GH16 Glycoside Hydrolases Divergently Contribute to Fungal Development, Stress Tolerance, and Virulence of an Insect Fungal Pathogen.

J Agric Food Chem

Key Laboratory of Agricultural Biosafety and Green Production of Upper Yangtze River (Ministry of Education), College of Plant Protection, Southwest University, Chongqing 400715, P. R. China.

Published: August 2025


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Article Abstract

Fungal glycoside hydrolases (GHs) include β-glucanases and glycosyltransferases, which are involved in fungal cell wall metabolism and crucial for fungal development and adaptation to varied environments and host niches. However, many GHs in entomopathogenic fungi (EPF) have not been well characterized. Here, 13 detectably expressed members of the GH16 family were systemically and genetically characterized in the EPF . Ten and nine proteins were differently involved in cell wall β-glucan metabolism and chitin assembly/metabolism, respectively. Eight to twelve members were differently associated with conidiation, conidial morphology, germination, response to cell wall/membrane stresses, and fungal virulence, in which contributions of nine members to conidial germination and/or stress response were correlated to their roles in virulence. Five virulence-related members were involved in evasion of insect immune defense response via reducing different pathogen-associated molecular patterns, β-1,3-glucan. As a result, GH16 members divergently contribute to fungal development, stress response, and virulence via orchestrating cell wall remodeling.

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http://dx.doi.org/10.1021/acs.jafc.5c06747DOI Listing

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