Identification and characterization of the Bombyx mori myosin II essential light chain and its effect in BmNPV infection

Authors

  • L J Hao Institute of Life Science, Jiangsu University, Zhenjiang, China
  • P Lü Institute of Life Science, Jiangsu University, Zhenjiang, China
  • L Gao Institute of Life Science, Jiangsu University, Zhenjiang, China
  • Y Zhou Institute of Life Science, Jiangsu University, Zhenjiang, China
  • Q Yao Institute of Life Science, Jiangsu University, Zhenjiang, China
  • Y H Yang Institute of Life Science, Jiangsu University, Zhenjiang, China
  • K P Chen Institute of Life Science, Jiangsu University, Zhenjiang, China

Keywords:

Bombyx mori, cell migration, myosin, ubiquitin

Abstract

Myosin, as a type of molecular motor, is mainly involved in muscle contraction. Recently, myosin research has made considerable progress. However, the function of Bombyx mori myosin remains unclear. In this study, we cloned the BmMyosin II essential light chain (BmMyosin II ELC) gene from a cDNA library of silkworm, which had an open reading frame (ORF) of 444 bp encoding 147 amino acids (about 16 kDa). After analyzing their sequences, BmMyosin II ELC was similar to the ELCs of 27 other Myosin II types, which contained EFh domain that bound Ca2+. In addition, 28 sequences had five motifs, motifs 1 and 3 were relatively conserved. We constructed two vectors with BmMyosin to transfect MGC803 or BmN, monolayer wound healing of cells indicated they can promote cell migration successfully. For three fifth instar silkworms, Bm306, BmNB, BmBC8, we mainly analyzed the change of BmMyosin II ELC from transcription and translation after infecting with nucleopolyhedrovirus (BmNPV). We found that gene expression of resistant strains were higher than susceptible strains at 12 h, while the result of the translation level was opposite that of the transcription level. Through in vitro protein interactions, we found BmMyosin II ELC can interact with BmNPV ubiquitin.

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Published

2015-02-02

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Section

Research Reports