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Identification and Comparison of Receptor Binding Characteristics of the Spike Protein of Two Porcine Epidemic Diarrhea Virus Strains
Porcine epidemic diarrhea virus (PEDV), a member of Alphacoronavirus, has caused huge economic losses for the global pork industry recently. The spike (S) protein mediates PEDV entry into host cells. Herein, we investigated the interactions between the S protein and its receptor porcine aminopeptida...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810246/ https://www.ncbi.nlm.nih.gov/pubmed/26907329 http://dx.doi.org/10.3390/v8030055 |
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author | Deng, Feng Ye, Gang Liu, Qianqian Navid, Muhammad Tariq Zhong, Xiaoli Li, Youwen Wan, Chunyun Xiao, Shaobo He, Qigai Fu, Zhen F. Peng, Guiqing |
author_facet | Deng, Feng Ye, Gang Liu, Qianqian Navid, Muhammad Tariq Zhong, Xiaoli Li, Youwen Wan, Chunyun Xiao, Shaobo He, Qigai Fu, Zhen F. Peng, Guiqing |
author_sort | Deng, Feng |
collection | PubMed |
description | Porcine epidemic diarrhea virus (PEDV), a member of Alphacoronavirus, has caused huge economic losses for the global pork industry recently. The spike (S) protein mediates PEDV entry into host cells. Herein, we investigated the interactions between the S protein and its receptor porcine aminopeptidase N (pAPN) or co-receptor sugars. The C-terminal domain (CTD) of the S1 domain is bound to pAPN. The prototype strain demonstrated similar receptor-binding activity compared with the variant field isolate. Three loops at the tips of the β-barrel domains did not play crucial roles in the PEDV S-pAPN association, indicating that PEDV conforms to a different receptor recognition model compared with transmissible gastroenteritis virus (TGEV), porcine respiratory CoV (PRCV), and human coronavirus NL63 (HCoV-NL63). The N-terminal domain (NTD) of the PEDV S1 domain could bind sugar, a possible co-receptor for PEDV. The prototype strain exhibited weaker sugar-binding activity compared with the variant field isolate. Strategies targeting the receptor binding domain (RBD) may be helpful for developing vaccines or antiviral drugs for PEDV. Understanding the differences in receptor binding between the prototype and the variant strains may provide insight into PEDV pathogenesis. |
format | Online Article Text |
id | pubmed-4810246 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-48102462016-04-04 Identification and Comparison of Receptor Binding Characteristics of the Spike Protein of Two Porcine Epidemic Diarrhea Virus Strains Deng, Feng Ye, Gang Liu, Qianqian Navid, Muhammad Tariq Zhong, Xiaoli Li, Youwen Wan, Chunyun Xiao, Shaobo He, Qigai Fu, Zhen F. Peng, Guiqing Viruses Article Porcine epidemic diarrhea virus (PEDV), a member of Alphacoronavirus, has caused huge economic losses for the global pork industry recently. The spike (S) protein mediates PEDV entry into host cells. Herein, we investigated the interactions between the S protein and its receptor porcine aminopeptidase N (pAPN) or co-receptor sugars. The C-terminal domain (CTD) of the S1 domain is bound to pAPN. The prototype strain demonstrated similar receptor-binding activity compared with the variant field isolate. Three loops at the tips of the β-barrel domains did not play crucial roles in the PEDV S-pAPN association, indicating that PEDV conforms to a different receptor recognition model compared with transmissible gastroenteritis virus (TGEV), porcine respiratory CoV (PRCV), and human coronavirus NL63 (HCoV-NL63). The N-terminal domain (NTD) of the PEDV S1 domain could bind sugar, a possible co-receptor for PEDV. The prototype strain exhibited weaker sugar-binding activity compared with the variant field isolate. Strategies targeting the receptor binding domain (RBD) may be helpful for developing vaccines or antiviral drugs for PEDV. Understanding the differences in receptor binding between the prototype and the variant strains may provide insight into PEDV pathogenesis. MDPI 2016-02-23 /pmc/articles/PMC4810246/ /pubmed/26907329 http://dx.doi.org/10.3390/v8030055 Text en © 2016 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons by Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Deng, Feng Ye, Gang Liu, Qianqian Navid, Muhammad Tariq Zhong, Xiaoli Li, Youwen Wan, Chunyun Xiao, Shaobo He, Qigai Fu, Zhen F. Peng, Guiqing Identification and Comparison of Receptor Binding Characteristics of the Spike Protein of Two Porcine Epidemic Diarrhea Virus Strains |
title | Identification and Comparison of Receptor Binding Characteristics of the Spike Protein of Two Porcine Epidemic Diarrhea Virus Strains |
title_full | Identification and Comparison of Receptor Binding Characteristics of the Spike Protein of Two Porcine Epidemic Diarrhea Virus Strains |
title_fullStr | Identification and Comparison of Receptor Binding Characteristics of the Spike Protein of Two Porcine Epidemic Diarrhea Virus Strains |
title_full_unstemmed | Identification and Comparison of Receptor Binding Characteristics of the Spike Protein of Two Porcine Epidemic Diarrhea Virus Strains |
title_short | Identification and Comparison of Receptor Binding Characteristics of the Spike Protein of Two Porcine Epidemic Diarrhea Virus Strains |
title_sort | identification and comparison of receptor binding characteristics of the spike protein of two porcine epidemic diarrhea virus strains |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810246/ https://www.ncbi.nlm.nih.gov/pubmed/26907329 http://dx.doi.org/10.3390/v8030055 |
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