Characterization and function of a short peptidoglycan recognition protein from the Chinese oak silkworm, Antheraea pernyi
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- 英文论文题名：Characterization and function of a short peptidoglycan recognition protein from the Chinese oak silkworm, Antheraea pernyi
- 论文作者：Li-Shang Dai ; Cen Qian ; LeiWang ; Guo-Qing Wei ; Qiu-Ning Liu ; Yu Sun ; Cong-Fen Zhang ; Jun Li ; Dong-Ran Liu ; Bao-Jian Zhu ; Chao-Liang Liu
- 英文论文作者：Li-Shang Dai ; Cen Qian ; LeiWang ; Guo-Qing Wei ; Qiu-Ning Liu ; Yu Sun ; Cong-Fen Zhang ; Jun Li ; Dong-Ran Liu ; Bao-Jian Zhu ; Chao-Liang Liu ; College of Life Science ; Anhui Agricultural University
- 年：2016
- 作者机构：College of Life Science, Anhui Agricultural University;
- 英文论文关键词：Antheraea pernyi ; Peptidoglycan recognition protein ; Expression ; Immune response
- 会议召开时间：2016-07-01
- 会议录名称：第十二届家（柞）蚕遗传育种暨良种繁育学术研讨会论文集（摘要汇编）
- 语种：英文
- 分类号：S885.1
- 学会代码：ZGCU
- 会议名称：第十二届家（柞）蚕遗传育种暨良种繁育学术研讨会
- 会议地点：中国重庆
- 主办单位：中国蚕学会、国家蚕桑产业技术体系
- 学会名称：中国蚕学会
- 页数：1
- 文件大小：498k
- 原文格式：D
- 会议级别：全国
摘要
Peptidoglycan recognition proteins(PGRPs) are conserved proteins in animals from insects to mammals and play an important role in immune response by recognizing peptidoglycan on microbial surfaces. In this study, a PGRP gene from Antheraea pernyi, named Ap-PGRP-A, was isolated and characterized. Sequence analysis revealed that the full-length c DNA of Ap-PGRP-A was 961 bp, containing a 40 bp 5′-untranslated sequence, a 339 bp 3′-untranslated region and an open reading frame of 582 bp. This gene encoded a putative protein of 193 amino acid residues. Phylogenetic analysis indicated that Ap-PGRP-A had the closest protein sequence similarity to Antheraea mylitta PGRP. The recombinant protein was successfully expressed in Escherichia coli cells and a rabbit anti-Ap-PGRP-A antibody was also prepared. Real-time quantitative reverse transcription-PCR analysis showed that Ap-PGRP-A was extensively expressed in the fat body, midgut, hemocyte, malpighian tubule and epidermis of A. pernyi, especially in the fat body and midgut. The expression levels of Ap-PGRP-A were significantly up-regulated by three types of microorganisms, and Ap-PGRP-A expression was more sensitive in response to the Gram-negative bacterium E. coli than the Gram-positive bacterium Bacillus subtilis or the fungus Beauveria bassiana. These data indicate that Ap-PGRP-A may play a role in the innate immune responses of A. pernyi.
Peptidoglycan recognition proteins(PGRPs) are conserved proteins in animals from insects to mammals and play an important role in immune response by recognizing peptidoglycan on microbial surfaces. In this study, a PGRP gene from Antheraea pernyi, named Ap-PGRP-A, was isolated and characterized. Sequence analysis revealed that the full-length c DNA of Ap-PGRP-A was 961 bp, containing a 40 bp 5′-untranslated sequence, a 339 bp 3′-untranslated region and an open reading frame of 582 bp. This gene encoded a putative protein of 193 amino acid residues. Phylogenetic analysis indicated that Ap-PGRP-A had the closest protein sequence similarity to Antheraea mylitta PGRP. The recombinant protein was successfully expressed in Escherichia coli cells and a rabbit anti-Ap-PGRP-A antibody was also prepared. Real-time quantitative reverse transcription-PCR analysis showed that Ap-PGRP-A was extensively expressed in the fat body, midgut, hemocyte, malpighian tubule and epidermis of A. pernyi, especially in the fat body and midgut. The expression levels of Ap-PGRP-A were significantly up-regulated by three types of microorganisms, and Ap-PGRP-A expression was more sensitive in response to the Gram-negative bacterium E. coli than the Gram-positive bacterium Bacillus subtilis or the fungus Beauveria bassiana. These data indicate that Ap-PGRP-A may play a role in the innate immune responses of A. pernyi.
Peptidoglycan recognition proteins(PGRPs) are conserved proteins in animals from insects to mammals and play an important role in immune response by recognizing peptidoglycan on microbial surfaces. In this study, a PGRP gene from Antheraea pernyi, named Ap-PGRP-A, was isolated and characterized. Sequence analysis revealed that the full-length c DNA of Ap-PGRP-A was 961 bp, containing a 40 bp 5′-untranslated sequence, a 339 bp 3′-untranslated region and an open reading frame of 582 bp. This gene encoded a putative protein of 193 amino acid residues. Phylogenetic analysis indicated that Ap-PGRP-A had the closest protein sequence similarity to Antheraea mylitta PGRP. The recombinant protein was successfully expressed in Escherichia coli cells and a rabbit anti-Ap-PGRP-A antibody was also prepared. Real-time quantitative reverse transcription-PCR analysis showed that Ap-PGRP-A was extensively expressed in the fat body, midgut, hemocyte, malpighian tubule and epidermis of A. pernyi, especially in the fat body and midgut. The expression levels of Ap-PGRP-A were significantly up-regulated by three types of microorganisms, and Ap-PGRP-A expression was more sensitive in response to the Gram-negative bacterium E. coli than the Gram-positive bacterium Bacillus subtilis or the fungus Beauveria bassiana. These data indicate that Ap-PGRP-A may play a role in the innate immune responses of A. pernyi.
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