Mannose-binding C-type lectin from Procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunity
Mannose-binding lectin (MBL), which is a member of the C-type lectin (CTL) family, plays crucial roles in non-self recognition and the clearance of invading microorganisms. In this study, an MBL (designated as PcMBL) was cloned and characterized from the crayfish Procambarus clarkii. PcMBL cDNA cons...
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| Format: | Article |
| Language: | English |
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Elsevier
2023-10-01
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| Series: | Aquaculture Reports |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2352513423002466 |
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| author | Ying Huang Ying Jiang Miao-miao Wang Min-yi Chen Huan-gen Chen Heng-yuan Chen Wen-jie Liu Xiao-rui Li Xiao-lei Han |
| author_facet | Ying Huang Ying Jiang Miao-miao Wang Min-yi Chen Huan-gen Chen Heng-yuan Chen Wen-jie Liu Xiao-rui Li Xiao-lei Han |
| author_sort | Ying Huang |
| collection | DOAJ |
| description | Mannose-binding lectin (MBL), which is a member of the C-type lectin (CTL) family, plays crucial roles in non-self recognition and the clearance of invading microorganisms. In this study, an MBL (designated as PcMBL) was cloned and characterized from the crayfish Procambarus clarkii. PcMBL cDNA consisted of 816 bp encoding a protein with 271 amino acid residues. The deduced PcMBL contained a signal peptide, three low-complexity regions, and a carbohydrate-recognition domain, as found in most CTLs. The mRNA encoding PcMBL was detected in all the examined tissues. PcMBL expression in hemocytes and intestines was significantly upregulated after stimulation with Vibrio parahaemolyticus and Staphylococcus aureus. RNA interference studies revealed that PcMBL silencing remarkably downregulated the transcription of five antimicrobial peptide genes, namely, Anti-lipopolysaccharide factor 1 (ALF-1), ALF-4, ALF-10, Crustin 1 (Crus-1), and Crus-4. Recombinant PcMBL protein was used for the functional analysis. The results showed that rPcMBL had the capacity to bind to all seven tested microorganisms and three carbohydrates. rPcMBL facilitated the clearance of V. parahaemolyticus and S. aureus and inhibited the formation of biofilms and growth of the two bacteria. In addition, rPcMBL could reduce the mortality of crayfish infected with V. parahaemolyticus or S. aureus. All these results suggest that PcMBL may be involved in immune recognition and pattern elimination in the innate immunity of P. clarkii. |
| first_indexed | 2024-03-11T22:31:59Z |
| format | Article |
| id | doaj.art-883f260794aa499c8e50fc6bbabe29ba |
| institution | Directory Open Access Journal |
| issn | 2352-5134 |
| language | English |
| last_indexed | 2024-03-11T22:31:59Z |
| publishDate | 2023-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Aquaculture Reports |
| spelling | doaj.art-883f260794aa499c8e50fc6bbabe29ba2023-09-23T05:11:24ZengElsevierAquaculture Reports2352-51342023-10-0132101707Mannose-binding C-type lectin from Procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunityYing Huang0Ying Jiang1Miao-miao Wang2Min-yi Chen3Huan-gen Chen4Heng-yuan Chen5Wen-jie Liu6Xiao-rui Li7Xiao-lei Han8Department of Marine Biology, College of Oceanography, Hohai University, 1 Xikang Road, Nanjing, Jiangsu 210098, ChinaChangshu Institute of Technology, 99 South Third Ring Road, Changshu, Jiangsu 215500, ChinaFisheries Technology Extension Center of Jiangsu Province, 302 Hanzhongmen Street, Nanjing, Jiangsu 210036, ChinaChangshu Institute of Technology, 99 South Third Ring Road, Changshu, Jiangsu 215500, ChinaFisheries Technology Extension Center of Jiangsu Province, 302 Hanzhongmen Street, Nanjing, Jiangsu 210036, ChinaChangshu Institute of Technology, 99 South Third Ring Road, Changshu, Jiangsu 215500, ChinaDepartment of Marine Biology, College of Oceanography, Hohai University, 1 Xikang Road, Nanjing, Jiangsu 210098, ChinaChangshu Institute of Technology, 99 South Third Ring Road, Changshu, Jiangsu 215500, ChinaChangshu Institute of Technology, 99 South Third Ring Road, Changshu, Jiangsu 215500, China; Corresponding author.Mannose-binding lectin (MBL), which is a member of the C-type lectin (CTL) family, plays crucial roles in non-self recognition and the clearance of invading microorganisms. In this study, an MBL (designated as PcMBL) was cloned and characterized from the crayfish Procambarus clarkii. PcMBL cDNA consisted of 816 bp encoding a protein with 271 amino acid residues. The deduced PcMBL contained a signal peptide, three low-complexity regions, and a carbohydrate-recognition domain, as found in most CTLs. The mRNA encoding PcMBL was detected in all the examined tissues. PcMBL expression in hemocytes and intestines was significantly upregulated after stimulation with Vibrio parahaemolyticus and Staphylococcus aureus. RNA interference studies revealed that PcMBL silencing remarkably downregulated the transcription of five antimicrobial peptide genes, namely, Anti-lipopolysaccharide factor 1 (ALF-1), ALF-4, ALF-10, Crustin 1 (Crus-1), and Crus-4. Recombinant PcMBL protein was used for the functional analysis. The results showed that rPcMBL had the capacity to bind to all seven tested microorganisms and three carbohydrates. rPcMBL facilitated the clearance of V. parahaemolyticus and S. aureus and inhibited the formation of biofilms and growth of the two bacteria. In addition, rPcMBL could reduce the mortality of crayfish infected with V. parahaemolyticus or S. aureus. All these results suggest that PcMBL may be involved in immune recognition and pattern elimination in the innate immunity of P. clarkii.http://www.sciencedirect.com/science/article/pii/S2352513423002466Procambarus clarkiiMannose-binding lectinAntimicrobial activityInnate immunity |
| spellingShingle | Ying Huang Ying Jiang Miao-miao Wang Min-yi Chen Huan-gen Chen Heng-yuan Chen Wen-jie Liu Xiao-rui Li Xiao-lei Han Mannose-binding C-type lectin from Procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunity Aquaculture Reports Procambarus clarkii Mannose-binding lectin Antimicrobial activity Innate immunity |
| title | Mannose-binding C-type lectin from Procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunity |
| title_full | Mannose-binding C-type lectin from Procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunity |
| title_fullStr | Mannose-binding C-type lectin from Procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunity |
| title_full_unstemmed | Mannose-binding C-type lectin from Procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunity |
| title_short | Mannose-binding C-type lectin from Procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunity |
| title_sort | mannose binding c type lectin from procambarus clarkii exhibited antimicrobial activity to mediate crayfish innate immunity |
| topic | Procambarus clarkii Mannose-binding lectin Antimicrobial activity Innate immunity |
| url | http://www.sciencedirect.com/science/article/pii/S2352513423002466 |
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