PmLT, a C-type lectin specific to hepatopancreas is involved in the innate defense of the shrimp Penaeus monodon

A diverse class of proteins called lectins plays a major role in shrimp innate immunity. In this study, the cDNA encoding a C-type lectin of Penaeus monodon (PmLT) was cloned, and its potential role examined. Despite the low overall amino acid sequence identity with other animal lectins, PmLT includ...

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Veröffentlicht in:Journal of invertebrate pathology 2008-11, Vol.99 (3), p.332-341
Hauptverfasser: Hoi-Tung Ma, Tracy, Benzie, John A.H., He, Jian-Guo, Chan, Siu-Ming
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container_title Journal of invertebrate pathology
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creator Hoi-Tung Ma, Tracy
Benzie, John A.H.
He, Jian-Guo
Chan, Siu-Ming
description A diverse class of proteins called lectins plays a major role in shrimp innate immunity. In this study, the cDNA encoding a C-type lectin of Penaeus monodon (PmLT) was cloned, and its potential role examined. Despite the low overall amino acid sequence identity with other animal lectins, PmLT includes conserved carbohydrate recognition domains (CRDs) characteristic of animal C-type lectins. Unlike the other two P. monodon lectin-like proteins described to date that have one CRD, PmLT has two CRDs. The first CRD contains a QPD motif with specificity for binding galactose, while the second CRD contains a EPN motif for binding mannose. PmLT transcripts can be detected in the hepatopancreas but not in other tissues. Expression studies showed that PmLT mRNA transcript level decreased initially and then gradually increased after whole shrimp or hepatopancreas tissue fragments were treated with white spot syndrome virus (WSSV) extract but were not affected by bacteria. Using anti-rPmLT antibody, PmLT was detected only in the hepatopancreas specific F cells (Hpf). In vitro encapsulation assay showed that agarose beads coated with rPmLT were encapsulated by hemocytes indicating a role in innate immune response. In summary, PmLT is produced in the hepatopancreas and may act as a pattern recognition protein for viral pathogens and also activates the innate immune responses of the shrimp to bacteria. The dual-CRD structure of PmLT may assist the recognition of diverse pathogens.
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In this study, the cDNA encoding a C-type lectin of Penaeus monodon (PmLT) was cloned, and its potential role examined. Despite the low overall amino acid sequence identity with other animal lectins, PmLT includes conserved carbohydrate recognition domains (CRDs) characteristic of animal C-type lectins. Unlike the other two P. monodon lectin-like proteins described to date that have one CRD, PmLT has two CRDs. The first CRD contains a QPD motif with specificity for binding galactose, while the second CRD contains a EPN motif for binding mannose. PmLT transcripts can be detected in the hepatopancreas but not in other tissues. Expression studies showed that PmLT mRNA transcript level decreased initially and then gradually increased after whole shrimp or hepatopancreas tissue fragments were treated with white spot syndrome virus (WSSV) extract but were not affected by bacteria. Using anti-rPmLT antibody, PmLT was detected only in the hepatopancreas specific F cells (Hpf). In vitro encapsulation assay showed that agarose beads coated with rPmLT were encapsulated by hemocytes indicating a role in innate immune response. In summary, PmLT is produced in the hepatopancreas and may act as a pattern recognition protein for viral pathogens and also activates the innate immune responses of the shrimp to bacteria. The dual-CRD structure of PmLT may assist the recognition of diverse pathogens.</description><identifier>ISSN: 0022-2011</identifier><identifier>EISSN: 1096-0805</identifier><identifier>DOI: 10.1016/j.jip.2008.08.003</identifier><identifier>PMID: 18793643</identifier><identifier>CODEN: JIVPAZ</identifier><language>eng</language><publisher>Amsterdam: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animal aquaculture ; Animal productions ; Animals ; Base Sequence ; Biochemistry. Physiology. 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In this study, the cDNA encoding a C-type lectin of Penaeus monodon (PmLT) was cloned, and its potential role examined. Despite the low overall amino acid sequence identity with other animal lectins, PmLT includes conserved carbohydrate recognition domains (CRDs) characteristic of animal C-type lectins. Unlike the other two P. monodon lectin-like proteins described to date that have one CRD, PmLT has two CRDs. The first CRD contains a QPD motif with specificity for binding galactose, while the second CRD contains a EPN motif for binding mannose. PmLT transcripts can be detected in the hepatopancreas but not in other tissues. Expression studies showed that PmLT mRNA transcript level decreased initially and then gradually increased after whole shrimp or hepatopancreas tissue fragments were treated with white spot syndrome virus (WSSV) extract but were not affected by bacteria. Using anti-rPmLT antibody, PmLT was detected only in the hepatopancreas specific F cells (Hpf). 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In this study, the cDNA encoding a C-type lectin of Penaeus monodon (PmLT) was cloned, and its potential role examined. Despite the low overall amino acid sequence identity with other animal lectins, PmLT includes conserved carbohydrate recognition domains (CRDs) characteristic of animal C-type lectins. Unlike the other two P. monodon lectin-like proteins described to date that have one CRD, PmLT has two CRDs. The first CRD contains a QPD motif with specificity for binding galactose, while the second CRD contains a EPN motif for binding mannose. PmLT transcripts can be detected in the hepatopancreas but not in other tissues. Expression studies showed that PmLT mRNA transcript level decreased initially and then gradually increased after whole shrimp or hepatopancreas tissue fragments were treated with white spot syndrome virus (WSSV) extract but were not affected by bacteria. Using anti-rPmLT antibody, PmLT was detected only in the hepatopancreas specific F cells (Hpf). In vitro encapsulation assay showed that agarose beads coated with rPmLT were encapsulated by hemocytes indicating a role in innate immune response. In summary, PmLT is produced in the hepatopancreas and may act as a pattern recognition protein for viral pathogens and also activates the innate immune responses of the shrimp to bacteria. The dual-CRD structure of PmLT may assist the recognition of diverse pathogens.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><pmid>18793643</pmid><doi>10.1016/j.jip.2008.08.003</doi><tpages>10</tpages></addata></record>
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source MEDLINE; Elsevier ScienceDirect Journals
subjects Amino Acid Sequence
Animal aquaculture
Animal productions
Animals
Base Sequence
Biochemistry. Physiology. Immunology
Biological and medical sciences
C-type lectin
Carbohydrate recognition domain
Cloning, Molecular
Crustacea
DNA Virus Infections - immunology
DNA Virus Infections - metabolism
DNA Virus Infections - transmission
DNA, Complementary - genetics
DNA, Complementary - metabolism
Encapsulation
Fundamental and applied biological sciences. Psychology
Gene Expression
Gene Expression Profiling
Gram-Negative Bacteria - physiology
hepatopancreas
Hepatopancreas - metabolism
Hepatopancreas - microbiology
Host-Pathogen Interactions - physiology
immunity
Immunity, Innate - genetics
Immunity, Innate - immunology
Innate immunity
Invertebrate aquaculture
Invertebrates
Lectin
lectins
Lectins - immunology
Marine
molecular cloning
Molecular Sequence Data
Penaeidae - genetics
Penaeidae - immunology
Penaeus monodon
Phylogeny
Physiology. Development
Shrimp
White spot syndrome virus
White spot syndrome virus 1 - physiology
title PmLT, a C-type lectin specific to hepatopancreas is involved in the innate defense of the shrimp Penaeus monodon
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