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A fungal pathogen secretes a cell wall-associated ß-N-acetylhexosaminidase that is co-expressed with chitinases to contribute to infection of insects.
Lu, Zhuoyue; Zhu, Qiankuan; Bai, Yuting; Zhao, Xin; Wang, Huifang; Peng, Xinxin; Luo, Zhibing; Zhang, Yongjun.
Affiliation
  • Lu Z; Key Laboratory of Agricultural Biosafety and Green Production of Upper Yangtze River (Ministry of Education), College of Plant Protection, Southwest University, Chongqing, People's Republic of China.
  • Zhu Q; Key Laboratory of Entomology and Pest Control Engineering, Beibei Culture Collection of Chongqing Agricultural Microbiology, Chongqing, People's Republic of China.
  • Bai Y; Key Laboratory of Agricultural Biosafety and Green Production of Upper Yangtze River (Ministry of Education), College of Plant Protection, Southwest University, Chongqing, People's Republic of China.
  • Zhao X; Key Laboratory of Entomology and Pest Control Engineering, Beibei Culture Collection of Chongqing Agricultural Microbiology, Chongqing, People's Republic of China.
  • Wang H; Key Laboratory of Agricultural Biosafety and Green Production of Upper Yangtze River (Ministry of Education), College of Plant Protection, Southwest University, Chongqing, People's Republic of China.
  • Peng X; Key Laboratory of Entomology and Pest Control Engineering, Beibei Culture Collection of Chongqing Agricultural Microbiology, Chongqing, People's Republic of China.
  • Luo Z; Key Laboratory of Agricultural Biosafety and Green Production of Upper Yangtze River (Ministry of Education), College of Plant Protection, Southwest University, Chongqing, People's Republic of China.
  • Zhang Y; Key Laboratory of Entomology and Pest Control Engineering, Beibei Culture Collection of Chongqing Agricultural Microbiology, Chongqing, People's Republic of China.
Pest Manag Sci ; 2024 May 21.
Article de En | MEDLINE | ID: mdl-38771009
ABSTRACT

BACKGROUND:

ß-N-acetylhexosaminidases (HEXs) are widely distributed in fungi and involved in cell wall chitin metabolism and utilization of chitin-containing substrates. However, details of the fungal pathogens-derived HEXs in the interaction with their hosts remain limited.

RESULTS:

An insect nutrients-induced ß-N-acetylhexosaminidase, BbHex1, was identified from the entomopathogenic fungus Beauveria bassiana, which was involved in cell wall modification and degradation of insect cuticle. BbHex1 was localized to cell wall and secreted, and displayed enzyme activity to degrade the chitinase-hydrolyzed product (GlcNAc)2. Disruption of BbHex1 resulted in a significant decrease in the level of cell wall chitin in the presence of insect nutrients and during infection of insects, with impaired ability to penetrate insect cuticle, accompanying downregulated cell wall metabolism-involved and cuticle-degrading chitinase genes. However, the opposite phenotypes were examined in the gene overexpression strain. Distinctly altered cell wall structures caused by BbHex1 mutation and overexpression led to the easy activation and evasion (respectively) of insect immune response during fungal infection. As a result, BbHex1 contributed to fungal virulence. Bioinformatics analysis revealed that promoters of some co-expressed chitinase genes with the BbHex1 promoter shared conserved transcription factors Skn7, Msn2 and Ste12, and CreA-binding motifs, implying co-regulation of those genes with BbHex1.

CONCLUSION:

These data support a mechanism that the fungal pathogen specifically expresses BbHex1, which is co-expressed with chitinases to modify cell wall for evasion of insect immune recognition and to degrade insect cuticle, and contributes to the fungal virulence against insects. © 2024 Society of Chemical Industry.
Mots clés

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Langue: En Journal: Pest Manag Sci Sujet du journal: TOXICOLOGIA Année: 2024 Type de document: Article

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Langue: En Journal: Pest Manag Sci Sujet du journal: TOXICOLOGIA Année: 2024 Type de document: Article
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