Proteomic Analysis of Larval Integument in a Dominant Obese Translucent (Obs) Silkworm Mutant

Lingyan Wang, Zhaoming Dong, Juan Wang, Yaru Yin, Huawei Liu, Wenbo Hu, Zhangchuan Peng, Chun Liu, Muwang Li, Yutaka Banno, Toru Shimada, Qingyou Xia, Ping Zhao

研究成果: ジャーナルへの寄稿記事

抄録

The dominant obese translucent (Obs) mutant of the silkworm (Bombyx mori) results in a short and stout larval body, translucent phenotype, and abnormal pigmentation in the integument. The Obs mutant also displays deficiency in ecdysis and metamorphosis. In the present study, to gain an understanding of multiple Obs phenotypes, we investigated the phenotypes of Obs and performed a comparative analysis of the larval integument proteomes of Obs and normal silkworms. The phenotypic analysis revealed that the Obs larvae were indeed short and fat, and that chitin and uric acid content were lower but melanin content was higher in the Obs mutant. Proteomic analysis revealed that 244 proteins were significantly differentially expressed between Obs and normal silkworms, some of which were involved in uric acid metabolism and melanin pigmentation. Twenty-six proteins were annotated as cuticular proteins, including RR motif-rich cuticular proteins (CPR), glycine-rich cuticular protein (CPG), hypothetical cuticular protein (CPH), cuticular protein analogous to peritrophins (CPAPs), and the chitin_bind_3 motif proteins, and accounted for over 84% of the abundance of the total significantly differentially expressed proteins. Moreover, 22 of the 26 cuticular proteins were downregulated in the Obs mutant. Comparative proteomic analysis suggested that the multiple phenotypes of the Obs mutant might be related to changes in the expression of proteins that participate in cuticular formation, uric acid metabolism, and melanin pigmentation. These results could lay a basis for further identification of the gene responsible for the Obs mutant. The data have been deposited to ProteomeXchange with identifier PXD010998.

元の言語英語
ジャーナルJournal of insect science (Online)
18
発行部数6
DOI
出版物ステータス出版済み - 11 1 2018

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silkworms
integument
proteomics
mutants
proteins
melanin
uric acid
pigmentation
phenotype
chitin
metabolism
ecdysis
Bombyx mori
proteome
metamorphosis
protein synthesis
larvae
lipids

All Science Journal Classification (ASJC) codes

  • Insect Science

これを引用

Proteomic Analysis of Larval Integument in a Dominant Obese Translucent (Obs) Silkworm Mutant. / Wang, Lingyan; Dong, Zhaoming; Wang, Juan; Yin, Yaru; Liu, Huawei; Hu, Wenbo; Peng, Zhangchuan; Liu, Chun; Li, Muwang; Banno, Yutaka; Shimada, Toru; Xia, Qingyou; Zhao, Ping.

:: Journal of insect science (Online), 巻 18, 番号 6, 01.11.2018.

研究成果: ジャーナルへの寄稿記事

Wang, L, Dong, Z, Wang, J, Yin, Y, Liu, H, Hu, W, Peng, Z, Liu, C, Li, M, Banno, Y, Shimada, T, Xia, Q & Zhao, P 2018, 'Proteomic Analysis of Larval Integument in a Dominant Obese Translucent (Obs) Silkworm Mutant', Journal of insect science (Online), 巻. 18, 番号 6. https://doi.org/10.1093/jisesa/iey098
Wang, Lingyan ; Dong, Zhaoming ; Wang, Juan ; Yin, Yaru ; Liu, Huawei ; Hu, Wenbo ; Peng, Zhangchuan ; Liu, Chun ; Li, Muwang ; Banno, Yutaka ; Shimada, Toru ; Xia, Qingyou ; Zhao, Ping. / Proteomic Analysis of Larval Integument in a Dominant Obese Translucent (Obs) Silkworm Mutant. :: Journal of insect science (Online). 2018 ; 巻 18, 番号 6.
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title = "Proteomic Analysis of Larval Integument in a Dominant Obese Translucent (Obs) Silkworm Mutant",
abstract = "The dominant obese translucent (Obs) mutant of the silkworm (Bombyx mori) results in a short and stout larval body, translucent phenotype, and abnormal pigmentation in the integument. The Obs mutant also displays deficiency in ecdysis and metamorphosis. In the present study, to gain an understanding of multiple Obs phenotypes, we investigated the phenotypes of Obs and performed a comparative analysis of the larval integument proteomes of Obs and normal silkworms. The phenotypic analysis revealed that the Obs larvae were indeed short and fat, and that chitin and uric acid content were lower but melanin content was higher in the Obs mutant. Proteomic analysis revealed that 244 proteins were significantly differentially expressed between Obs and normal silkworms, some of which were involved in uric acid metabolism and melanin pigmentation. Twenty-six proteins were annotated as cuticular proteins, including RR motif-rich cuticular proteins (CPR), glycine-rich cuticular protein (CPG), hypothetical cuticular protein (CPH), cuticular protein analogous to peritrophins (CPAPs), and the chitin_bind_3 motif proteins, and accounted for over 84{\%} of the abundance of the total significantly differentially expressed proteins. Moreover, 22 of the 26 cuticular proteins were downregulated in the Obs mutant. Comparative proteomic analysis suggested that the multiple phenotypes of the Obs mutant might be related to changes in the expression of proteins that participate in cuticular formation, uric acid metabolism, and melanin pigmentation. These results could lay a basis for further identification of the gene responsible for the Obs mutant. The data have been deposited to ProteomeXchange with identifier PXD010998.",
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AU - Wang, Lingyan

AU - Dong, Zhaoming

AU - Wang, Juan

AU - Yin, Yaru

AU - Liu, Huawei

AU - Hu, Wenbo

AU - Peng, Zhangchuan

AU - Liu, Chun

AU - Li, Muwang

AU - Banno, Yutaka

AU - Shimada, Toru

AU - Xia, Qingyou

AU - Zhao, Ping

PY - 2018/11/1

Y1 - 2018/11/1

N2 - The dominant obese translucent (Obs) mutant of the silkworm (Bombyx mori) results in a short and stout larval body, translucent phenotype, and abnormal pigmentation in the integument. The Obs mutant also displays deficiency in ecdysis and metamorphosis. In the present study, to gain an understanding of multiple Obs phenotypes, we investigated the phenotypes of Obs and performed a comparative analysis of the larval integument proteomes of Obs and normal silkworms. The phenotypic analysis revealed that the Obs larvae were indeed short and fat, and that chitin and uric acid content were lower but melanin content was higher in the Obs mutant. Proteomic analysis revealed that 244 proteins were significantly differentially expressed between Obs and normal silkworms, some of which were involved in uric acid metabolism and melanin pigmentation. Twenty-six proteins were annotated as cuticular proteins, including RR motif-rich cuticular proteins (CPR), glycine-rich cuticular protein (CPG), hypothetical cuticular protein (CPH), cuticular protein analogous to peritrophins (CPAPs), and the chitin_bind_3 motif proteins, and accounted for over 84% of the abundance of the total significantly differentially expressed proteins. Moreover, 22 of the 26 cuticular proteins were downregulated in the Obs mutant. Comparative proteomic analysis suggested that the multiple phenotypes of the Obs mutant might be related to changes in the expression of proteins that participate in cuticular formation, uric acid metabolism, and melanin pigmentation. These results could lay a basis for further identification of the gene responsible for the Obs mutant. The data have been deposited to ProteomeXchange with identifier PXD010998.

AB - The dominant obese translucent (Obs) mutant of the silkworm (Bombyx mori) results in a short and stout larval body, translucent phenotype, and abnormal pigmentation in the integument. The Obs mutant also displays deficiency in ecdysis and metamorphosis. In the present study, to gain an understanding of multiple Obs phenotypes, we investigated the phenotypes of Obs and performed a comparative analysis of the larval integument proteomes of Obs and normal silkworms. The phenotypic analysis revealed that the Obs larvae were indeed short and fat, and that chitin and uric acid content were lower but melanin content was higher in the Obs mutant. Proteomic analysis revealed that 244 proteins were significantly differentially expressed between Obs and normal silkworms, some of which were involved in uric acid metabolism and melanin pigmentation. Twenty-six proteins were annotated as cuticular proteins, including RR motif-rich cuticular proteins (CPR), glycine-rich cuticular protein (CPG), hypothetical cuticular protein (CPH), cuticular protein analogous to peritrophins (CPAPs), and the chitin_bind_3 motif proteins, and accounted for over 84% of the abundance of the total significantly differentially expressed proteins. Moreover, 22 of the 26 cuticular proteins were downregulated in the Obs mutant. Comparative proteomic analysis suggested that the multiple phenotypes of the Obs mutant might be related to changes in the expression of proteins that participate in cuticular formation, uric acid metabolism, and melanin pigmentation. These results could lay a basis for further identification of the gene responsible for the Obs mutant. The data have been deposited to ProteomeXchange with identifier PXD010998.

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