Identification of hydrophobin genes and their physiological functions related to growth and development in Pleurotus ostreatus.

Hydrophobins are small secreted proteins with important physiological functions and potential applications. Here, Pleurotus ostreatus hydrophobin genes were systematically analyzed: they were characterized, classified, and their expression profiles and gene functions were explored. In total, 40 P. ostreatus hydrophobin genes were found and showed genetic diversity, of which 15 were newly identified. The hydrophobin protein sequences were diverse but all contained eight cysteine residues with a conserved spacing pattern, and 33 of them were class I hydrophobins. The expression profile analyses showed that Vmh3 and Hydph20 were abundant in monokaryotic and dikaryotic mycelia, whereas Hydph17, Po.hyd16, Hydph8 were specifically expressed in monokaryotic mycelia and Po.hyd10 were specific in dikaryotic mycelia. Furthermore, Vmh3, Hydph20, Po.hyd7, and Po.hyd10 were abundant when dikaryotic mycelia cultivated on PDA, which are different from on substrate (Vmh2, Vmh3, Hydph7, Po.hyd3, Po.hyd7, Po.hyd9); Hydph12, POH1, and Po.hyd4 can be induced by natural light and cold stimulation during development from mycelia to primordia; Vmh3, FBH1, Hydph12, Po.hyd1-Po.hyd5, and Po.hyd8 were highly expressed in primordia and young fruiting bodies; Hydph12, Po.hyd1, Po.hyd4, and Po.hyd5 were specifically expressed in pilei. In addition, RNAi transformants of FBH1 exhibited slower growth rates and had fewer primordia and fruiting bodies, which suggests FBH1 affects the growth rate and primordia formation of P. ostreatus. Therefore, P. ostreatus hydrophobin genes belong to a large family and are temporally and spatially expressed to meet the developmental needs of mushroom.

Identification and In Silico Analysis of Lectins in Gray Oyster Culinary-Medicinal Mushroom Pleurotus ostreatus (Agaricomycetes) Based on the Transcriptomes.

Lectins, one of the most important bioactive compounds, are nonimmunoglobulin proteins that can bind carbohydrates specifically. However, few reports have been published on Pleurotus ostreatus lectin at the molecular level. Hence, in this study, seven lectins were identified based on transcriptomes in four developmental stages, i.e., mycelium, primordium, young fruiting body, and mature fruiting body. The expression profiles of the lectin genes were verified by quantitative real-time PCR. Lectin2-lectin6 had the highest expression in mycelium, while lectin1 was rich in mature fruiting body, and lectin7 was in primordium. We inferred that lectin2-lectin6 may take part in cell flocculation, lectin7 was the critical gene for primordium formation, and lectinl may be involved in fruiting body maturation, respectively. By in silico analysis, all lectins were divided into three distinct groups. Lectin1-Lectin5 were about 38.5-40.7 kDa as extracellular protein and belonged to the PCL-like lectins. Lectin6 (15.4 kDa) was predicted in nucleus and belonged to fungal fruit body lectins. Lectin7 (38.5 kDa) was a member of legume-like lectins and located in the plasma membrane. This study will help us understand how lectins mediate mushroom development.