Caspase-3, a shrimp phosphorylated hemocytic protein is necessary to control YHV infection
Autor: | Sittiruk Roytrakul, Phattara-orn Havanapan, Kallaya Sritunyalucksana, Suparat Taengchaiyaphum, Chartchai Krittanai, Atchara Paemanee, Nuanwan Phungthanom |
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Rok vydání: | 2021 |
Předmět: |
0301 basic medicine
Hemocytes Caspase 3 Roniviridae Aquatic Science Biology Gene Expression Regulation Enzymologic Phosphorylation Process Serine 03 medical and health sciences Penaeidae Animals Environmental Chemistry Phosphoproteomics 04 agricultural and veterinary sciences General Medicine Molecular biology Shrimp 030104 developmental biology Phosphoprotein Host-Pathogen Interactions 040102 fisheries 0401 agriculture forestry and fisheries Immunohistochemistry Phosphorylation |
Zdroj: | Fish & Shellfish Immunology. 114:36-48 |
ISSN: | 1050-4648 |
DOI: | 10.1016/j.fsi.2021.04.007 |
Popis: | By using immunohistochemistry detection, yellow head virus (YHV) was found to replicate in granule-containing hemocytes including semi-granular hemocytes (SGC) and granular hemocytes (GC) during the early phase (24 h post injection) of YHV-infected shrimp. Higher signal of YHV infection was found in GC more than in SGC. Comparative phosphoproteomic profiles between YHV-infected and non-infected GC reveal a number of phosphoproteins with different expression levels. The phosphoprotein spot with later on identified as caspase-3 in YHV-infected GC is most interesting. Blocking caspase-3 function using a specific inhibitor (Ac-DEVD-CMK) demonstrated high replication of YHV and consequently, high shrimp mortality. The immunohistochemistry results confirmed the high viral load in shrimp that caspase-3 activity was blocked. Caspase-3 is regulated through a variety of posttranslational modifications, including phosphorylation. Analysis of phosphorylation sites of shrimp caspase-3 revealed phosphorylation sites at serine residue. Taken together, caspase-3 is a hemocytic protein isolated from shrimp granular hemocytes with a role in anti-YHV response and regulated through the phosphorylation process. |
Databáze: | OpenAIRE |
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