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The Pekin duck programmed death ligand-2: cDNA cloning, genomic structure, molecular characterization and expression analysis
Programmed death-1 (PD-1), upon engagement by its ligands, programmed death ligand-1 (PD-L1) and programmed death ligand-2 (PD-L2), provides signals that attenuate adaptive immune responses. Here we describe the identification of the Pekin duck PD-L2 (duPD-L2) and its gene structure. The duPD-L2 cDN...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5857182/ https://www.ncbi.nlm.nih.gov/pubmed/29556566 http://dx.doi.org/10.1016/j.bbrep.2018.01.008 |
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author | Yao, Qingxia Fischer, Karl P. Lorne Tyrrell, D. Gutfreund, Klaus S. |
author_facet | Yao, Qingxia Fischer, Karl P. Lorne Tyrrell, D. Gutfreund, Klaus S. |
author_sort | Yao, Qingxia |
collection | PubMed |
description | Programmed death-1 (PD-1), upon engagement by its ligands, programmed death ligand-1 (PD-L1) and programmed death ligand-2 (PD-L2), provides signals that attenuate adaptive immune responses. Here we describe the identification of the Pekin duck PD-L2 (duPD-L2) and its gene structure. The duPD-L2 cDNA encodes a 321 amino acid protein that has an amino acid identity of 76% and 35% with chicken and human PD-L2, respectively. Mapping of the duPD-L2 cDNA with duck genomic sequences revealed an exonic structure similar to that of the human Pdcd1lg2 gene. Homology modelling of the duPD-L2 protein was compatible with the murine PD-L2 ectodomain structure. Residues known to be important for PD-1 receptor binding of murine PD-L2 were mostly conserved in duPD-L2 within sheets A and G and partially conserved within sheets C and F. DuPD-L2 mRNA was constitutively expressed in all tissues examined with highest expression levels in lung, spleen, cloaca, bursa, cecal tonsil, duodenum and very low levels of expression in muscle, kidney and brain. Lipopolysaccharide treatment of adherent duck PBMC upregulated duPD-L2 mRNA expression. Our work shows evolutionary conservation of the PD-L2 ectodomain structure and residues important for PD-1 binding in vertebrates including fish. The information provided will be useful for further investigation of the role of duPD-L2 in the regulation of duck adaptive immunity and exploration of PD-1-targeted immunotherapies in the duck hepatitis B infection model. |
format | Online Article Text |
id | pubmed-5857182 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-58571822018-03-19 The Pekin duck programmed death ligand-2: cDNA cloning, genomic structure, molecular characterization and expression analysis Yao, Qingxia Fischer, Karl P. Lorne Tyrrell, D. Gutfreund, Klaus S. Biochem Biophys Rep Research Article Programmed death-1 (PD-1), upon engagement by its ligands, programmed death ligand-1 (PD-L1) and programmed death ligand-2 (PD-L2), provides signals that attenuate adaptive immune responses. Here we describe the identification of the Pekin duck PD-L2 (duPD-L2) and its gene structure. The duPD-L2 cDNA encodes a 321 amino acid protein that has an amino acid identity of 76% and 35% with chicken and human PD-L2, respectively. Mapping of the duPD-L2 cDNA with duck genomic sequences revealed an exonic structure similar to that of the human Pdcd1lg2 gene. Homology modelling of the duPD-L2 protein was compatible with the murine PD-L2 ectodomain structure. Residues known to be important for PD-1 receptor binding of murine PD-L2 were mostly conserved in duPD-L2 within sheets A and G and partially conserved within sheets C and F. DuPD-L2 mRNA was constitutively expressed in all tissues examined with highest expression levels in lung, spleen, cloaca, bursa, cecal tonsil, duodenum and very low levels of expression in muscle, kidney and brain. Lipopolysaccharide treatment of adherent duck PBMC upregulated duPD-L2 mRNA expression. Our work shows evolutionary conservation of the PD-L2 ectodomain structure and residues important for PD-1 binding in vertebrates including fish. The information provided will be useful for further investigation of the role of duPD-L2 in the regulation of duck adaptive immunity and exploration of PD-1-targeted immunotherapies in the duck hepatitis B infection model. Elsevier 2018-02-03 /pmc/articles/PMC5857182/ /pubmed/29556566 http://dx.doi.org/10.1016/j.bbrep.2018.01.008 Text en © 2018 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article Yao, Qingxia Fischer, Karl P. Lorne Tyrrell, D. Gutfreund, Klaus S. The Pekin duck programmed death ligand-2: cDNA cloning, genomic structure, molecular characterization and expression analysis |
title | The Pekin duck programmed death ligand-2: cDNA cloning, genomic structure, molecular characterization and expression analysis |
title_full | The Pekin duck programmed death ligand-2: cDNA cloning, genomic structure, molecular characterization and expression analysis |
title_fullStr | The Pekin duck programmed death ligand-2: cDNA cloning, genomic structure, molecular characterization and expression analysis |
title_full_unstemmed | The Pekin duck programmed death ligand-2: cDNA cloning, genomic structure, molecular characterization and expression analysis |
title_short | The Pekin duck programmed death ligand-2: cDNA cloning, genomic structure, molecular characterization and expression analysis |
title_sort | pekin duck programmed death ligand-2: cdna cloning, genomic structure, molecular characterization and expression analysis |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5857182/ https://www.ncbi.nlm.nih.gov/pubmed/29556566 http://dx.doi.org/10.1016/j.bbrep.2018.01.008 |
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