A Proteomic Analysis Provides Novel Insights into the Stress Responses of Caenorhabditis elegans towards Nematicidal Cry6A Toxin from Bacillus thuringiensis
Abstract Cry6A represents a novel family of nematicidal crystal proteins from Bacillus thuringiensis. It has distinctive architecture as well as mechanism of action from Cry5B, a highly focused family of nematicidal crystal proteins, and even from other insecticidal crystal proteins containing the c...
Main Authors: | , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2017-10-01
|
Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-017-14428-3 |
id |
doaj-1ce70033e9f241f789e6f363ae749a66 |
---|---|
record_format |
Article |
spelling |
doaj-1ce70033e9f241f789e6f363ae749a662020-12-08T00:13:27ZengNature Publishing GroupScientific Reports2045-23222017-10-017111410.1038/s41598-017-14428-3A Proteomic Analysis Provides Novel Insights into the Stress Responses of Caenorhabditis elegans towards Nematicidal Cry6A Toxin from Bacillus thuringiensisBing Wang0Haiwen Wang1Jing Xiong2Qiaoni Zhou3Huan Wu4Liqiu Xia5Lin Li6Ziquan Yu7State Key Laboratory of Developmental Biology of Freshwater Fish, College of Life Science, Hunan Normal UniversityState Key Laboratory of Developmental Biology of Freshwater Fish, College of Life Science, Hunan Normal UniversityState Key Laboratory of Developmental Biology of Freshwater Fish, College of Life Science, Hunan Normal UniversityState Key Laboratory of Developmental Biology of Freshwater Fish, College of Life Science, Hunan Normal UniversityState Key Laboratory of Developmental Biology of Freshwater Fish, College of Life Science, Hunan Normal UniversityState Key Laboratory of Developmental Biology of Freshwater Fish, College of Life Science, Hunan Normal UniversityState Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural UniversityState Key Laboratory of Developmental Biology of Freshwater Fish, College of Life Science, Hunan Normal UniversityAbstract Cry6A represents a novel family of nematicidal crystal proteins from Bacillus thuringiensis. It has distinctive architecture as well as mechanism of action from Cry5B, a highly focused family of nematicidal crystal proteins, and even from other insecticidal crystal proteins containing the conserved three-domain. However, how nematode defends against Cry6A toxin remains obscure. In this study, the global defense pattern of Caenorhabditis elegans against Cry6Aa2 toxin was investigated by proteomic analysis. In response to Cry6Aa2, 12 proteins with significantly altered abundances were observed from worms, participating in innate immune defense, insulin-like receptor (ILR) signaling pathway, energy metabolism, and muscle assembly. The differentially expressed proteins (DEPs) functioning in diverse biological processes suggest that a variety of defense responses participate in the stress responses of C. elegans to Cry6Aa2. The functional verifications of DEPs suggest that ILR signaling pathway, DIM-1, galectin LEC-6 all are the factors of defense responses to Cry6Aa2. Moreover, Cry6Aa2 also involves in accelerating the metabolic energy production which fulfills the energy demand for the immune responses. In brief, our findings illustrate the global pattern of defense responses of nematode against Cry6A for the first time, and provide a novel insight into the mechanism through which worms respond to Cry6A.https://doi.org/10.1038/s41598-017-14428-3 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Bing Wang Haiwen Wang Jing Xiong Qiaoni Zhou Huan Wu Liqiu Xia Lin Li Ziquan Yu |
spellingShingle |
Bing Wang Haiwen Wang Jing Xiong Qiaoni Zhou Huan Wu Liqiu Xia Lin Li Ziquan Yu A Proteomic Analysis Provides Novel Insights into the Stress Responses of Caenorhabditis elegans towards Nematicidal Cry6A Toxin from Bacillus thuringiensis Scientific Reports |
author_facet |
Bing Wang Haiwen Wang Jing Xiong Qiaoni Zhou Huan Wu Liqiu Xia Lin Li Ziquan Yu |
author_sort |
Bing Wang |
title |
A Proteomic Analysis Provides Novel Insights into the Stress Responses of Caenorhabditis elegans towards Nematicidal Cry6A Toxin from Bacillus thuringiensis |
title_short |
A Proteomic Analysis Provides Novel Insights into the Stress Responses of Caenorhabditis elegans towards Nematicidal Cry6A Toxin from Bacillus thuringiensis |
title_full |
A Proteomic Analysis Provides Novel Insights into the Stress Responses of Caenorhabditis elegans towards Nematicidal Cry6A Toxin from Bacillus thuringiensis |
title_fullStr |
A Proteomic Analysis Provides Novel Insights into the Stress Responses of Caenorhabditis elegans towards Nematicidal Cry6A Toxin from Bacillus thuringiensis |
title_full_unstemmed |
A Proteomic Analysis Provides Novel Insights into the Stress Responses of Caenorhabditis elegans towards Nematicidal Cry6A Toxin from Bacillus thuringiensis |
title_sort |
proteomic analysis provides novel insights into the stress responses of caenorhabditis elegans towards nematicidal cry6a toxin from bacillus thuringiensis |
publisher |
Nature Publishing Group |
series |
Scientific Reports |
issn |
2045-2322 |
publishDate |
2017-10-01 |
description |
Abstract Cry6A represents a novel family of nematicidal crystal proteins from Bacillus thuringiensis. It has distinctive architecture as well as mechanism of action from Cry5B, a highly focused family of nematicidal crystal proteins, and even from other insecticidal crystal proteins containing the conserved three-domain. However, how nematode defends against Cry6A toxin remains obscure. In this study, the global defense pattern of Caenorhabditis elegans against Cry6Aa2 toxin was investigated by proteomic analysis. In response to Cry6Aa2, 12 proteins with significantly altered abundances were observed from worms, participating in innate immune defense, insulin-like receptor (ILR) signaling pathway, energy metabolism, and muscle assembly. The differentially expressed proteins (DEPs) functioning in diverse biological processes suggest that a variety of defense responses participate in the stress responses of C. elegans to Cry6Aa2. The functional verifications of DEPs suggest that ILR signaling pathway, DIM-1, galectin LEC-6 all are the factors of defense responses to Cry6Aa2. Moreover, Cry6Aa2 also involves in accelerating the metabolic energy production which fulfills the energy demand for the immune responses. In brief, our findings illustrate the global pattern of defense responses of nematode against Cry6A for the first time, and provide a novel insight into the mechanism through which worms respond to Cry6A. |
url |
https://doi.org/10.1038/s41598-017-14428-3 |
work_keys_str_mv |
AT bingwang aproteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT haiwenwang aproteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT jingxiong aproteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT qiaonizhou aproteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT huanwu aproteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT liqiuxia aproteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT linli aproteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT ziquanyu aproteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT bingwang proteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT haiwenwang proteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT jingxiong proteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT qiaonizhou proteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT huanwu proteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT liqiuxia proteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT linli proteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis AT ziquanyu proteomicanalysisprovidesnovelinsightsintothestressresponsesofcaenorhabditiseleganstowardsnematicidalcry6atoxinfrombacillusthuringiensis |
_version_ |
1724396547624402944 |