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Dali rogi is a soil-based pathogenic fungus, which infects plant roots by forming attached branches, causing serious yellow wilt disease in the world and causing huge economic losses to China's cotton production.
like other pathogenic microorganisms, one of the important pathogenic strategies of Dali-Mycobacteria is to secrete effect proteins to plant cells, interfering with plant immune response, but its secretion structure and secretion transport mechanism need to be explored.
Guo Huishan, a researcher at the Institute of Microbiology of the Chinese Academy of Sciences, continued to carry out research on the secretion protein delivery pathways during the invasion and infection of Dali-round mycobacteria on the basis of the early discovery of the attached branches of the dali-round mycobacteria-infested structure.
The team found that Dali rogi by repeatedly forming attachment branches and penetrating nails to pierce the root cell wall of the plant, when the formation of invasive mycelium, penetration nails into mycelium neck ring (Figure A), and with the host to form a close interoperability of the penetration interface. Through cell biology, the
team found that the cell skeletons of Dali mycobacteria, Septin5 and F-actin, were located in the form of rings (Septin rings), where secretion proteins were secreted in large quantities outside the Septin ring (Figure B);
further experiments show that vesicle transport factors VdSec22, VdSyn8 and cell vomit sub-base VdExo70 are involved in the transfer and transport of secreted proteins, the absence of which leads to the retention of secretion proteins in attached branches within the cervical ring of mycelium; the knockout mutations of the VdSep5, VdSec22, VdSyn8, and VdExo70 genes significantly reduced the pathogenicity of Otsia on cotton.
A: Terrieric mycobacteria attachment branch (HP), mycelium neck (HN) and invasive mycelium (IH) electroscopic diagram.
B: Secretion protein VdSCPs-GFP (green fluorescence) is located on the periphery of the mycelium neck ring composed of Septin5 skeleton protein (red fluorescence).
C: A diagram of multiple proteins involved in secreting protein transport to the penetration interface.
This study is the first to clarify the secretion protein transport mechanism of Septin5, that is, Septin5 skeleton protein is assembled in the mycelium neck ring and forms a fungal-host penetration interface, which can effectively secrete effect protein;
the study was published in the international journal PLoS Pathogens.
,000-year-old doctoral student Zhou Wei is the first author of the thesis, and Guo Huishan is the author of the communication.
research has been supported by the Strategic Pilot (Class B) project of the Chinese Academy of Sciences and the Ministry of Agriculture's major gm-modified projects.
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