Identification and Molecular Characterization of a Serine Protease Inhibitor Gene in the Khapra Beetle Trogoderma granarium

Aslı Dağeri

Makale detayları

Identification and Molecular Characterization of a Serine Protease Inhibitor Gene in the Khapra Beetle Trogoderma granarium

Yazarlar:

Aslı Dağeri

Yayıncı:

Karyay Karadeniz Yayımcılık

Ana Başlıklar:

Moleküler Evrim | Genetik (Diğer)

Dergi:

Black Sea Journal of Engineering and Science Vol.7 Issue 5, pp.982-987

Belge Tipi:

Makale

Yayın Tarihi:

9/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001324908

pISSN:

2619-8991

Anahtar kelimeler:

Özet:

 Insect serine protease inhibitors ISPIs are essential for regulating various protease-mediated activities and play crucial roles in metabolism, metamorphosis, reproduction, and immunity. As a member of the ISPIs, serpins are recognized as the most essential protease inhibitor family in higher eukaryotes, encompassing a diverse array of biological functions. They are involved in the Toll pathway, the prophenoloxidase cascade, development, immunity, and reproduction in all insects. In this study, a serpin from the khapra beetle, Trogoderma granarium Everts Coleoptera: Dermestideae was identified and characterized using both transcriptomic and bioinformatics methodologies. The BGISEQ-500 platform was used to construct a cDNA library from T. granarium, which led to the identification and characterization of a novel Serine Protease Inhibitor gene TgSPI. Sequence analysis confirmed TgSPIs classification within the serine protease inhibitor SPI superfamily. It has conserved features, including a Reactive Center Loop RCL close to the C-terminal end, which is essential for protease inhibition. Phylogenetic analysis and 3D structure modeling of TgSPI were performed using MEGA6 software and the Phyre2 Protein Fold Recognition Server, respectively. The phylogenetic analysis positioned TgSPI within a cluster of coleopteran insect SPIs ISPIs, supporting its evolutionary lineage. Predicted tertiary structure modeling of TgSPI revealed similarity to conserpin in the latent state. This study provides foundational information on the evolutionary patterns and structural-functional aspects of TgSPI in the khapra beetle and highlights probable role of TgSPI as a promising target for further genetic and functional studies aimed at sustainable pest control strategies.

 Insect serine protease inhibitors ISPIs are essential for regulating various protease-mediated activities and play crucial roles in metabolism, metamorphosis, reproduction, and immunity. As a member of the ISPIs, serpins are recognized as the most essential protease inhibitor family in higher eukaryotes, encompassing a diverse array of biological functions. They are involved in the Toll pathway, the prophenoloxidase cascade, development, immunity, and reproduction in all insects. In this study, a serpin from the khapra beetle, Trogoderma granarium Everts Coleoptera: Dermestideae was identified and characterized using both transcriptomic and bioinformatics methodologies. The BGISEQ-500 platform was used to construct a cDNA library from T. granarium, which led to the identification and characterization of a novel Serine Protease Inhibitor gene TgSPI. Sequence analysis confirmed TgSPIs classification within the serine protease inhibitor SPI superfamily. It has conserved features, including a Reactive Center Loop RCL close to the C-terminal end, which is essential for protease inhibition. Phylogenetic analysis and 3D structure modeling of TgSPI were performed using MEGA6 software and the Phyre2 Protein Fold Recognition Server, respectively. The phylogenetic analysis positioned TgSPI within a cluster of coleopteran insect SPIs ISPIs, supporting its evolutionary lineage. Predicted tertiary structure modeling of TgSPI revealed similarity to conserpin in the latent state. This study provides foundational information on the evolutionary patterns and structural-functional aspects of TgSPI in the khapra beetle and highlights probable role of TgSPI as a promising target for further genetic and functional studies aimed at sustainable pest control strategies.

 Insect serine protease inhibitors ISPIs are essential for regulating various protease-mediated activities and play crucial roles in metabolism, metamorphosis, reproduction, and immunity. As a member of the ISPIs, serpins are recognized as the most essential protease inhibitor family in higher eukaryotes, encompassing a diverse array of biological functions. They are involved in the Toll pathway, the prophenoloxidase cascade, development, immunity, and reproduction in all insects. In this study, a serpin from the khapra beetle, Trogoderma granarium Everts Coleoptera: Dermestideae was identified and characterized using both transcriptomic and bioinformatics methodologies. The BGISEQ-500 platform was used to construct a cDNA library from T. granarium, which led to the identification and characterization of a novel Serine Protease Inhibitor gene TgSPI. Sequence analysis confirmed TgSPIs classification within the serine protease inhibitor SPI superfamily. It has conserved features, including a Reactive Center Loop RCL close to the C-terminal end, which is essential for protease inhibition. Phylogenetic analysis and 3D structure modeling of TgSPI were performed using MEGA6 software and the Phyre2 Protein Fold Recognition Server, respectively. The phylogenetic analysis positioned TgSPI within a cluster of coleopteran insect SPIs ISPIs, supporting its evolutionary lineage. Predicted tertiary structure modeling of TgSPI revealed similarity to conserpin in the latent state. This study provides foundational information on the evolutionary patterns and structural-functional aspects of TgSPI in the khapra beetle and highlights probable role of TgSPI as a promising target for further genetic and functional studies aimed at sustainable pest control strategies.

 Insect serine protease inhibitors ISPIs are essential for regulating various protease-mediated activities and play crucial roles in metabolism, metamorphosis, reproduction, and immunity. As a member of the ISPIs, serpins are recognized as the most essential protease inhibitor family in higher eukaryotes, encompassing a diverse array of biological functions. They are involved in the Toll pathway, the prophenoloxidase cascade, development, immunity, and reproduction in all insects. In this study, a serpin from the khapra beetle, Trogoderma granarium Everts Coleoptera: Dermestideae was identified and characterized using both transcriptomic and bioinformatics methodologies. The BGISEQ-500 platform was used to construct a cDNA library from T. granarium, which led to the identification and characterization of a novel Serine Protease Inhibitor gene TgSPI. Sequence analysis confirmed TgSPIs classification within the serine protease inhibitor SPI superfamily. It has conserved features, including a Reactive Center Loop RCL close to the C-terminal end, which is essential for protease inhibition. Phylogenetic analysis and 3D structure modeling of TgSPI were performed using MEGA6 software and the Phyre2 Protein Fold Recognition Server, respectively. The phylogenetic analysis positioned TgSPI within a cluster of coleopteran insect SPIs ISPIs, supporting its evolutionary lineage. Predicted tertiary structure modeling of TgSPI revealed similarity to conserpin in the latent state. This study provides foundational information on the evolutionary patterns and structural-functional aspects of TgSPI in the khapra beetle and highlights probable role of TgSPI as a promising target for further genetic and functional studies aimed at sustainable pest control strategies.

Makale detayları

Identification and Molecular Characterization of a Serine Protease Inhibitor Gene in the Khapra Beetle Trogoderma granarium

Yazarlar:

Aslı Dağeri

Yayıncı:

Karyay Karadeniz Yayımcılık

Ana Başlıklar:

Moleküler Evrim | Genetik (Diğer)

Dergi:

Black Sea Journal of Engineering and Science Vol.7 Issue 5, pp.982-987

Belge Tipi:

Makale

Yayın Tarihi:

9/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001324908

pISSN:

2619-8991

Gene characterization

Insect serine protease inhibitor

Khapra beetle

SerpinGene characterization

Insect serine protease inhibitor

Khapra beetle

Serpin

Sayı

Makale detayları

Yazarlar: Aslı Dağeri

Yayıncı: Karyay Karadeniz Yayımcılık

Ana Başlıklar: Moleküler Evrim | Genetik (Diğer)

Dergi: Black Sea Journal of Engineering and Science Vol.7 Issue 5, pp.982-987

Belge Tipi: Makale

Yayın Tarihi: 9/2024

Belge Dili: İngilizce

Document ID (Org No.): 2001324908

pISSN: 2619-8991

Sayı

Yazarlar:

Aslı Dağeri

Yayıncı:

Karyay Karadeniz Yayımcılık

Ana Başlıklar:

Moleküler Evrim | Genetik (Diğer)

Dergi:

Black Sea Journal of Engineering and Science Vol.7 Issue 5, pp.982-987

Belge Tipi:

Makale

Yayın Tarihi:

9/2024

Belge Dili:

İngilizce

Document ID (Org No.):

2001324908

pISSN:

2619-8991