Publications by authors named "De-Jie Cheng"

Article Synopsis
  • Viral diseases, particularly the sweet potato virus 2 (SPV2), are major threats to sweet potato crops globally, with SPV2 being a primary pathogen.
  • Researchers detected a new isolate of SPV2 (SPV2-LN) in a plant called Ipomoea nil in China, analyzing its complete genome and comparing it to existing isolates.
  • The study found that the SPV2-LN genome has specific characteristics and similarities to another isolate, which could help in understanding and managing sweet potato viral diseases better.
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Cucumis melo L. is an important fruit with widespread consumption and commercial value. However, an undescribed disease affecting Hami melon (Cucumis melo L.

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In recent years, the sugarcane streak mosaic virus (SCSMV) has been the primary pathogen of sugarcane mosaic disease in southern China. In this study, the complete genome of a sugarcane mosaic sample (named YN-21) from Kaiyuan City, Yunnan Province, was amplified and sequenced. By comparing the amino acid sequences of YN-21 and 15 other SCSMV isolates from the NCBI database, the protease recognition site of SCSMV was determined.

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Chloroplasts play an indispensable role in the arms race between plant viruses and hosts. Chloroplast proteins are often recruited by plant viruses to support viral replication and movement. However, the mechanism by which chloroplast proteins regulate potyvirus infection remains largely unknown.

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Potyviral coat protein (CP) is involved in the replication and movement of potyviruses. However, little information is available on the roles of CP-coding sequence in potyviral infection. Here, we introduced synonymous substitutions to the codon CGC coding conserved residue arginine at position 192 (R) of tobacco vein banding mosaic virus (TVBMV) CP.

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Potyviruses move to neighboring cells in the form of virus particles or a coat protein (CP)-containing ribonucleoprotein complex. However, the precise roles of RNA-binding residues in potyviral CP in viral cell-to-cell movement remain to be elucidated. In this study, we predicted the three-dimensional model of tobacco vein banding mosaic virus (TVBMV)-encoded CP and found nine residues presumably located in the CP RNA-binding pocket.

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Article Synopsis
  • Coat proteins (CPs) are essential for the movement of potyviruses between plant cells, with specific focus on the role of tryptophan at position 122 in the CP of tobacco vein banding mosaic virus (TVBMV).
  • Substitutions of tryptophan with other amino acids, such as alanine or glutamic acid, severely hindered virus movement and resulted in reduced levels of CP and viral RNA in affected plants.
  • The study suggests that the aromatic structure of tryptophan is crucial for maintaining CP stability and efficient viral replication, with similar findings observed in related viruses like watermelon mosaic virus and potato virus Y.
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Cross-protection is a promising measure to control plant viral diseases. Reverse genetics had been recently adopted to generate attenuated mutants that have potential in cross-protection. But studies on the variability of the progeny viruses of the attenuated mutants are scarce.

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Article Synopsis
  • - Potato virus Y (PVY) is a significant threat to potato and tobacco crops globally; researchers cloned the genome of a specific PVY strain from China into a vector for experimentation.
  • - A modified plasmid, pCamPVY-GZ-GFP, was created to express a green fluorescence protein, allowing for the tracking of PVY infections in various plants, showing successful infection in several species including potato and tomato.
  • - A mutant strain of PVY, named PVY-K391R/E410D, was engineered to lack certain harmful effects on tobacco plants and demonstrated the ability to protect these plants from severe PVY strains, suggesting a new method for disease prevention.
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Chloroplast-bound vesicles are key components in viral replication complexes (VRCs) of potyviruses. The potyviral VRCs are induced by the second 6 kDa protein (6K2) and contain at least viral RNA and nuclear inclusion protein b. To date, no chloroplast protein has been identified to interact with 6K2 and involve in potyvirus replication.

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