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Analysis of the Binding Sites of Porcine Sialoadhesin Receptor with PRRSV

Porcine reproductive and respiratory syndrome virus (PRRSV) can infect pigs and cause enormous economic losses to the pig industry worldwide. Porcine sialoadhesin (pSN) and CD163 have been identified as key viral receptors on porcine alveolar macrophages (PAM), a main target cell infected by PRRSV....

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Autores principales: Jiang, Yibo, Khan, Faheem Ahmed, Pandupuspitasari, Nuruliarizki Shinta, Kadariya, Ishwari, Cheng, Zhangrui, Ren, Yuwei, Chen, Xing, Zhou, Ao, Yang, Liguo, Kong, Dexin, Zhang, Shujun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3876088/
https://www.ncbi.nlm.nih.gov/pubmed/24351868
http://dx.doi.org/10.3390/ijms141223955
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author Jiang, Yibo
Khan, Faheem Ahmed
Pandupuspitasari, Nuruliarizki Shinta
Kadariya, Ishwari
Cheng, Zhangrui
Ren, Yuwei
Chen, Xing
Zhou, Ao
Yang, Liguo
Kong, Dexin
Zhang, Shujun
author_facet Jiang, Yibo
Khan, Faheem Ahmed
Pandupuspitasari, Nuruliarizki Shinta
Kadariya, Ishwari
Cheng, Zhangrui
Ren, Yuwei
Chen, Xing
Zhou, Ao
Yang, Liguo
Kong, Dexin
Zhang, Shujun
author_sort Jiang, Yibo
collection PubMed
description Porcine reproductive and respiratory syndrome virus (PRRSV) can infect pigs and cause enormous economic losses to the pig industry worldwide. Porcine sialoadhesin (pSN) and CD163 have been identified as key viral receptors on porcine alveolar macrophages (PAM), a main target cell infected by PRRSV. In this study, the protein structures of amino acids 1–119 from the pSN and cSN (cattle sialoadhesin) N-termini (excluding the 19-amino acid signal peptide) were modeled via homology modeling based on mSN (mouse sialoadhesin) template structures using bioinformatics tools. Subsequently, pSN and cSN homology structures were superposed onto the mSN protein structure to predict the binding sites of pSN. As a validation experiment, the SN N-terminus (including the wild-type and site-directed-mutant-types of pSN and cSN) was cloned and expressed as a SN-GFP chimera protein. The binding activity between SN and PRRSV was confirmed by WB (Western blotting), FAR-WB (far Western blotting), ELISA (enzyme-linked immunosorbent assay) and immunofluorescence assay. We found that the S107 amino acid residue in the pSN N-terminal played a crucial role in forming a special cavity, as well as a hydrogen bond for enhancing PRRSV binding during PRRSV infection. S107 may be glycosylated during PRRSV infection and may also be involved in forming the cavity for binding PRRSV along with other sites, including W2, Y44, S45, R97, R105, W106 and V109. Additionally, S107 might also be important for pSN binding with PRRSV. However, the function of these binding sites must be confirmed by further studies.
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spelling pubmed-38760882013-12-31 Analysis of the Binding Sites of Porcine Sialoadhesin Receptor with PRRSV Jiang, Yibo Khan, Faheem Ahmed Pandupuspitasari, Nuruliarizki Shinta Kadariya, Ishwari Cheng, Zhangrui Ren, Yuwei Chen, Xing Zhou, Ao Yang, Liguo Kong, Dexin Zhang, Shujun Int J Mol Sci Article Porcine reproductive and respiratory syndrome virus (PRRSV) can infect pigs and cause enormous economic losses to the pig industry worldwide. Porcine sialoadhesin (pSN) and CD163 have been identified as key viral receptors on porcine alveolar macrophages (PAM), a main target cell infected by PRRSV. In this study, the protein structures of amino acids 1–119 from the pSN and cSN (cattle sialoadhesin) N-termini (excluding the 19-amino acid signal peptide) were modeled via homology modeling based on mSN (mouse sialoadhesin) template structures using bioinformatics tools. Subsequently, pSN and cSN homology structures were superposed onto the mSN protein structure to predict the binding sites of pSN. As a validation experiment, the SN N-terminus (including the wild-type and site-directed-mutant-types of pSN and cSN) was cloned and expressed as a SN-GFP chimera protein. The binding activity between SN and PRRSV was confirmed by WB (Western blotting), FAR-WB (far Western blotting), ELISA (enzyme-linked immunosorbent assay) and immunofluorescence assay. We found that the S107 amino acid residue in the pSN N-terminal played a crucial role in forming a special cavity, as well as a hydrogen bond for enhancing PRRSV binding during PRRSV infection. S107 may be glycosylated during PRRSV infection and may also be involved in forming the cavity for binding PRRSV along with other sites, including W2, Y44, S45, R97, R105, W106 and V109. Additionally, S107 might also be important for pSN binding with PRRSV. However, the function of these binding sites must be confirmed by further studies. Molecular Diversity Preservation International (MDPI) 2013-12-09 /pmc/articles/PMC3876088/ /pubmed/24351868 http://dx.doi.org/10.3390/ijms141223955 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Jiang, Yibo
Khan, Faheem Ahmed
Pandupuspitasari, Nuruliarizki Shinta
Kadariya, Ishwari
Cheng, Zhangrui
Ren, Yuwei
Chen, Xing
Zhou, Ao
Yang, Liguo
Kong, Dexin
Zhang, Shujun
Analysis of the Binding Sites of Porcine Sialoadhesin Receptor with PRRSV
title Analysis of the Binding Sites of Porcine Sialoadhesin Receptor with PRRSV
title_full Analysis of the Binding Sites of Porcine Sialoadhesin Receptor with PRRSV
title_fullStr Analysis of the Binding Sites of Porcine Sialoadhesin Receptor with PRRSV
title_full_unstemmed Analysis of the Binding Sites of Porcine Sialoadhesin Receptor with PRRSV
title_short Analysis of the Binding Sites of Porcine Sialoadhesin Receptor with PRRSV
title_sort analysis of the binding sites of porcine sialoadhesin receptor with prrsv
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3876088/
https://www.ncbi.nlm.nih.gov/pubmed/24351868
http://dx.doi.org/10.3390/ijms141223955
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