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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...

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Autores principales: Deng, Feng, Ye, Gang, Liu, Qianqian, Navid, Muhammad Tariq, Zhong, Xiaoli, Li, Youwen, Wan, Chunyun, Xiao, Shaobo, He, Qigai, Fu, Zhen F., Peng, Guiqing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
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.
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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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