Identification of a Bacillus Thuringiensis Cry8Ea3 to Xin-Binding Alkaline Phosphatase from Holotrichiaparallela
- Wei WANG, Dan ZHAO, Wei GUO, Xiao-ping YAN, Ya-kun ZHANG, Kun-li ZHAO, Yu-jie GAO, Xiao-yun WANG
- Corresponding Author
- Wei WANG
Available Online May 2017.
- https://doi.org/10.2991/bbe-17.2017.94How to use a DOI?
- Holotriciaparallela, Alkaline phosphatase, Ligand blot, qRT-PCR.
- In order to further study the Insecticidal Mechanism of Bt protein against Holotricia parallela. In the study, According to the results of midgut transcriptome sequencing and RACE-PCR, the full-length hpalp gene was cloned. Sequencing analysis showed that the open reading frame of hpalp (GenBank accession NO. KY922835) was 1605 bp long, encoding 534 amino acid residues. The predicted molecular weight and isoelectric point of HpALP were 59 kDa and 5.18, respectively. Analysis of HpALP signal peptide with 21 amino acids, GPI anchor point is located in the C-terminal D514, and has two N-glycosylation sites: N100, N296. The results of Ligand blot showed that the binding of HpALP with Cry8Ea3 toxin. Transcriptional analysis of hpalp in different tissues of H. parallela larvae was performed by qRT-PCR, which revealed that the hpalp was primarly expressed higher in midgut, but lower in the foregut.
- Open Access
- This is an open access article distributed under the CC BY-NC license.
Cite this article
TY - CONF AU - Wei WANG AU - Dan ZHAO AU - Wei GUO AU - Xiao-ping YAN AU - Ya-kun ZHANG AU - Kun-li ZHAO AU - Yu-jie GAO AU - Xiao-yun WANG PY - 2017/05 DA - 2017/05 TI - Identification of a Bacillus Thuringiensis Cry8Ea3 to Xin-Binding Alkaline Phosphatase from Holotrichiaparallela BT - 2nd International Conference on Biomedical and Biological Engineering 2017 (BBE 2017) PB - Atlantis Press SN - 2468-5747 UR - https://doi.org/10.2991/bbe-17.2017.94 DO - https://doi.org/10.2991/bbe-17.2017.94 ID - WANG2017/05 ER -