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<p><i>Leishmania donovani</i> is the causative agent of the fatal visceral leishmaniasis (VL) disease in humans in the tropical regions, mainly the Indian Subcontinent and Africa. We have previously described centrin1, a basal body associated cell division specific protein in this parasite important for the parasite’s host intracellular stage. In this study, we identified a novel centrin1-binding protein called <i>LdDRP</i> through pull-down and MS/MS analysis, which is a homolog of the XPC protein of humans involved in DNA damage. The protein interaction with <i>LdCen1</i> was also confirmed through peptide spectrum analysis against the UniProt database. Immunofluorescence analysis confirms that <i>LdDRP</i> is localized within the nucleus, suggesting the protein’s possible role in DNA interaction. The overexpression of three <i>LdDRP</i> forms in the parasite, each fused with HA-tag (<i>LdDRPF</i> [full length] <i>LdDRPN</i> [only N-terminal], and <i>LdDRPC</i> [only C-terminal]), revealed that only <i>LdDRPF</i> and <i>LdDRPC</i> were able to support the retention of the parasite’s shape and promote rapid division following the UV-damage recovery period. This was also correlated to the elevated expression level of both <i>LdDRPC</i> and <i>LdCen1</i>, by Western blot analysis soon after UV-C exposure in the parasites compared to control. The study emphasizes the role of the <i>LdDRP</i>, and its crucial domains involved in the DNA binding process, DNA damage response, and interaction with centrin, particularly in response to UV-C light-induced DNA damage.</p>

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Mechanistic insights into LdCen1-LdDRP interaction facilitating UV-induced DNA damage repair in Leishmania donovani

  • 期刊论文

  • 发表日期：

    2025年4月9日

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  • Roshanara,
  • Rati Tandon,
  • Niti Puri,
  • A. Selvapandiyan

摘要

Leishmania donovani is the causative agent of the fatal visceral leishmaniasis (VL) disease in humans in the tropical regions, mainly the Indian Subcontinent and Africa. We have previously described centrin1, a basal body associated cell division specific protein in this parasite important for the parasite’s host intracellular stage. In this study, we identified a novel centrin1-binding protein called LdDRP through pull-down and MS/MS analysis, which is a homolog of the XPC protein of humans involved in DNA damage. The protein interaction with LdCen1 was also confirmed through peptide spectrum analysis against the UniProt database. Immunofluorescence analysis confirms that LdDRP is localized within the nucleus, suggesting the protein’s possible role in DNA interaction. The overexpression of three LdDRP forms in the parasite, each fused with HA-tag (LdDRPF [full length] LdDRPN [only N-terminal], and LdDRPC [only C-terminal]), revealed that only LdDRPF and LdDRPC were able to support the retention of the parasite’s shape and promote rapid division following the UV-damage recovery period. This was also correlated to the elevated expression level of both LdDRPC and LdCen1, by Western blot analysis soon after UV-C exposure in the parasites compared to control. The study emphasizes the role of the LdDRP, and its crucial domains involved in the DNA binding process, DNA damage response, and interaction with centrin, particularly in response to UV-C light-induced DNA damage.