Browsing by Author "Khan, Iqra Nafees"

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    Cross-kingdom global proteomics reveals specific modulation of disease signaling in multi-host fungal pathogen infection in chickpea and worm
    (American Chemical Society, 2026) Narula, Kanika; Ghosh, Shobha; Khan, Iqra Nafees; Sengupta, Atreyee; Chakraborty, Niranjan; Chakraborty, Subhra
    An interconnected loop of messages and counter-messages determine the outcome of host-pathogen interactions. Multihost pathogenicity across plants and animals, particularly nematode, is a major source of new infectious diseases. Fusarium oxysporum, a multihost pathogen, causes vascular wilt in chickpea and fusariosis in worm and humans. To comprehend Fusarium-responsive multihost pathogenicity, we temporally profiled cross-kingdom species, chickpea and worm using SWATH-mass spectrometry. Morphological analyses revealed that increased wilting and intestinal disintegration elicits a disease response in chickpea and worm. Peptide-spectrum library consisted of 5629 and 3138 proteins from Fusarium infected chickpea and worm, respectively. SWATH analysis identified 1573 and 2249 disease-responsive chickpea (CaDRPs) and worm proteins (CeDRPs) linked to diverse organs, organelles, and functionality. Pairwise comparisons; over-representation analysis between time, treatment, and organism; wilt, and fusariosis diseasome revealed common and unique modules. CaDRPs involved in preformed defense, biomolecule synthesis, phytohormone regulation, ser/thr kinase, and ATP signaling have perturbed interactions and functions, majorly in chloroplast. CeDRPs linked to the cuticular support, muscle organization, neuronal information, intestinal metabolism, G-protein, and notch signaling showed a deregulated function, especially in the cytoplasm. Common biological processes, included primary metabolism, ribosome biogenesis, calcium signaling, and proteostasis. Our data provide first evidence of translational plasticity in the Fusarium diseasome providing novel insights into multihost pathogenesis.
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    Nuclear proteome reprogramming and acquired thermotolerance in chickpea exposed to escalating high-temperature stress
    (Elsevier B.V., 2026) Pareek, Akanksha; Wardhan, Vijay; Mishra, Divya; Rathi, Divya; Khan, Iqra Nafees; Subba, Pratigya; Saxena, Harshita; Jeevaraj, Theboral; Chakraborty, Subhra; Chakraborty, Niranjan
    Global chickpea (Cicer arietinum L.) production amounted to ∼17.55 MMT during 2024-2025, whose market size is valued at ∼$16.83 billion. Chickpea is highly susceptible to high-temperature stress (HTS), and its yield declines 10-15% with the rise in each degree of temperature. In this study, the HTS-responsive nuclear proteome of a thermotolerant chickpea cultivar ICC 1205 was investigated, leading to the identification of 2705 proteins, including 424 differentially regulated proteins designated as HTS-responsive (HRPs). Of these, 212 were shared between immediate (day-1) and later (day-4) stages of HTS, with 117 proteins specific to day-1 and 95 to day-4. Functional network analysis revealed a complex network of nuclear proteins involved in regulatory and stress-related functions. Detailed analysis of the proteome revealed several non-canonical proteins, suggesting HTS-responsive reprograming of the nuclear proteome landscape. The cross-species multiple abiotic stress responses recognized unique HRPs, reflecting genetic foundation that leads to crop adaptation. Comparison of protein and mRNA expression shed light on the intricate regulatory mechanisms of thermotolerance response in chickpea. The characterization of root-phototropism 2 protein (CaRPT2), a member of the NPH3 gene-family, showed significant regulations, particularly under dehydration stress and ABA treatments. Subcellular localization of CaRPT2 demonstrated its dual localization in both plasma membrane and nucleus. Analysis of physiological indices in atrpt2 loss-of function mutants in Arabidopsis demonstrated better germination rate, resilience and growth under progressive HTS, suggesting the putative role of RPT2 in regulating multiple stress-responsive genes.