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A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein
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| Zeitschriftentitel: | Insect Molecular Biology |
|---|---|
| Personen und Körperschaften: | , , , , , , , , |
| In: | Insect Molecular Biology, 28, 2019, 4, S. 578-590 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Zhou, X.‐S. Chen, C. Li, T.‐H. Tang, J.‐J. Zhu, B.‐J. Wei, G.‐Q. Qian, C. Liu, C.‐L. Wang, L. Zhou, X.‐S. Chen, C. Li, T.‐H. Tang, J.‐J. Zhu, B.‐J. Wei, G.‐Q. Qian, C. Liu, C.‐L. Wang, L. |
|---|---|
| author |
Zhou, X.‐S. Chen, C. Li, T.‐H. Tang, J.‐J. Zhu, B.‐J. Wei, G.‐Q. Qian, C. Liu, C.‐L. Wang, L. |
| spellingShingle |
Zhou, X.‐S. Chen, C. Li, T.‐H. Tang, J.‐J. Zhu, B.‐J. Wei, G.‐Q. Qian, C. Liu, C.‐L. Wang, L. Insect Molecular Biology A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein Insect Science Genetics Molecular Biology |
| author_sort |
zhou, x.‐s. |
| spelling |
Zhou, X.‐S. Chen, C. Li, T.‐H. Tang, J.‐J. Zhu, B.‐J. Wei, G.‐Q. Qian, C. Liu, C.‐L. Wang, L. 0962-1075 1365-2583 Wiley Insect Science Genetics Molecular Biology http://dx.doi.org/10.1111/imb.12573 <jats:title>Abstract</jats:title><jats:p>The <jats:italic>QM</jats:italic> gene that encodes for the ribosomal protein L10 was firstly identified from human tumour cells as a tumour suppressor. In this study, a <jats:italic>QM</jats:italic> gene was identified in silkworm <jats:italic>Bombyx mori</jats:italic> (<jats:italic>BmQM</jats:italic>) and its immunomodulatory function was explored. BmQM messenger RNA (mRNA) and protein were highly expressed in the silk gland and fat body, and expressed in all stages of silkworm growth. After challenged with four different microorganisms, the expression levels of <jats:italic>BmQM</jats:italic> mRNA in fat body or haemocytes were significantly upregulated compared with the control. After knock‐down of <jats:italic>BmQM</jats:italic> gene, the expressions of some immune genes (<jats:italic>PGRPS6</jats:italic>, <jats:italic>Gloverin0</jats:italic>, <jats:italic>Lysozyme</jats:italic> and <jats:italic>Moricin</jats:italic>) were affected, and the transcripts of <jats:italic>prophenoloxidase1</jats:italic> and <jats:italic>prophenoloxidase2</jats:italic> have different degrees of change. The phenoloxidase activity was significantly reduced when the purified recombinant BmQM protein was injected. Recombinant BmQM protein inhibited systemic melanization and suppressed prophenoloxidase activation stimulated by <jats:italic>Micrococcus luteus</jats:italic>, but it did not affect phenoloxidase activity. Far‐western blotting assays showed that the BmQM protein interacted with silkworm BmJun protein, which negatively regulates AP‐1 expression. Our results indicated that BmQM protein could affect some immune gene expression and negatively regulate the prophenoloxidase‐activating system, and it may play an important role in regulation of the innate immunity in insects.</jats:p> A QM protein from <i>Bombyx mori</i> negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein Insect Molecular Biology |
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| title |
A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_unstemmed |
A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_full |
A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_fullStr |
A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_full_unstemmed |
A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_short |
A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_sort |
a qm protein from <i>bombyx mori</i> negatively regulates prophenoloxidase activation and melanization by interacting with jun protein |
| topic |
Insect Science Genetics Molecular Biology |
| url |
http://dx.doi.org/10.1111/imb.12573 |
| publishDate |
2019 |
| physical |
578-590 |
| description |
<jats:title>Abstract</jats:title><jats:p>The <jats:italic>QM</jats:italic> gene that encodes for the ribosomal protein L10 was firstly identified from human tumour cells as a tumour suppressor. In this study, a <jats:italic>QM</jats:italic> gene was identified in silkworm <jats:italic>Bombyx mori</jats:italic> (<jats:italic>BmQM</jats:italic>) and its immunomodulatory function was explored. BmQM messenger RNA (mRNA) and protein were highly expressed in the silk gland and fat body, and expressed in all stages of silkworm growth. After challenged with four different microorganisms, the expression levels of <jats:italic>BmQM</jats:italic> mRNA in fat body or haemocytes were significantly upregulated compared with the control. After knock‐down of <jats:italic>BmQM</jats:italic> gene, the expressions of some immune genes (<jats:italic>PGRPS6</jats:italic>, <jats:italic>Gloverin0</jats:italic>, <jats:italic>Lysozyme</jats:italic> and <jats:italic>Moricin</jats:italic>) were affected, and the transcripts of <jats:italic>prophenoloxidase1</jats:italic> and <jats:italic>prophenoloxidase2</jats:italic> have different degrees of change. The phenoloxidase activity was significantly reduced when the purified recombinant BmQM protein was injected. Recombinant BmQM protein inhibited systemic melanization and suppressed prophenoloxidase activation stimulated by <jats:italic>Micrococcus luteus</jats:italic>, but it did not affect phenoloxidase activity. Far‐western blotting assays showed that the BmQM protein interacted with silkworm BmJun protein, which negatively regulates AP‐1 expression. Our results indicated that BmQM protein could affect some immune gene expression and negatively regulate the prophenoloxidase‐activating system, and it may play an important role in regulation of the innate immunity in insects.</jats:p> |
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| author | Zhou, X.‐S., Chen, C., Li, T.‐H., Tang, J.‐J., Zhu, B.‐J., Wei, G.‐Q., Qian, C., Liu, C.‐L., Wang, L. |
| author_facet | Zhou, X.‐S., Chen, C., Li, T.‐H., Tang, J.‐J., Zhu, B.‐J., Wei, G.‐Q., Qian, C., Liu, C.‐L., Wang, L., Zhou, X.‐S., Chen, C., Li, T.‐H., Tang, J.‐J., Zhu, B.‐J., Wei, G.‐Q., Qian, C., Liu, C.‐L., Wang, L. |
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| description | <jats:title>Abstract</jats:title><jats:p>The <jats:italic>QM</jats:italic> gene that encodes for the ribosomal protein L10 was firstly identified from human tumour cells as a tumour suppressor. In this study, a <jats:italic>QM</jats:italic> gene was identified in silkworm <jats:italic>Bombyx mori</jats:italic> (<jats:italic>BmQM</jats:italic>) and its immunomodulatory function was explored. BmQM messenger RNA (mRNA) and protein were highly expressed in the silk gland and fat body, and expressed in all stages of silkworm growth. After challenged with four different microorganisms, the expression levels of <jats:italic>BmQM</jats:italic> mRNA in fat body or haemocytes were significantly upregulated compared with the control. After knock‐down of <jats:italic>BmQM</jats:italic> gene, the expressions of some immune genes (<jats:italic>PGRPS6</jats:italic>, <jats:italic>Gloverin0</jats:italic>, <jats:italic>Lysozyme</jats:italic> and <jats:italic>Moricin</jats:italic>) were affected, and the transcripts of <jats:italic>prophenoloxidase1</jats:italic> and <jats:italic>prophenoloxidase2</jats:italic> have different degrees of change. The phenoloxidase activity was significantly reduced when the purified recombinant BmQM protein was injected. Recombinant BmQM protein inhibited systemic melanization and suppressed prophenoloxidase activation stimulated by <jats:italic>Micrococcus luteus</jats:italic>, but it did not affect phenoloxidase activity. Far‐western blotting assays showed that the BmQM protein interacted with silkworm BmJun protein, which negatively regulates AP‐1 expression. Our results indicated that BmQM protein could affect some immune gene expression and negatively regulate the prophenoloxidase‐activating system, and it may play an important role in regulation of the innate immunity in insects.</jats:p> |
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| imprint | Wiley, 2019 |
| imprint_str_mv | Wiley, 2019 |
| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14 |
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| physical | 578-590 |
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| series | Insect Molecular Biology |
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| spelling | Zhou, X.‐S. Chen, C. Li, T.‐H. Tang, J.‐J. Zhu, B.‐J. Wei, G.‐Q. Qian, C. Liu, C.‐L. Wang, L. 0962-1075 1365-2583 Wiley Insect Science Genetics Molecular Biology http://dx.doi.org/10.1111/imb.12573 <jats:title>Abstract</jats:title><jats:p>The <jats:italic>QM</jats:italic> gene that encodes for the ribosomal protein L10 was firstly identified from human tumour cells as a tumour suppressor. In this study, a <jats:italic>QM</jats:italic> gene was identified in silkworm <jats:italic>Bombyx mori</jats:italic> (<jats:italic>BmQM</jats:italic>) and its immunomodulatory function was explored. BmQM messenger RNA (mRNA) and protein were highly expressed in the silk gland and fat body, and expressed in all stages of silkworm growth. After challenged with four different microorganisms, the expression levels of <jats:italic>BmQM</jats:italic> mRNA in fat body or haemocytes were significantly upregulated compared with the control. After knock‐down of <jats:italic>BmQM</jats:italic> gene, the expressions of some immune genes (<jats:italic>PGRPS6</jats:italic>, <jats:italic>Gloverin0</jats:italic>, <jats:italic>Lysozyme</jats:italic> and <jats:italic>Moricin</jats:italic>) were affected, and the transcripts of <jats:italic>prophenoloxidase1</jats:italic> and <jats:italic>prophenoloxidase2</jats:italic> have different degrees of change. The phenoloxidase activity was significantly reduced when the purified recombinant BmQM protein was injected. Recombinant BmQM protein inhibited systemic melanization and suppressed prophenoloxidase activation stimulated by <jats:italic>Micrococcus luteus</jats:italic>, but it did not affect phenoloxidase activity. Far‐western blotting assays showed that the BmQM protein interacted with silkworm BmJun protein, which negatively regulates AP‐1 expression. Our results indicated that BmQM protein could affect some immune gene expression and negatively regulate the prophenoloxidase‐activating system, and it may play an important role in regulation of the innate immunity in insects.</jats:p> A QM protein from <i>Bombyx mori</i> negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein Insect Molecular Biology |
| spellingShingle | Zhou, X.‐S., Chen, C., Li, T.‐H., Tang, J.‐J., Zhu, B.‐J., Wei, G.‐Q., Qian, C., Liu, C.‐L., Wang, L., Insect Molecular Biology, A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein, Insect Science, Genetics, Molecular Biology |
| title | A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_full | A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_fullStr | A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_full_unstemmed | A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_short | A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| title_sort | a qm protein from <i>bombyx mori</i> negatively regulates prophenoloxidase activation and melanization by interacting with jun protein |
| title_unstemmed | A QM protein from Bombyx mori negatively regulates prophenoloxidase activation and melanization by interacting with Jun protein |
| topic | Insect Science, Genetics, Molecular Biology |
| url | http://dx.doi.org/10.1111/imb.12573 |