A two‐domain protein triggers heat shock pathway and necrosis pathway both in model plant and nematode. (17th August 2015)
- Record Type:
- Journal Article
- Title:
- A two‐domain protein triggers heat shock pathway and necrosis pathway both in model plant and nematode. (17th August 2015)
- Main Title:
- A two‐domain protein triggers heat shock pathway and necrosis pathway both in model plant and nematode
- Authors:
- Ruan, Lifang
Wang, Huihui
Cai, Ge
Peng, Donghai
Zhou, Hua
Zheng, Jinshui
Zhu, Lei
Wang, Xixi
Yu, Haoquan
Li, Seng
Geng, Ce
Sun, Ming - Abstract:
- Summary: The entomopathogen B acillus thuringiensis is equipped with multiple virulent factors. The genome sequence of B . thuringiensis YBT1520 revealed the presence of a two‐domain protein named Nel which is composed of a necrosis‐inducing phytophthora protein 1‐like domain found in phytopathogens and a ricin B‐like lectin domain. The merging of two distantly related domains is relatively rare. Nel induced necrosis and pathogen‐triggered immunity (PTI) on model plants. The Nel also exhibited inhibition activity to nematode. Microscopic observation showed that the toxicity of Nel to nematodes targets the intestine. Quantitative proteomics revealed that Nel stimulated the host defence. The Nel thus possesses dual roles, as both toxin and elicitor. Remarkably, the Nel protein triggered a similar response, induction of the heat shock pathway and the necrosis pathway, in both model plants and nematodes. The unusual ability of Nel to function across kingdom suggests a highly conserved mechanism in eukaryotes that predates the divergence of plants and animal. It is also speculated that the two‐domain protein is the result of horizontal gene transfer (HGT) between phytopathogens and entomopathogens. Our results provide an example that HGT occurs between members of different species or even genera with lower frequency are particularly important for evolution of new bacterial pathogen lineages with new virulence. B acillus thuringiensis occupies the same ecological niches, plantSummary: The entomopathogen B acillus thuringiensis is equipped with multiple virulent factors. The genome sequence of B . thuringiensis YBT1520 revealed the presence of a two‐domain protein named Nel which is composed of a necrosis‐inducing phytophthora protein 1‐like domain found in phytopathogens and a ricin B‐like lectin domain. The merging of two distantly related domains is relatively rare. Nel induced necrosis and pathogen‐triggered immunity (PTI) on model plants. The Nel also exhibited inhibition activity to nematode. Microscopic observation showed that the toxicity of Nel to nematodes targets the intestine. Quantitative proteomics revealed that Nel stimulated the host defence. The Nel thus possesses dual roles, as both toxin and elicitor. Remarkably, the Nel protein triggered a similar response, induction of the heat shock pathway and the necrosis pathway, in both model plants and nematodes. The unusual ability of Nel to function across kingdom suggests a highly conserved mechanism in eukaryotes that predates the divergence of plants and animal. It is also speculated that the two‐domain protein is the result of horizontal gene transfer (HGT) between phytopathogens and entomopathogens. Our results provide an example that HGT occurs between members of different species or even genera with lower frequency are particularly important for evolution of new bacterial pathogen lineages with new virulence. B acillus thuringiensis occupies the same ecological niches, plant and soil, as phytopathogens, providing the opportunity for gene exchange. … (more)
- Is Part Of:
- Environmental microbiology. Volume 17:Number 11(2015:Nov.)
- Journal:
- Environmental microbiology
- Issue:
- Volume 17:Number 11(2015:Nov.)
- Issue Display:
- Volume 17, Issue 11 (2015)
- Year:
- 2015
- Volume:
- 17
- Issue:
- 11
- Issue Sort Value:
- 2015-0017-0011-0000
- Page Start:
- 4547
- Page End:
- 4565
- Publication Date:
- 2015-08-17
- Subjects:
- Microbial ecology -- Periodicals
Environmental Microbiology -- Periodicals
579.17 - Journal URLs:
- http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1462-2912;screen=info;ECOIP ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920/issues ↗
http://www.blackwell-synergy.com/member/institutions/issuelist.asp?journal=emi ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/1462-2920.12968 ↗
- Languages:
- English
- ISSNs:
- 1462-2912
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3791.522600
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British Library HMNTS - ELD Digital store - Ingest File:
- 262.xml