A Nematode Effector, MiMSP8, Targets U2AF, a Subunit of a Splicing Factor Involved in Host pre-mRNA Splicing, Thereby

Cong Chen1,2, Wenjun Hu1,2, Chen Chen1,2

  • 1State Key Laboratory of Agricultural and Forestry Biosecurity, College of Plant Protection, Nanjing Agricultural University, Nanjing, China.

PubMed

Insights

Root-knot nematodes use the MiMSP8 effector to disrupt plant gene splicing. This nuclear effector targets the spliceosome, altering pre-mRNA splicing and increasing plant susceptibility to nematode infection.

Area of Science:

  • Plant-pathogen interactions
  • Molecular plant pathology
  • Nematode parasitism

Background:

  • Root-knot nematodes secrete effectors to parasitize plants.
  • The Meloidogyne incognita effector MiMSP8 localizes to the nucleus but its function is unknown.

Purpose of the Study:

  • To investigate the role of the MiMSP8 effector in nematode parasitism.
  • To elucidate the molecular mechanism by which MiMSP8 affects plant cells.

Main Methods:

  • Expression analysis of MiMSP8 in M. incognita and infected plant tissues.
  • Gene silencing and overexpression of MiMSP8 in plants.
  • Yeast three-hybrid assays to identify protein interactions.
  • Analysis of alternative splicing changes in response to MiMSP8 overexpression.
  • Investigating the effect of SlU2AF35 silencing on plant susceptibility.

Main Results:

  • MiMSP8 is expressed in M. incognita juveniles and detected in nematode-induced giant cells.
  • Silencing MiMSP8 reduces nematode parasitism, while overexpression increases susceptibility.
  • MiMSP8 interacts with tomato SlU2AF35, disrupting U2AF spliceosome complex formation.
  • MiMSP8 overexpression causes genome-wide alternative splicing alterations.
  • MiMSP8 interferes with pre-mRNA binding to SlU2AF35.
  • SlU2AF35 silencing leads to aberrant splicing and increased plant sensitivity to nematodes.

Conclusions:

  • Meloidogyne incognita utilizes the nuclear effector MiMSP8 to manipulate plant pre-mRNA splicing.
  • MiMSP8 targets the spliceosome component SlU2AF35, disrupting splicing to promote parasitism.
  • Understanding this interaction provides insights into nematode virulence strategies and potential control mechanisms.

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