Identification of a Bacillus Thuringiensis Cry8Ea3 to Xin-Binding Alkaline Phosphatase from Holotrichiaparallela

DOI

10.2991/bbe-17.2017.94How to use a DOI?

Keywords

Holotriciaparallela, Alkaline phosphatase, Ligand blot, qRT-PCR.

Abstract

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.

Copyright

© 2017, the Authors. Published by Atlantis Press.

Open Access

This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

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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  - Proceedings of the 2nd International Conference on Biomedical and Biological Engineering 2017 (BBE 2017)
PB  - Atlantis Press
SP  - 593
EP  - 600
SN  - 2468-5747
UR  - https://doi.org/10.2991/bbe-17.2017.94
DO  - 10.2991/bbe-17.2017.94
ID  - WANG2017/05
ER  -