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Recently, the team of Li Bin, a researcher from the Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, has made important progress in the antiviral mechanism of porcine coronavirus-porcine epidemic diarrhea virus (PEDV) variant strain escape complement C3.
The related research results are titled "No.
"nstructural protein 1 of variant PEDV plays a key role in escaping replication restriction by complement C3" was published online in the Journal of Virology, an international authoritative journal in the field of virology (IF=6.
5, top journal)
.
Researcher Li Bin is the corresponding author of the paper, animal Associate researcher Fan Baochao and postdoctoral fellow Peng Qi of the diarrheal disease prevention and control innovation team are the co-first authors of the paper
.
The related research results are titled "No.
"nstructural protein 1 of variant PEDV plays a key role in escaping replication restriction by complement C3" was published online in the Journal of Virology, an international authoritative journal in the field of virology (IF=6.
5, top journal)
.
Researcher Li Bin is the corresponding author of the paper, animal Associate researcher Fan Baochao and postdoctoral fellow Peng Qi of the diarrheal disease prevention and control innovation team are the co-first authors of the paper
.
Porcine epidemic diarrhea virus (PEDV) of the alphacoronavirus genus was first identified in the 1970s and has since spread around the world
.
Since 2010, outbreaks of highly pathogenic PEDV variants have caused huge economic losses to the global swine industry
.
Compared with the classic strain, the PEDV variant strain is more pathogenic, and still occurs in pig farms immunized with the original vaccine, but its virulence enhancement and immune escape mechanisms are still unclear
.
.
Since 2010, outbreaks of highly pathogenic PEDV variants have caused huge economic losses to the global swine industry
.
Compared with the classic strain, the PEDV variant strain is more pathogenic, and still occurs in pig farms immunized with the original vaccine, but its virulence enhancement and immune escape mechanisms are still unclear
.
The complement system is an important part of the organism's immune system and plays an important role in anti-viral infection.
Among them, the complement molecule C3 is at the core of the activation of the three complement pathways, and it can also participate in the intracellular immune response
.
In this study, we found that C3 transcript levels were significantly reduced in the intestinal epithelial cells of piglets infected with PEDV variants
.
In vitro, through the interference and overexpression of C3, C3 was found to significantly inhibit the replication of PEDV
.
Among them, the complement molecule C3 is at the core of the activation of the three complement pathways, and it can also participate in the intracellular immune response
.
In this study, we found that C3 transcript levels were significantly reduced in the intestinal epithelial cells of piglets infected with PEDV variants
.
In vitro, through the interference and overexpression of C3, C3 was found to significantly inhibit the replication of PEDV
.
The researchers used the human liver cancer cell line Huh7 to conduct virus infection test, and found that compared with the classic PEDV strain, the mutant strain significantly inhibited the transcription and expression levels of C3 in Huh7; it was further found that both the PEDV mutant strain and the classic strain induced high levels of IL-1β in the cells.
, but the variant strain significantly downregulated IL-1β-induced C3 transcription and expression compared with the PEDV classic strain
.
In-depth study found that the PEDV variant strain inhibited C3 transcription by inhibiting the phosphorylation of C/EBP-β in the C3 expression signaling pathway p38-MAPK-C/EBP-β
.
, but the variant strain significantly downregulated IL-1β-induced C3 transcription and expression compared with the PEDV classic strain
.
In-depth study found that the PEDV variant strain inhibited C3 transcription by inhibiting the phosphorylation of C/EBP-β in the C3 expression signaling pathway p38-MAPK-C/EBP-β
.
Through the screening of viral proteins and the construction of site mutants, it is clear that the 50th amino acid of PEDV non-structural protein nsp1 has the function of regulating C/EBP-β phosphorylation
.
Finally, the researchers constructed the corresponding site mutant strains and verified at the virus level that the 50th amino acid of PEDV nsp1 plays a key role in regulating C3 expression
.
.
Finally, the researchers constructed the corresponding site mutant strains and verified at the virus level that the 50th amino acid of PEDV nsp1 plays a key role in regulating C3 expression
.
This study is the first to report the anti-PEDV infection ability of complement C3, and found that PEDV mutants can evade its antiviral effect by downregulating C3 expression, revealing a new immune evasion strategy of PEDV mutants, deepening the pathogenesis of the pathogen.
The understanding of the pathogenesis also provides new ideas for the prevention and control of coronavirus
.
The understanding of the pathogenesis also provides new ideas for the prevention and control of coronavirus
.
The research was funded by the 14th Five-Year National Key R&D Program (2021YFD1801104), the National Natural Science Foundation of China, the Natural Science Foundation of Jiangsu Province, the Independent Innovation Fund of Jiangsu Province, and the subversive exploratory projects of the Institute
.
.
Original link: https://journals.
asm.
org/doi/10.
1128/jvi.
01024-22
asm.
org/doi/10.
1128/jvi.
01024-22
