghui, He Yuanchuan, Chen Shijiang, Yan Jun, Li Junhong, Zhang Xiaobing
Institute of Chinese Caterpillar Fungus, Chongqing Academy of Chinese Materia Medica, Nanshan Road, Nan'an District, Chongqing, China.
Chongqing Taiji Industry (Group) Co., Ltd, Chongqing, China.
Int J Med Mushrooms. 2015;17(11):1087-93. doi: 10.1615/intjmedmushrooms.v17.i11.90.
In the Chinese caterpillar mushroom Ophiocordyceps sinensis, a subtislin-like serine protease (Pr1) is one of the most important enzymes for its infection activity against insect cuticles. The Pr1 gene was isolated from the valuable Chinese medicinal fungus O. sinensis using rapid amplification of 5' and 3' complementary DNA ends. The 2079-bp full-length complementary DNA sequence containing the 1605-bp predicted open reading frame of the Pr1 gene was obtained (GenBank accession no. KF836756). The open reading frame encodes a protein comprising 534 amino acids. Protein sequence multiple alignment analysis revealed high homology with 16 other subtilisin serine proteases and exhibited the highly conserved catalytic domain (D195, H227, and S393). We also constructed a phylogenetic tree in this study. Further molecular studies are needed to elucidate the mechanisms of fungal infection.
在冬虫夏草菌(中华被毛孢)中,一种类枯草杆菌蛋白酶的丝氨酸蛋白酶(Pr1)是其针对昆虫表皮感染活性的最重要酶之一。利用5'和3'互补DNA末端的快速扩增技术,从珍贵的中药材真菌中华被毛孢中分离出Pr1基因。获得了包含Pr1基因1605bp预测开放阅读框的2079bp全长互补DNA序列(GenBank登录号:KF836756)。该开放阅读框编码一个由534个氨基酸组成的蛋白质。蛋白质序列多重比对分析显示与其他16种枯草杆菌蛋白酶丝氨酸蛋白酶具有高度同源性,并呈现出高度保守的催化结构域(D195、H227和S393)。在本研究中我们还构建了系统发育树。需要进一步的分子研究来阐明真菌感染的机制。