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

Published online by Cambridge University Press:  03 November 2014

YING WANG
Affiliation:
State Key Laboratory of Silkworm genome Biology, Southwest University, Chongqing 400716, China
XIAOQUN DANG
Affiliation:
State Key Laboratory of Silkworm genome Biology, Southwest University, Chongqing 400716, China Laboratory of Animal Biology, Chongqing Normal University, Chongqing 400047, China
QIANG MA
Affiliation:
State Key Laboratory of Silkworm genome Biology, Southwest University, Chongqing 400716, China
FANGYAN LIU
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
TIAN LI
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 Laboratory of Animal Biology, Chongqing Normal University, Chongqing 400047, China
*
*Corresponding author. State Key Laboratory of Silkworm genome Biology, Southwest University, Chongqing 400716, China. E-mail: [email protected]

Summary

Nosema bombycis, a pathogen of silkworm pebrine, is an obligate unicellular eukaryotic parasite. It is reported that the spore wall proteins have essential functions in the adherence and infection process of microsporidia. To date, the information related to spore wall proteins from microsporidia is still limited. Here, a 44 kDa spore wall protein NbSWP16 was characterized in N. bombycis. In NbSWP16, a 25 amino acids signal peptide and 3 heparin binding motifs were predicted. Interestingly, a region that contains 3 proline-rich tandem repeats lacking homology to any known protein was also present in this protein. The immunofluorescence analysis (IFA) demonstrated that distinct fluorescent signals were detected both on the surface of mature spores and the germinated spore coats. Immunolocation by electron microscopy revealed that NbSWP16 localized on the exospore regions. Finally, spore adherence analysis indicated that spore adherence to host cell was decreased more than 20% by anti-NbSWP16 blocking compared with the negative control in vitro. In contrast with anti-NbSWP16, no remarkable decrement inhibition was detected when antibodies of NbSWP16 and NbSWP5 were used simultaneously. Collectively, these results suggest that NbSWP16 is a new exospore protein and probably be involved in spore adherence of N. bombycis.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2014 

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