The NADPH oxidase AoNoxA in Arthrobotrys oligospora functions as an initial factor in the infection of Caenorhabditis elegans

• Published in: The journal of microbiology Vol. 55; no. 11; pp. 885 - 891
• Main Authors: Li, Xin, Kang, Ying-Qian, Luo, Yan-Lu, Zhang, Ke-Qin, Zou, Cheng-Gang, Liang, Lian-Ming
• Format: Journal Article
• Language: English
• Published: Seoul The Microbiological Society of Korea 01.11.2017; Springer Nature B.V; 한국미생물학회
• Subjects: Arthrobotrys oligospora; Biomedical and Life Sciences; Caenorhabditis elegans; Germination; Life Sciences; Microbial Pathogenesis and Host-Microbe Interaction; Microbiology; NAD(P)H oxidase; Nematodes; Nematophagous fungi; Oxidase; Reactive oxygen species; Serine; Serine proteinase; Signaling; Virulence; Virulence factors; 생물학; trap formation; nematode-trapping fungi; NADPH oxidase; reactive oxygen species
• ISSN: 1225-8873; 1976-3794
• DOI: 10.1007/s12275-017-7169-x

Reactive oxygen species (ROS) produced by NADPH oxidases can serve as signaling molecules to regulate a variety of physiological processes in multi-cellular organisms. In the nematophagous fungus Arthrobotrys oligospora , we found that ROS were produced during conidial germination, hyphal extension, and trap formation in the presence of nematodes. Generation of an AoNoxA knockout strain demonstrated the crucial role of NADPH oxidase in the production of ROS in A. oligospora , with trap formation impaired in the AoNoxA mutant, even in the presence of the nematode host. In addition, the expression of virulence factor serine protease P186 was up-regulated in the wild-type strain, but not in the mutant strain, in the presence of Caenorhabditis elegans . These results indicate that ROS derived from AoNoxA are essential for full virulence of A. oligospora in nematodes.