Title |
Molecular cloning, expression and adhesion analysis of silent slpB of Lactobacillus acidophilus NCFM
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Published in |
AMB Express, June 2018
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DOI | 10.1186/s13568-018-0631-2 |
Pubmed ID | |
Authors |
Yuxing Guo, Xiangyue Li, Yao Yang, Zhen Wu, Xiaoqun Zeng, Fawze Nadari, Daodong Pan |
Abstract |
The slpB gene of Lactobacillus acidophilus NCFM, which differs from the slpA gene and is silent under normal conditions, was successfully amplified and ligated to the corresponding available sites on a recombinant pET-28a vector. Then the pET-28a-slpB vector was transformed into Escherichia coli DH (DE3) and the fusion His-slpB protein was expressed by induction with 1 mM IPTG for 14 h at 37 °C. The resulting His-slpB protein (SB) had a relative molecular weight of 48 kDa. It was purified using a Ni-NTA column and was confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and western blot contrastive analysis. The slpA protein (SA) from L. acidophilus NCFM was extracted and purified. It had a relative molecular weight of 46 kDa. Circular dichroism measurements suggested that the two S-layer proteins had a high β-sheet content and a low α-helix structure content. In an adhesion experiment, SA displayed higher adhesive capability towards Caco-2 cells than did SB. The results suggest that these two S-layer proteins could have biotechnological applications. |
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