Publication: Interaction study of a novel Macrobrachium rosenbergii effector caspase with B2 and capsid proteins of M.rosenbergii nodavirus reveals their roles in apoptosis
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Issued Date
2015
Resource Type
File Type
application/pdf
ISSN
10504648
Other identifier(s)
2-s2.0-84930204530
Rights Holder(s)
มหาวิทยาลัยศรีนครินทรวิโรฒ
Bibliographic Citation
Fish and Shellfish Immunology. Vol 45, No.2 (2015), p.534-542
Suggested Citation
Youngcharoen S., Senapin S., Lertwimol T., Longyant S., Sithigorngul P., Flegel T.W., Chaivisuthangkura P. Interaction study of a novel Macrobrachium rosenbergii effector caspase with B2 and capsid proteins of M.rosenbergii nodavirus reveals their roles in apoptosis. Fish and Shellfish Immunology. Vol 45, No.2 (2015), p.534-542. doi:10.1016/j.fsi.2015.05.009 Retrieved from: https://hdl.handle.net/20.500.14740/6114
Abstract
Apoptosis is an essential immune response to protect invertebrates from virus infected cells. In shrimp, virus infection has been reported to induce apoptosis. Macrobrachium rosenbergii (. Mr) was considered to be a disease-resistant host when compared to penaeid shrimps. Caspase-3 was classified as an executioner caspase which played a key role in virus-induced apoptosis. In this study, an effector caspase gene of M.rosenbergii (. Mrcasp) was cloned and characterized. The open reading frame (ORF) of Mrcasp was 957 nucleotide encoding 318 amino acid with a deduced molecular mass of 35.87kDa. RT-PCR analysis showed the presence of Mrcasp in all examined tissues. The phylogenetic tree indicated that Mrcasp was closely related with caspase 3 of shrimp. The functions of the Mrcasp, B2 and capsid proteins of M. rosenbergii nodavirus (. MrNV) were assayed in Sf-9 cells. The results showed that Mrcasp induce apoptotic morphology cells; however, capsid protein of MrNV could inhibit apoptotic cells whereas B2 could neither induce nor inhibit apoptotic cells by DAPI staining. The protein interaction between Mrcasp and viral MrNV structure revealed that Mrcasp did not bind to B2 or capsid protein whereas B2 and capsid proteins could bind directly to each other. This study reported a novel sequence of a full-length Mrcasp and its functional studies indicated that Mrcasp could induce apoptotic cells. Our data is the first report demonstrating the direct protein-protein interaction between capsid protein and B2 protein of MrNV. © 2015 Elsevier Ltd.
Subject(s)
Decapoda (Crustacea)
Invertebrata
Macrobrachium rosenbergii
Miridae
Nodaviridae
Penaeidae
Caspase
Complementary DNA
Fish protein
Virus protein
Amino acid sequence
Animal
Genetics
Metabolism
Molecular cloning
Molecular genetics
Nodaviridae
Nucleotide sequence
Palaemonidae
Phylogeny
Amino Acid Sequence
Animals
Base Sequence
Caspases
Cloning, Molecular
DNA, Complementary
Fish Proteins
Molecular Sequence Data
Nodaviridae
Palaemonidae
Phylogeny
Viral Proteins
Invertebrata
Macrobrachium rosenbergii
Miridae
Nodaviridae
Penaeidae
Caspase
Complementary DNA
Fish protein
Virus protein
Amino acid sequence
Animal
Genetics
Metabolism
Molecular cloning
Molecular genetics
Nodaviridae
Nucleotide sequence
Palaemonidae
Phylogeny
Amino Acid Sequence
Animals
Base Sequence
Caspases
Cloning, Molecular
DNA, Complementary
Fish Proteins
Molecular Sequence Data
Nodaviridae
Palaemonidae
Phylogeny
Viral Proteins