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Horizontal gene transfer of Cccyt contributes to virulence of mycoparasite Calcarisporium cordycipiticola by interacting with a host heat shock protein.

Authors :
Xu, Yanyan
Liu, Qing
Meng, Guoliang
Dong, Caihong
Source :
International Journal of Biological Macromolecules. Jul2023:Part 4, Vol. 242, pN.PAG-N.PAG. 1p.
Publication Year :
2023

Abstract

Horizontal gene transfer (HGT) is an important driving force for virulence evolution of pathogens, however, functions of these transferred genes are still not fully investigated. Here, an HGT effector, CcCYT was reported to contribute to virulence of a mycoparasite, Calcarisporium cordycipiticola to the host Cordyceps militaris, an important mushroom. Cccyt was predicted to be horizontally transferred from Actinobacteria ancestor by phylogenetic, synteny, GC content and codon usage pattern analyses. The transcript of Cccyt was sharply up-regulated at the early stage of infecting C. militaris. This effector was localized to the cell wall and contributed to the virulence of C. cordycipiticola without affecting its morphology, mycelial growth, conidiation, and resistance to abiotic stress. CcCYT can firstly bind the septa, and finally cytoplasm of the deformed hyphal cells of C. militaris. Pull-down assay coupled mass spectrometry revealed that proteins with which CcCYT interacted were related to protein process, folding and degradation. GST-Pull down assay confirmed that C. cordycipiticola effector CcCYT can interact with host protein CmHSP90 to inhibit the immune response of host. The results provided functional evidence that HGT is an important driving force for the virulence evolution and will be helpful for revealing the interaction between mycoparasite and mushroom host. [Display omitted] • C. cordycipiticola Cccyt was originated from a cross-kingdom gene transfer event. • CcCYT is a typical effector located to the cell wall of C. cordycipiticola. • Cccyt is not necessary for growth but contributes to virulence of C. cordycipiticola. • CcCYT binds the septa of C. militaris and interacts with a host heat shock protein. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
01418130
Volume :
242
Database :
Academic Search Index
Journal :
International Journal of Biological Macromolecules
Publication Type :
Academic Journal
Accession number :
164301345
Full Text :
https://doi.org/10.1016/j.ijbiomac.2023.124927