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Nbseptin2 Expression Pattern and Its Interaction with NbPTP1 during Microsporidia Nosema bombycis Polar Tube

Fangyan Liu1,2,3, Jie Chen1,2,3, Xiaoqun Dang4

  • 1State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, 400716, China.

The Journal of Eukaryotic Microbiology
|July 24, 2019
PubMed

Insights

Nosema bombycis septin2 (Nbseptin2) is crucial for microsporidia germination. This protein interacts with NbPTP1, aiding in spore invasion and understanding disease mechanisms.

Area of Science:

  • Microbiology
  • Cell Biology
  • Parasitology

Background:

  • Nosema bombycis causes pébrine disease, impacting sericulture.
  • Septins are vital for pathogen invasion and act as virulence factors.
  • Previous studies indicated Nbseptin2 interacts with NbSLP2.

Purpose of the Study:

  • To investigate the role of Nosema bombycis septin2 (Nbseptin2) in microsporidia germination.
  • To determine the localization and interaction partners of Nbseptin2 during spore germination.

Main Methods:

  • Immunofluorescence microscopy to track Nbseptin2 localization.
  • Co-immunoprecipitation and yeast two-hybrid assays to confirm protein interactions.

Main Results:

  • Nbseptin2 is primarily associated with the plasma membrane in spores.
  • Upon germination, Nbseptin2 co-localizes with NbPTP1 at the polar tube.
  • Nbseptin2 directly interacts with NbPTP1.

Conclusions:

  • Nbseptin2 plays a significant role in the polar tube extrusion process during microsporidia germination.
  • The interaction between Nbseptin2 and NbPTP1 is critical for Nosema bombycis invasion.
  • This study enhances understanding of microsporidia germination mechanisms.
Keywords:
Germinationlocalizationmembrane-associated proteinpolar capseptin

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