The novel peptide NbPPI1 identified from Nicotiana benthamiana triggers immune responses and enhances resistance against Phytophthora pathogens.
Identifieur interne : 000025 ( Main/Exploration ); précédent : 000024; suivant : 000026The novel peptide NbPPI1 identified from Nicotiana benthamiana triggers immune responses and enhances resistance against Phytophthora pathogens.
Auteurs : Qujiang Wen [République populaire de Chine] ; Manli Sun [République populaire de Chine] ; Xianglan Kong [République populaire de Chine] ; Yang Yang [République populaire de Chine] ; Qiang Zhang [République populaire de Chine] ; Guiyan Huang [République populaire de Chine] ; Wenqin Lu [République populaire de Chine] ; Wanyue Li [République populaire de Chine] ; Yuling Meng [République populaire de Chine] ; Weixing Shan [République populaire de Chine]Source :
- Journal of integrative plant biology [ 1744-7909 ] ; 2020.
Abstract
In plants, recognition of small secreted peptides, such as damage/danger-associated molecular patterns (DAMPs), regulates diverse processes, including stress and immune responses. Here, we identified an SGPS (Ser-Gly-Pro-Ser) motif-containing peptide, Nicotiana tabacum NtPROPPI, and its two homologs in Nicotiana benthamiana, NbPROPPI1 and NbPROPPI2. Phytophthora parasitica infection and salicylic acid (SA) treatment induced NbPROPPI1/2 expression. Moreover, SignalP predicted that the 89-amino acid NtPROPPI includes a 24-amino acid N-terminal signal peptide and NbPROPPI1/2-GFP fusion proteins were mainly localized to the periplasm. Transient expression of NbPROPPI1/2 inhibited P. parasitica colonization, and NbPROPPI1/2 knockdown rendered plants more susceptible to P. parasitica. An eight-amino-acid segment in the NbPROPPI1 C-terminus was essential for its immune function and a synthetic 20-residue peptide, NbPPI1, derived from the C-terminus of NbPROPPI1 provoked significant immune responses in N. benthamiana. These responses led to enhanced accumulation of reactive oxygen species, activation of mitogen-activated protein kinases, and up-regulation of the defense genes Flg22-induced receptor-like kinase (FRK) and WRKY DNA-binding protein 33 (WRKY33). The NbPPI1-induced defense responses require Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1). These results suggest that NbPPI1 functions as a DAMP in N. benthamiana; this novel DAMP provides a potentially useful target for improving resistance to P. parasitica. This article is protected by copyright. All rights reserved.
DOI: 10.1111/jipb.13033
PubMed: 33205861
Affiliations:
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<front><div type="abstract" xml:lang="en">In plants, recognition of small secreted peptides, such as damage/danger-associated molecular patterns (DAMPs), regulates diverse processes, including stress and immune responses. Here, we identified an SGPS (Ser-Gly-Pro-Ser) motif-containing peptide, Nicotiana tabacum NtPROPPI, and its two homologs in Nicotiana benthamiana, NbPROPPI1 and NbPROPPI2. Phytophthora parasitica infection and salicylic acid (SA) treatment induced NbPROPPI1/2 expression. Moreover, SignalP predicted that the 89-amino acid NtPROPPI includes a 24-amino acid N-terminal signal peptide and NbPROPPI1/2-GFP fusion proteins were mainly localized to the periplasm. Transient expression of NbPROPPI1/2 inhibited P. parasitica colonization, and NbPROPPI1/2 knockdown rendered plants more susceptible to P. parasitica. An eight-amino-acid segment in the NbPROPPI1 C-terminus was essential for its immune function and a synthetic 20-residue peptide, NbPPI1, derived from the C-terminus of NbPROPPI1 provoked significant immune responses in N. benthamiana. These responses led to enhanced accumulation of reactive oxygen species, activation of mitogen-activated protein kinases, and up-regulation of the defense genes Flg22-induced receptor-like kinase (FRK) and WRKY DNA-binding protein 33 (WRKY33). The NbPPI1-induced defense responses require Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1). These results suggest that NbPPI1 functions as a DAMP in N. benthamiana; this novel DAMP provides a potentially useful target for improving resistance to P. parasitica. This article is protected by copyright. All rights reserved.</div>
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<Abstract><AbstractText>In plants, recognition of small secreted peptides, such as damage/danger-associated molecular patterns (DAMPs), regulates diverse processes, including stress and immune responses. Here, we identified an SGPS (Ser-Gly-Pro-Ser) motif-containing peptide, Nicotiana tabacum NtPROPPI, and its two homologs in Nicotiana benthamiana, NbPROPPI1 and NbPROPPI2. Phytophthora parasitica infection and salicylic acid (SA) treatment induced NbPROPPI1/2 expression. Moreover, SignalP predicted that the 89-amino acid NtPROPPI includes a 24-amino acid N-terminal signal peptide and NbPROPPI1/2-GFP fusion proteins were mainly localized to the periplasm. Transient expression of NbPROPPI1/2 inhibited P. parasitica colonization, and NbPROPPI1/2 knockdown rendered plants more susceptible to P. parasitica. An eight-amino-acid segment in the NbPROPPI1 C-terminus was essential for its immune function and a synthetic 20-residue peptide, NbPPI1, derived from the C-terminus of NbPROPPI1 provoked significant immune responses in N. benthamiana. These responses led to enhanced accumulation of reactive oxygen species, activation of mitogen-activated protein kinases, and up-regulation of the defense genes Flg22-induced receptor-like kinase (FRK) and WRKY DNA-binding protein 33 (WRKY33). The NbPPI1-induced defense responses require Brassinosteroid insensitive 1-associated receptor kinase 1 (BAK1). These results suggest that NbPPI1 functions as a DAMP in N. benthamiana; this novel DAMP provides a potentially useful target for improving resistance to P. parasitica. This article is protected by copyright. All rights reserved.</AbstractText>
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<tree><country name="République populaire de Chine"><noRegion><name sortKey="Wen, Qujiang" sort="Wen, Qujiang" uniqKey="Wen Q" first="Qujiang" last="Wen">Qujiang Wen</name>
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<name sortKey="Huang, Guiyan" sort="Huang, Guiyan" uniqKey="Huang G" first="Guiyan" last="Huang">Guiyan Huang</name>
<name sortKey="Kong, Xianglan" sort="Kong, Xianglan" uniqKey="Kong X" first="Xianglan" last="Kong">Xianglan Kong</name>
<name sortKey="Li, Wanyue" sort="Li, Wanyue" uniqKey="Li W" first="Wanyue" last="Li">Wanyue Li</name>
<name sortKey="Lu, Wenqin" sort="Lu, Wenqin" uniqKey="Lu W" first="Wenqin" last="Lu">Wenqin Lu</name>
<name sortKey="Meng, Yuling" sort="Meng, Yuling" uniqKey="Meng Y" first="Yuling" last="Meng">Yuling Meng</name>
<name sortKey="Shan, Weixing" sort="Shan, Weixing" uniqKey="Shan W" first="Weixing" last="Shan">Weixing Shan</name>
<name sortKey="Sun, Manli" sort="Sun, Manli" uniqKey="Sun M" first="Manli" last="Sun">Manli Sun</name>
<name sortKey="Yang, Yang" sort="Yang, Yang" uniqKey="Yang Y" first="Yang" last="Yang">Yang Yang</name>
<name sortKey="Zhang, Qiang" sort="Zhang, Qiang" uniqKey="Zhang Q" first="Qiang" last="Zhang">Qiang Zhang</name>
</country>
</tree>
</affiliations>
</record>
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