@article{MAKHILLJAVA201211203804,
    title = {Expression of the B Subunit of <I>Escherichia coli</I> Heat-Labile Enterotoxin in Transformed <I>Bombyx mori</I> BmN Cells},
    journal = {Journal of Animal and Veterinary Advances},
    volume = {11},
    number = {20},
    pages = {3785-3791},
    year = {2012},
    issn = {1680-5593},
    doi = {javaa.2012.3785.3791},
    url = {https://makhillpublications.co/view-article.php?issn=1680-5593&doi=javaa.2012.3785.3791},
    author = {Jin-Ru,Hong-Biao,Cheng-Liang,Ai-Hong,Wen-Lin,Li-Hua,Ren-Yu,Guang-Li and},
    keywords = {Escherichia coli heat-labile enterotoxin,piggyBac transposon,Bombyx mori,BmN cell,genetic transformation},
    abstract = {The non-toxic B subunit of<I> Escherichia coli</I> heat-labile 
  enterotoxin (LTB) is a potent mucosal immunogen and immunoadjuvant for coadministered 
  antigens. To obtain transformed silkworm cell line stably expressing LTB, researchers 
  fused the LTB coding sequence, neomycin-resistance gene (<I>Neo<SUP>R</SUP></I>) 
  and <I>gfp</I> gene into piggyBac-based transponson vector and transduced into 
  silkworm BmN cells. After screening against antibiotic G418, the positive rate 
  of cells emitting green fluorescence was 70.79%. PCR detection indicates the 
  existence of exogenous LTB coding sequence, Neo<SUP>R</SUP> and gfp in the transformed 
  cell genome. Western blot analysis also confirms the predicated ~60 kDa band 
  of LTB protein. These results demonstrated that the strategy was practicable.}
    }