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Identification of a novel chitin-binding spore wall protein (NbSWP12) with a BAR-2 domain from Nosema bombycis (microsporidia)

Published online by Cambridge University Press:  07 August 2013

JIE CHEN
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
LINA GENG
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
MENGXIAN LONG
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
TIAN LI
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
ZHI LI
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China College of Life Sciences, Chongqing Normal University, Chongqing 400047, China
DONGLIN YANG
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
CHAO MA
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
HAIJING WU
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
ZHENGANG MA
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
CHUNFENG LI
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
GUOQING PAN
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China
ZEYANG ZHOU
Affiliation:
State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing 400716, China College of Life Sciences, Chongqing Normal University, Chongqing 400047, China
Corresponding
E-mail address:

Summary

The spore wall of Nosema bombycis plays an important role in microsporidian pathogenesis. Protein fractions from germinated spore coats were analysed by two-dimensional polyacrylamide gel electrophoresis and MALDI-TOF/TOF mass spectrometry. Three protein spots were identified as the hypothetical spore wall protein NbHSWP12. A BAR-2 domain (e-value: 1.35e-03) was identified in the protein, and an N-terminal protein-heparin interaction motif, a potential N-glycosylation site, and 16 phosphorylation sites primarily activated by protein kinase C were also predicted. The sequence analysis suggested that Nbhswp12 and its homologous genes are widely distributed among microsporidia. Additionally, Nbhswp12 gene homologues share similar sequence features. An indirect immunofluorescence analysis showed that NbHSWP12 localized to the spore wall, and thus we renamed it spore wall protein 12 (NbSWP12). Moreover, NbSWP12 could adhere to deproteinized N. bombycis chitin coats that were obtained by hot alkaline treatment. This novel N. bombycis spore wall protein may function in a structural capacity to facilitate microsporidial spore maintenance.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2013 

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References

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Identification of a novel chitin-binding spore wall protein (NbSWP12) with a BAR-2 domain from Nosema bombycis (microsporidia)
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