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<p>Mungbean Yellow Mosaic India Virus (MYMIV), a bipartite<i> Begomovirus</i>, significantly constrains pulse crop productivity across South and Southeast Asia. This study characterized the physicochemical and structural properties of MYMIV-encoded proteins using Multiple Protein Profiler 1.0 (MPP). Analysis encompassed proteins from both DNA-A and DNA-B components, revealing diverse molecular characteristics. Protein lengths ranged from 83 (AC5) to 362 (AC1) amino acids, with molecular weights between 9.1 and 41.3&#xa0;kDa. Most proteins exhibited hydrophilic properties (negative GRAVY values), except AC3 and AC5 which showed hydrophobic tendencies. Isoelectric points varied from acidic (AV2, pI 5.73) to highly basic (AC4, pI 10.0). Instability analysis indicated AC3, AC4 and BV1 are the most stable protein, while other proteins were classified as unstable. Secondary structure predictions revealed varying α-helix, β-sheet, and turn compositions. Aromaticity and extinction coefficient analyses further differentiated protein profiles. These findings demonstrate functional diversity among MYMIV proteins, providing insights into viral replication, movement, and host interactions, potentially informing targeted antiviral strategies and resistance breeding programs.</p>

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Proteomic Insights into Mungbean Yellow Mosaic Virus (MYMIV): A Comprehensive Profiling Approach Using Multiple Protein Profiler 1.0 (MPP)

  • 期刊论文

  • 发表日期：

    2026年4月9日

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  • Subham Dutta,
  • Mritunjoy Barman,
  • Souvik Chhandogi,
  • Moumita Panda,
  • Thomas Wilbur Davis,
  • Jayanta Tarafdar,
  • Gouranga Upadhyaya

摘要

Mungbean Yellow Mosaic India Virus (MYMIV), a bipartite Begomovirus, significantly constrains pulse crop productivity across South and Southeast Asia. This study characterized the physicochemical and structural properties of MYMIV-encoded proteins using Multiple Protein Profiler 1.0 (MPP). Analysis encompassed proteins from both DNA-A and DNA-B components, revealing diverse molecular characteristics. Protein lengths ranged from 83 (AC5) to 362 (AC1) amino acids, with molecular weights between 9.1 and 41.3 kDa. Most proteins exhibited hydrophilic properties (negative GRAVY values), except AC3 and AC5 which showed hydrophobic tendencies. Isoelectric points varied from acidic (AV2, pI 5.73) to highly basic (AC4, pI 10.0). Instability analysis indicated AC3, AC4 and BV1 are the most stable protein, while other proteins were classified as unstable. Secondary structure predictions revealed varying α-helix, β-sheet, and turn compositions. Aromaticity and extinction coefficient analyses further differentiated protein profiles. These findings demonstrate functional diversity among MYMIV proteins, providing insights into viral replication, movement, and host interactions, potentially informing targeted antiviral strategies and resistance breeding programs.