Identification and characterization of two highly homologous lysozymes from red swamp crayfish, Procambarus clarkii
Lysozyme is an important immune effector in innate immunity against pathogen infection. But the study on the active region of lysozyme is limited. In this study, two highly homologous lysozymes were identified from crayfish (designated as PcLysi4 and PcLysi5). The molecular structures of PcLysi4 and...
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Elsevier
2021-12-01
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Series: | Fish and Shellfish Immunology Reports |
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author | Yin Cheng-Ming Li Ning-Qiu Ren Li-Chao Wang Zhe Chai Lian-Qin Lan Jiang-Feng |
author_facet | Yin Cheng-Ming Li Ning-Qiu Ren Li-Chao Wang Zhe Chai Lian-Qin Lan Jiang-Feng |
author_sort | Yin Cheng-Ming |
collection | DOAJ |
description | Lysozyme is an important immune effector in innate immunity against pathogen infection. But the study on the active region of lysozyme is limited. In this study, two highly homologous lysozymes were identified from crayfish (designated as PcLysi4 and PcLysi5). The molecular structures of PcLysi4 and PcLysi5 were predicted by SWISS-MODEL with the structure of lysozyme (PDB accession No. 4PJ2.2.B) as model. The results suggested that the structure of PcLysi4 and PcLysi5 were highly similar, but there were more α-helices at positions (127–139) and longer β-sheet at positions (49–57) in the structure of PcLysi5 than in that of PcLysi4. The antibacterial and antiviral functions of the two lysozymes were investigated. PcLysi4 and PcLysi5 could promote the bacterial clearance ability of crayfish, and increase the survival rate of Vibrio-infected crayfish. Further study showed that PcLysi5 inhibited WSSV replication, and enhanced the survival rate of WSSV-infected crayfish. There was no evidence that PcLysi4 has an influence on WSSV replication. Furthermore, PcLysi5 was detected to interact with envelope protein VP24 of WSSV. Our results would provide a new reference for the study on active region of lysozyme. |
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issn | 2667-0119 |
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last_indexed | 2024-12-20T16:11:22Z |
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series | Fish and Shellfish Immunology Reports |
spelling | doaj.art-704439e725e841738ba60203e23561bd2022-12-21T19:33:58ZengElsevierFish and Shellfish Immunology Reports2667-01192021-12-012100017Identification and characterization of two highly homologous lysozymes from red swamp crayfish, Procambarus clarkiiYin Cheng-Ming0Li Ning-Qiu1Ren Li-Chao2Wang Zhe3Chai Lian-Qin4Lan Jiang-Feng5Shandong Provincial Key Laboratory of Animal Biotechnology and Disease Control and Prevention, College of Animal Science and Veterinary Medicine, Shandong Agricultural University, Taian 271018, ChinaPearl River Fishery Research Institute, Chinese Academy of Fishery Sciences, Key Laboratory of Fishery Drug Development, Ministry of Agriculture, Key Laboratory of Aquatic Animal Immune Technology, Guangzhou 510380, ChinaShandong Provincial Key Laboratory of Animal Biotechnology and Disease Control and Prevention, College of Animal Science and Veterinary Medicine, Shandong Agricultural University, Taian 271018, ChinaState Key Laboratory of Cotton Biology, School of Life Sciences Henan University, Kaifeng 475004, ChinaState Key Laboratory of Cotton Biology, School of Life Sciences Henan University, Kaifeng 475004, China; School of Life Sciences Henan University, Kaifeng 475004, China.Shandong Provincial Key Laboratory of Animal Biotechnology and Disease Control and Prevention, College of Animal Science and Veterinary Medicine, Shandong Agricultural University, Taian 271018, China; Corresponding authors at: Shandong Agricultural University, Taian 271018, China.Lysozyme is an important immune effector in innate immunity against pathogen infection. But the study on the active region of lysozyme is limited. In this study, two highly homologous lysozymes were identified from crayfish (designated as PcLysi4 and PcLysi5). The molecular structures of PcLysi4 and PcLysi5 were predicted by SWISS-MODEL with the structure of lysozyme (PDB accession No. 4PJ2.2.B) as model. The results suggested that the structure of PcLysi4 and PcLysi5 were highly similar, but there were more α-helices at positions (127–139) and longer β-sheet at positions (49–57) in the structure of PcLysi5 than in that of PcLysi4. The antibacterial and antiviral functions of the two lysozymes were investigated. PcLysi4 and PcLysi5 could promote the bacterial clearance ability of crayfish, and increase the survival rate of Vibrio-infected crayfish. Further study showed that PcLysi5 inhibited WSSV replication, and enhanced the survival rate of WSSV-infected crayfish. There was no evidence that PcLysi4 has an influence on WSSV replication. Furthermore, PcLysi5 was detected to interact with envelope protein VP24 of WSSV. Our results would provide a new reference for the study on active region of lysozyme.http://www.sciencedirect.com/science/article/pii/S2667011921000128LysozymeWhite spot syndrome virusProcambarus clarkiiAntimicrobial peptides |
spellingShingle | Yin Cheng-Ming Li Ning-Qiu Ren Li-Chao Wang Zhe Chai Lian-Qin Lan Jiang-Feng Identification and characterization of two highly homologous lysozymes from red swamp crayfish, Procambarus clarkii Fish and Shellfish Immunology Reports Lysozyme White spot syndrome virus Procambarus clarkii Antimicrobial peptides |
title | Identification and characterization of two highly homologous lysozymes from red swamp crayfish, Procambarus clarkii |
title_full | Identification and characterization of two highly homologous lysozymes from red swamp crayfish, Procambarus clarkii |
title_fullStr | Identification and characterization of two highly homologous lysozymes from red swamp crayfish, Procambarus clarkii |
title_full_unstemmed | Identification and characterization of two highly homologous lysozymes from red swamp crayfish, Procambarus clarkii |
title_short | Identification and characterization of two highly homologous lysozymes from red swamp crayfish, Procambarus clarkii |
title_sort | identification and characterization of two highly homologous lysozymes from red swamp crayfish procambarus clarkii |
topic | Lysozyme White spot syndrome virus Procambarus clarkii Antimicrobial peptides |
url | http://www.sciencedirect.com/science/article/pii/S2667011921000128 |
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