TY  - JOUR
T1  - Expression of the B Subunit of <I>Escherichia coli</I> Heat-Labile Enterotoxin in Transformed <I>Bombyx mori</I> BmN Cells
AU - Cao, Jin-Ru AU - Weng, Hong-Biao AU - Gong, Cheng-Liang AU - Ye, Ai-Hong AU - Zhou, Wen-Lin AU - He, Li-Hua AU - Xue, Ren-Yu AU - Cao, Guang-Li AU - Wang, Yong-Qiang 
JO  - Journal of Animal and Veterinary Advances
VL  - 11
IS  - 20
SP  - 3785
EP  - 3791
PY  - 2012
DA  - 2001/08/19
SN  - 1680-5593
DO  - javaa.2012.3785.3791
UR  - https://makhillpublications.co/view-article.php?doi=javaa.2012.3785.3791
KW  - Escherichia coli heat-labile enterotoxin
KW  -piggyBac transposon
KW  -Bombyx mori
KW  -BmN cell
KW  -genetic transformation
AB  - 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.
ER  -