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Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus
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Zeitschriftentitel: | International Journal of Molecular Sciences |
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Personen und Körperschaften: | , , , , , , |
In: | International Journal of Molecular Sciences, 21, 2020, 3, S. 982 |
Format: | E-Article |
Sprache: | Englisch |
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MDPI AG
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author_facet |
Meng, Fanli Li, Yongxia Liu, Zhenkai Wang, Xuan Feng, Yuqian Zhang, Wei Zhang, Xingyao Meng, Fanli Li, Yongxia Liu, Zhenkai Wang, Xuan Feng, Yuqian Zhang, Wei Zhang, Xingyao |
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author |
Meng, Fanli Li, Yongxia Liu, Zhenkai Wang, Xuan Feng, Yuqian Zhang, Wei Zhang, Xingyao |
spellingShingle |
Meng, Fanli Li, Yongxia Liu, Zhenkai Wang, Xuan Feng, Yuqian Zhang, Wei Zhang, Xingyao International Journal of Molecular Sciences Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis |
author_sort |
meng, fanli |
spelling |
Meng, Fanli Li, Yongxia Liu, Zhenkai Wang, Xuan Feng, Yuqian Zhang, Wei Zhang, Xingyao 1422-0067 MDPI AG Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis http://dx.doi.org/10.3390/ijms21030982 <jats:p>Bursaphelenchus xylophilus is a nematode species that has damaged pine trees worldwide, but its pathogenesis has not been fully characterized. α-pinene helps protect host species during the early B. xylophilus infection and colonization stages. In this study, we identified potential molecular mimicry proteins based on a comparative transcriptomic analysis of B. xylophilus. The expression levels of three genes encoding secreted B. xylophilus proteins were influenced by α-pinene. We cloned one gene encoding a thaumatin-like protein, Bx-tlp-2 (accession number MK000287), and another gene encoding a cysteine proteinase inhibitor, Bx-cpi (accession number MK000288). Additionally, α-pinene appeared to induce Bx-tlp-1 expression, but had the opposite effect on Bx-cpi expression. An analysis of the expression of the potential molecular mimicry proteins in B. xylophilus infecting pine trees revealed that the α-pinene content was consistent with the expression levels of Bx-tlp-1 (Bx-cpi) and Pm-tlp (Pm-cpi) over time. Thus, these genes likely have important roles contributing to the infection of pine species by B. xylophilus. The results of this study may be relevant for future investigations of the functions of Bx-tlp-1, Bx-tlp-2 and Bx-cpi, which may provide a point to explore the relationship between B. xylophilus and host pines.</jats:p> Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus International Journal of Molecular Sciences |
doi_str_mv |
10.3390/ijms21030982 |
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Biologie Chemie und Pharmazie Physik Informatik |
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International Journal of Molecular Sciences |
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title |
Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_unstemmed |
Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_full |
Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_fullStr |
Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_full_unstemmed |
Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_short |
Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_sort |
potential molecular mimicry proteins responsive to α-pinene in bursaphelenchus xylophilus |
topic |
Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis |
url |
http://dx.doi.org/10.3390/ijms21030982 |
publishDate |
2020 |
physical |
982 |
description |
<jats:p>Bursaphelenchus xylophilus is a nematode species that has damaged pine trees worldwide, but its pathogenesis has not been fully characterized. α-pinene helps protect host species during the early B. xylophilus infection and colonization stages. In this study, we identified potential molecular mimicry proteins based on a comparative transcriptomic analysis of B. xylophilus. The expression levels of three genes encoding secreted B. xylophilus proteins were influenced by α-pinene. We cloned one gene encoding a thaumatin-like protein, Bx-tlp-2 (accession number MK000287), and another gene encoding a cysteine proteinase inhibitor, Bx-cpi (accession number MK000288). Additionally, α-pinene appeared to induce Bx-tlp-1 expression, but had the opposite effect on Bx-cpi expression. An analysis of the expression of the potential molecular mimicry proteins in B. xylophilus infecting pine trees revealed that the α-pinene content was consistent with the expression levels of Bx-tlp-1 (Bx-cpi) and Pm-tlp (Pm-cpi) over time. Thus, these genes likely have important roles contributing to the infection of pine species by B. xylophilus. The results of this study may be relevant for future investigations of the functions of Bx-tlp-1, Bx-tlp-2 and Bx-cpi, which may provide a point to explore the relationship between B. xylophilus and host pines.</jats:p> |
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author | Meng, Fanli, Li, Yongxia, Liu, Zhenkai, Wang, Xuan, Feng, Yuqian, Zhang, Wei, Zhang, Xingyao |
author_facet | Meng, Fanli, Li, Yongxia, Liu, Zhenkai, Wang, Xuan, Feng, Yuqian, Zhang, Wei, Zhang, Xingyao, Meng, Fanli, Li, Yongxia, Liu, Zhenkai, Wang, Xuan, Feng, Yuqian, Zhang, Wei, Zhang, Xingyao |
author_sort | meng, fanli |
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container_title | International Journal of Molecular Sciences |
container_volume | 21 |
description | <jats:p>Bursaphelenchus xylophilus is a nematode species that has damaged pine trees worldwide, but its pathogenesis has not been fully characterized. α-pinene helps protect host species during the early B. xylophilus infection and colonization stages. In this study, we identified potential molecular mimicry proteins based on a comparative transcriptomic analysis of B. xylophilus. The expression levels of three genes encoding secreted B. xylophilus proteins were influenced by α-pinene. We cloned one gene encoding a thaumatin-like protein, Bx-tlp-2 (accession number MK000287), and another gene encoding a cysteine proteinase inhibitor, Bx-cpi (accession number MK000288). Additionally, α-pinene appeared to induce Bx-tlp-1 expression, but had the opposite effect on Bx-cpi expression. An analysis of the expression of the potential molecular mimicry proteins in B. xylophilus infecting pine trees revealed that the α-pinene content was consistent with the expression levels of Bx-tlp-1 (Bx-cpi) and Pm-tlp (Pm-cpi) over time. Thus, these genes likely have important roles contributing to the infection of pine species by B. xylophilus. The results of this study may be relevant for future investigations of the functions of Bx-tlp-1, Bx-tlp-2 and Bx-cpi, which may provide a point to explore the relationship between B. xylophilus and host pines.</jats:p> |
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spelling | Meng, Fanli Li, Yongxia Liu, Zhenkai Wang, Xuan Feng, Yuqian Zhang, Wei Zhang, Xingyao 1422-0067 MDPI AG Inorganic Chemistry Organic Chemistry Physical and Theoretical Chemistry Computer Science Applications Spectroscopy Molecular Biology General Medicine Catalysis http://dx.doi.org/10.3390/ijms21030982 <jats:p>Bursaphelenchus xylophilus is a nematode species that has damaged pine trees worldwide, but its pathogenesis has not been fully characterized. α-pinene helps protect host species during the early B. xylophilus infection and colonization stages. In this study, we identified potential molecular mimicry proteins based on a comparative transcriptomic analysis of B. xylophilus. The expression levels of three genes encoding secreted B. xylophilus proteins were influenced by α-pinene. We cloned one gene encoding a thaumatin-like protein, Bx-tlp-2 (accession number MK000287), and another gene encoding a cysteine proteinase inhibitor, Bx-cpi (accession number MK000288). Additionally, α-pinene appeared to induce Bx-tlp-1 expression, but had the opposite effect on Bx-cpi expression. An analysis of the expression of the potential molecular mimicry proteins in B. xylophilus infecting pine trees revealed that the α-pinene content was consistent with the expression levels of Bx-tlp-1 (Bx-cpi) and Pm-tlp (Pm-cpi) over time. Thus, these genes likely have important roles contributing to the infection of pine species by B. xylophilus. The results of this study may be relevant for future investigations of the functions of Bx-tlp-1, Bx-tlp-2 and Bx-cpi, which may provide a point to explore the relationship between B. xylophilus and host pines.</jats:p> Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus International Journal of Molecular Sciences |
spellingShingle | Meng, Fanli, Li, Yongxia, Liu, Zhenkai, Wang, Xuan, Feng, Yuqian, Zhang, Wei, Zhang, Xingyao, International Journal of Molecular Sciences, Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus, Inorganic Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Computer Science Applications, Spectroscopy, Molecular Biology, General Medicine, Catalysis |
title | Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_full | Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_fullStr | Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_full_unstemmed | Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_short | Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
title_sort | potential molecular mimicry proteins responsive to α-pinene in bursaphelenchus xylophilus |
title_unstemmed | Potential Molecular Mimicry Proteins Responsive to α-pinene in Bursaphelenchus xylophilus |
topic | Inorganic Chemistry, Organic Chemistry, Physical and Theoretical Chemistry, Computer Science Applications, Spectroscopy, Molecular Biology, General Medicine, Catalysis |
url | http://dx.doi.org/10.3390/ijms21030982 |