Identification of a Nosema bombycis (Microsporidia) spore wall protein corresponding to spore phagocytosis
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Published on: April 6, 2022
Shunfeng Cai1, Xingmeng Lu, Haihong Qiu
1Laboratory of Invertebrate Pathology, Zhejiang University, Hangzhou 310029, China.
Abstract:
Life-cycle stages of the microsporidia Nosema bombycis, the pathogen causing silkworm pebrine, were separated and purified by an improved method of Percoll-gradient centrifugation. Soluble protein fractions of late sporoblasts (spore precursor cells) and mature spores were analysed by two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). Protein spots were recovered from gels and analysed by mass spectrometry. The most abundant differential protein spot was identified by database search to be a hypothetical spore wall protein. Using immunoelectron microscopy, we demonstrated that HSWP5 is localized to the exospore of mature spores and renamed it as spore wall protein 5 (NbSWP5). Further spore phagocytosis assays indicated that NbSWP5 can protect spores from phagocytic uptake by cultured insect cells. This spore wall protein may function both for structural integrity and in modulating host cell invasion.
Insights
Researchers identified a novel spore wall protein, NbSWP5, in Nosema bombycis, a silkworm pathogen. This protein strengthens spores and helps them evade insect cell defenses, offering insights into microsporidia infection mechanisms.
Area of Science:
- Microbiology
- Insect Pathology
- Molecular Biology
Background:
- Nosema bombycis is a microsporidian parasite causing pebrine disease in silkworms.
- Understanding the molecular mechanisms of N. bombycis spore structure and host interaction is crucial for disease management.
Purpose of the Study:
- To identify and characterize novel proteins involved in the structure and function of Nosema bombycis spores.
- To investigate the role of identified spore proteins in host cell interactions.
Main Methods:
- Improved Percoll-gradient centrifugation for separating microsporidia life-cycle stages.
- Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) for protein analysis.
- Mass spectrometry for protein identification.
- Immunoelectron microscopy for protein localization.
- Spore phagocytosis assays to assess host cell interactions.
Main Results:
- A hypothetical spore wall protein, HSWP5, was identified as the most abundant differential protein in mature spores.
- HSWP5 was localized to the exospore of mature N. bombycis spores and renamed spore wall protein 5 (NbSWP5).
- NbSWP5 demonstrated a protective effect against phagocytic uptake by cultured insect cells.
Conclusions:
- NbSWP5 is a key component of the N. bombycis spore wall, contributing to structural integrity.
- NbSWP5 plays a role in evading host immune responses, potentially by inhibiting phagocytosis.
- This spore wall protein is a potential target for developing novel strategies against microsporidian infections.
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