scholarly journals Expression and localization of the spore wall protein SWP26 of <i>Nosema bombycis </i>in the silkworm BmN cell line

2013 ◽  
Vol 04 (02) ◽  
pp. 79-84
Author(s):  
Feng Zhu ◽  
Zhongyuan Shen ◽  
Shengyan Xiao ◽  
Yajie Yue ◽  
Xuliang Fu ◽  
...  
Keyword(s):  
Cell Line ◽  
Spore Wall ◽  
Nosema Bombycis ◽  
Bmn Cell

Identification of a protein interacting with the spore wall protein SWP26 of Nosema bombycis in a cultured BmN cell line of silkworm

2013 ◽  
Vol 17 ◽  
pp. 38-45 ◽  
Author(s):  
Feng Zhu ◽  
Zhongyuan Shen ◽  
Jiange Hou ◽  
Jiao Zhang ◽  
Tao Geng ◽  
...  
Keyword(s):  
Cell Line ◽  
Spore Wall ◽  
Nosema Bombycis ◽  
Bmn Cell

scholarly journals The role of NbTMP1, a surface protein of sporoplasm, in Nosema bombycis infection

2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Shiyi Zheng ◽  
Yukang Huang ◽  
Hongyun Huang ◽  
Bin Yu ◽  
Ni Zhou ◽  
...  
Keyword(s):  
Indirect Immunofluorescence ◽  
Selective Breeding ◽  
Developmental Stages ◽  
Transmembrane Protein ◽  
Surface Protein ◽  
Spore Wall ◽  
Significant Inhibition ◽  
Pcr Analysis ◽  
Immunofluorescence Analysis ◽  
Nosema Bombycis

Abstract Background Nosema bombycis is a unicellular eukaryotic pathogen of the silkworm, Bombyx mori, and is an economic and occupational hazard in the silkworm industry. Because of its long incubation period and horizontal and vertical transmission, it is subject to quarantine measures in sericulture production. The microsporidian life-cycle includes a dormant extracellular phase and intracellular proliferation phase, with the proliferation period being the most active period. This latter period lacks spore wall protection and may be the most susceptible stage for control. Methods In order to find suitable target for the selective breeding of N. bombycis-resistant silkworm strains, we screen highly expressed membrane proteins from the transcriptome data of N. bombycis. The subcellular localization of the candidate protein was verified by Indirect immunofluorescence analysis (IFA) and immunoelectron microscopy (IEM), and its role in N. bombycis proliferation was verified by RNAi. Results The N. bombycis protein (NBO_76g0014) was identified as a transmembrane protein and named NbTMP1. It is homologous with hypothetical proteins NGRA_1734 from Nosema granulosis. NbTMP1 has a transmembrane region of 23 amino acids at the N-terminus. Indirect immunofluorescence analysis (IFA) results suggest that NbTMP1 is secreted on the plasma membrane as the spores develop. Western blot and qRT-PCR analysis showed that NbTMP1 was expressed in all developmental stages of N. bombycis in infected cells and in the silkworm midgut. Downregulation of NbTMP1 expression resulted in significant inhibition of N. bombycis proliferation. Conclusions We confirmed that NbTMP1 is a membrane protein of N. bombycis. Reduction of the transcription level of NbTMP1 significantly inhibited N. bombycis proliferation, and this protein may be a target for the selective breeding of N. bombycis-resistant silkworm strains.

scholarly journals Interaction between SWP9 and Polar Tube Proteins of the Microsporidian Nosema bombycis and Function of SWP9 as a Scaffolding Protein Contribute to Polar Tube Tethering to the Spore Wall

2016 ◽  
Vol 85 (3) ◽  
Author(s):  
Donglin Yang ◽  
Lixia Pan ◽  
Pai Peng ◽  
Xiaoqun Dang ◽  
Chunfeng Li ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Spore Wall ◽  
Scaffolding Protein ◽  
Dependent Manner ◽  
Polar Tube ◽  
Content Type ◽  
Nosema Bombycis ◽  
Invasion Mechanism ◽  
In The Beginning ◽  
And Function

ABSTRACTAll microsporidia possess a unique, highly specialized invasion mechanism that involves the polar tube and spore wall. The interaction between spore wall proteins (SWPs) and polar tube proteins (PTPs) in the formation, arrangement, orderly orientation, and function of the polar tube and spore wall remains to be determined. This study was undertaken to examine the protein interactions ofNosema bombycisSWP7 (NbSWP7), NbSWP9, and PTPs. Coimmunoprecipitation, liquid chromatography-tandem mass spectrometry (LC-MS/MS), and yeast two-hybrid data demonstrated that NbSWP9, but not NbSWP7, interacts with NbPTP1 and NbPTP2. Furthermore, immunoelectron microscopy (IEM) showed that NbSWP9 was localized mainly in the developing polar tube of sporoblasts, while NbSWP7 was found randomly in the cytoplasm. However, both NbSWP9 and NbSWP7 were located in the polar tube and spore wall ofN. bombycismature spores. The reason why NbSWP7 was localized to the polar tube may be due to the interaction between NbSWP9 and NbSWP7. Interestingly, the majority of NbSWP9, but not NbSWP7, accumulated in the beginning part of the extruded polar tube and the ruptured spore wall called the anchoring disk (AD) when the mature spores germinated under weak-alkaline environmental stimulation. Additionally, anti-NbSWP9 antibody reduced spore germination in a dose-dependent manner. In conclusion, our study further confirmed that NbSWP9 is a scaffolding protein that not only anchors and holds the polar tube but also tethers the polar tube to the spore wall.

scholarly journals Interaction and Assembly of Two Novel Proteins in the Spore Wall of the Microsporidian Species Nosema bombycis and Their Roles in Adherence to and Infection of Host Cells

2015 ◽  
Vol 83 (4) ◽  
pp. 1715-1731 ◽  
Author(s):  
Donglin Yang ◽  
Guoqing Pan ◽  
Xiaoqun Dang ◽  
Yawei Shi ◽  
Chunfeng Li ◽  
...  
Keyword(s):  
Host Cell ◽  
Spore Wall ◽  
Host Cells ◽  
Scaffolding Protein ◽  
Environmental Pressures ◽  
Content Type ◽  
Nosema Bombycis ◽  
Major Function ◽  
Microsporidian Species

Microsporidia are obligate intracellular parasites with rigid spore walls that protect against various environmental pressures. Despite an extensive description of the spore wall, little is known regarding the mechanism by which it is deposited or the role it plays in cell adhesion and infection. In this study, we report the identification and characterization of two novel spore wall proteins, SWP7 and SWP9, in the microsporidian speciesNosema bombycis. SWP7 and SWP9 are mainly localized to the exospore and endospore of mature spores and the cytoplasm of sporonts, respectively. In addition, a portion of SWP9 is targeted to the spore wall of sporoblasts earlier than SWP7 is. Both SWP7 and SWP9 are specifically colocalized to the spore wall in mature spores. Furthermore, immunoprecipitation, far-Western blotting, unreduced SDS-PAGE, and yeast two-hybrid data demonstrated that SWP7 interacted with SWP9. The chitin binding assay showed that, within the total spore protein, SWP9 and SWP7 can bind to the deproteinated chitin spore coats (DCSCs) ofN. bombycis. However, binding of the recombinant protein rSWP7-His to the DCSCs is dependent on the combination of rSWP9–glutathioneS-transferase (GST) with the DCSCs. Finally, rSWP9-GST, anti-SWP9, and anti-SWP7 antibodies decreased spore adhesion and infection of the host cell. In conclusion, SWP7 and SWP9 may have important structural capacities and play significant roles in modulating host cell adherence and infectionin vitro. A possible major function of SWP9 is as a scaffolding protein that supports other proteins (such as SWP7) that form the integrated spore wall ofN. bombycis.

l-Cysteine induced hemin/G-quadruplex concatemers electrocatalytic amplification with Pt–Pd supported on fullerene as a nanocarrier for sensing the spore wall protein of Nosema bombycis

2015 ◽  
Vol 51 (7) ◽  
pp. 1255-1258 ◽  
Author(s):  
Qin Wang ◽  
Yue Song ◽  
Hua Xie ◽  
Yaqin Chai ◽  
Yali Yuan ◽  
...  
Keyword(s):  
Spore Wall ◽  
Nosema Bombycis ◽  
G Quadruplex

This work described an amplified immunosensor for sensing spore wall protein (SWP) ofN. bombycisbased on a novel electrocatalytic function of C60@Pt–Pd loaded with hemin/G-quadruplex.

Identification of a Nosema bombycis (Microsporidia) spore wall protein corresponding to spore phagocytosis

Parasitology ◽  
2011 ◽  
Vol 138 (9) ◽  
pp. 1102-1109 ◽  
Author(s):  
SHUNFENG CAI ◽  
XINGMENG LU ◽  
HAIHONG QIU ◽  
MINGQIAN LI ◽  
ZHENZHEN FENG
Keyword(s):  
Structural Integrity ◽  
Insect Cells ◽  
Gradient Centrifugation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Spore Wall ◽  
Host Cell Invasion ◽  
Improved Method ◽  
Nosema Bombycis ◽  
Life Cycle Stages ◽  
Phagocytic Uptake

SUMMARYLife-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.

Characterization of a novel spore wall protein NbSWP16 with proline-rich tandem repeats from Nosema bombycis (microsporidia)

Parasitology ◽  
2014 ◽  
Vol 142 (04) ◽  
pp. 534-542 ◽  
Author(s):  
YING WANG ◽  
XIAOQUN DANG ◽  
QIANG MA ◽  
FANGYAN LIU ◽  
GUOQING PAN ◽  
...  
Keyword(s):  
Tandem Repeats ◽  
Spore Wall ◽  
Nosema Bombycis

Development of an approach to analyze the interaction between Nosema bombycis (microsporidia) deproteinated chitin spore coats and spore wall proteins

2014 ◽  
Vol 115 ◽  
pp. 1-7 ◽  
Author(s):  
Donglin Yang ◽  
Xiaoqun Dang ◽  
Rui Tian ◽  
Mengxian Long ◽  
Chunfeng Li ◽  
...  
Keyword(s):  
Spore Wall ◽  
Nosema Bombycis
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