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New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina
BACKGROUND: Subtilisin-like serine proteases play an important role in pathogenic fungi during the penetration and colonization of their hosts. In this study, we perform an evolutionary analysis of the subtilisin-like serine protease genes of subphylum Pezizomycotina to find if there are similar pat...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848655/ https://www.ncbi.nlm.nih.gov/pubmed/20211028 http://dx.doi.org/10.1186/1471-2148-10-68 |
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author | Li, Juan Yu, Li Yang, Jinkui Dong, Linqian Tian, Baoyu Yu, Zefen Liang, Lianming Zhang, Ying Wang, Xu Zhang, Keqin |
author_facet | Li, Juan Yu, Li Yang, Jinkui Dong, Linqian Tian, Baoyu Yu, Zefen Liang, Lianming Zhang, Ying Wang, Xu Zhang, Keqin |
author_sort | Li, Juan |
collection | PubMed |
description | BACKGROUND: Subtilisin-like serine proteases play an important role in pathogenic fungi during the penetration and colonization of their hosts. In this study, we perform an evolutionary analysis of the subtilisin-like serine protease genes of subphylum Pezizomycotina to find if there are similar pathogenic mechanisms among the pathogenic fungi with different life styles, which utilize subtilisin-like serine proteases as virulence factors. Within Pezizomycotina, nematode-trapping fungi are unique because they capture soil nematodes using specialized trapping devices. Increasing evidence suggests subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles. Here we also conduct positive selection analysis on the subtilisin-like serine protease genes from nematode-trapping fungi. RESULTS: Phylogenetic analysis of 189 subtilisin-like serine protease genes from Pezizomycotina suggests five strongly-supported monophyletic clades. The subtilisin-like serine protease genes previously identified or presumed as endocellular proteases were clustered into one clade and diverged the earliest in the phylogeny. In addition, the cuticle-degrading protease genes from entomopathogenic and nematode-parasitic fungi were clustered together, indicating that they might have overlapping pathogenic mechanisms against insects and nematodes. Our experimental bioassays supported this conclusion. Interestingly, although they both function as cuticle-degrading proteases, the subtilisin-like serine protease genes from nematode-trapping fungi and nematode-parasitic fungi were not grouped together in the phylogenetic tree. Our evolutionary analysis revealed evidence for positive selection on the subtilisin-like serine protease genes of the nematode-trapping fungi. CONCLUSIONS: Our study provides new insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina. Pezizomycotina subtilisins most likely evolved from endocellular to extracellular proteases. The entomopathogenic and nematode-parasitic fungi likely share similar properties in parasitism. In addition, our data provided better understanding about the duplications and subsequent functional divergence of subtilisin-like serine protease genes in Pezizomycotina. The evidence of positive selection detected in the subtilisin-like serine protease genes of nematode-trapping fungi in the present study suggests that the subtilisin-like serine proteases may have played important roles during the evolution of pathogenicity of nematode-trapping fungi against nematodes. |
format | Text |
id | pubmed-2848655 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-28486552010-04-02 New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina Li, Juan Yu, Li Yang, Jinkui Dong, Linqian Tian, Baoyu Yu, Zefen Liang, Lianming Zhang, Ying Wang, Xu Zhang, Keqin BMC Evol Biol Research article BACKGROUND: Subtilisin-like serine proteases play an important role in pathogenic fungi during the penetration and colonization of their hosts. In this study, we perform an evolutionary analysis of the subtilisin-like serine protease genes of subphylum Pezizomycotina to find if there are similar pathogenic mechanisms among the pathogenic fungi with different life styles, which utilize subtilisin-like serine proteases as virulence factors. Within Pezizomycotina, nematode-trapping fungi are unique because they capture soil nematodes using specialized trapping devices. Increasing evidence suggests subtilisin-like serine proteases from nematode-trapping fungi are involved in the penetration and digestion of nematode cuticles. Here we also conduct positive selection analysis on the subtilisin-like serine protease genes from nematode-trapping fungi. RESULTS: Phylogenetic analysis of 189 subtilisin-like serine protease genes from Pezizomycotina suggests five strongly-supported monophyletic clades. The subtilisin-like serine protease genes previously identified or presumed as endocellular proteases were clustered into one clade and diverged the earliest in the phylogeny. In addition, the cuticle-degrading protease genes from entomopathogenic and nematode-parasitic fungi were clustered together, indicating that they might have overlapping pathogenic mechanisms against insects and nematodes. Our experimental bioassays supported this conclusion. Interestingly, although they both function as cuticle-degrading proteases, the subtilisin-like serine protease genes from nematode-trapping fungi and nematode-parasitic fungi were not grouped together in the phylogenetic tree. Our evolutionary analysis revealed evidence for positive selection on the subtilisin-like serine protease genes of the nematode-trapping fungi. CONCLUSIONS: Our study provides new insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina. Pezizomycotina subtilisins most likely evolved from endocellular to extracellular proteases. The entomopathogenic and nematode-parasitic fungi likely share similar properties in parasitism. In addition, our data provided better understanding about the duplications and subsequent functional divergence of subtilisin-like serine protease genes in Pezizomycotina. The evidence of positive selection detected in the subtilisin-like serine protease genes of nematode-trapping fungi in the present study suggests that the subtilisin-like serine proteases may have played important roles during the evolution of pathogenicity of nematode-trapping fungi against nematodes. BioMed Central 2010-03-09 /pmc/articles/PMC2848655/ /pubmed/20211028 http://dx.doi.org/10.1186/1471-2148-10-68 Text en Copyright ©2010 Li et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research article Li, Juan Yu, Li Yang, Jinkui Dong, Linqian Tian, Baoyu Yu, Zefen Liang, Lianming Zhang, Ying Wang, Xu Zhang, Keqin New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina |
title | New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina |
title_full | New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina |
title_fullStr | New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina |
title_full_unstemmed | New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina |
title_short | New insights into the evolution of subtilisin-like serine protease genes in Pezizomycotina |
title_sort | new insights into the evolution of subtilisin-like serine protease genes in pezizomycotina |
topic | Research article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2848655/ https://www.ncbi.nlm.nih.gov/pubmed/20211028 http://dx.doi.org/10.1186/1471-2148-10-68 |
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