Title |
Interaction between hypoviral-regulated fungal virulence factor laccase3 and small heat shock protein Hsp24 from the chestnut blight fungus Cryphonectria parasitica |
Author |
Jeesun Chun†, Yo-Han Ko†, and Dae-Hyuk Kim* |
Address |
Department of Molecular Biology, Institute for Molecular Biology and Genetics, Jeonbuk National University, Jeonju 54896, Republic of Korea |
Bibliography |
Journal of Microbiology, 60(1),57-62, 2022,
|
DOI |
10.1007/s12275-022-1498-0
|
Key Words |
Cryphonectria parasitica, laccase3, small heat shock
protein 24, hypovirulence |
Abstract |
Laccase3 is an important virulence factor of the fungus Cryphonectria
parasitica. Laccase3 gene (lac3) transcription is
induced by tannic acid, a group of phenolic compounds found
in chestnut trees, and its induction is regulated by the hypovirus
CHV1 infection. CpHsp24, a small heat shock protein
gene of C. parasitica, plays a determinative role in stress adaptation
and pathogen virulence. Having uncovered in our previous
study that transcriptional regulation of the CpHsp24
gene in response to tannic acid supplementation and CHV1
infection was similar to that of the lac3, and that conserved
phenotypic changes of reduced virulence were observed in
mutants of both genes, we inferred that both genes were implicated
in a common pathway. Building on this finding, in this
paper we examined whether the CpHsp24 protein (CpHSP24)
was a molecular chaperone for the lac3 protein (LAC3). Our
pull-down experiment indicated that the protein products
of the two genes directly interacted with each other. Heterologous
co-expression of CpHsp24 and lac3 genes using Saccharomyces
cerevisiae resulted in more laccase activity in the cotransformant
than in a parental lac3-expresssing yeast strain.
These findings suggest that CpHSP24 is, in fact, a molecular
chaperone for the LAC3, which is critical component of fungal
pathogenesis. |