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Herpes B virus gD interaction with its human receptor – an in silico analysis approach

BACKGROUND: The glycoprotein D (gD) is essential for Herpes B virus (BV) entry into mammalian cells. Nectin-1, an HSV-1 gD receptor, is found to be the receptor which mediated BV induced cell-cell fusion, while HVEM does not mediate fusion by BV glycoprotein. However, the specific sequence and struc...

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Autores principales: Li, Lingke, Qiu, Zhengliang, Li, Yan, Liang, Feng, Ye, Huahu, Cai, Yongqin, Guo, Wanfeng, Yue, Junjie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4106229/
https://www.ncbi.nlm.nih.gov/pubmed/24902525
http://dx.doi.org/10.1186/1742-4682-11-27
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author Li, Lingke
Qiu, Zhengliang
Li, Yan
Liang, Feng
Ye, Huahu
Cai, Yongqin
Guo, Wanfeng
Li, Yan
Yue, Junjie
author_facet Li, Lingke
Qiu, Zhengliang
Li, Yan
Liang, Feng
Ye, Huahu
Cai, Yongqin
Guo, Wanfeng
Li, Yan
Yue, Junjie
author_sort Li, Lingke
collection PubMed
description BACKGROUND: The glycoprotein D (gD) is essential for Herpes B virus (BV) entry into mammalian cells. Nectin-1, an HSV-1 gD receptor, is found to be the receptor which mediated BV induced cell-cell fusion, while HVEM does not mediate fusion by BV glycoprotein. However, the specific sequence and structural requirements of the BV gD for the recognition of and binding to Nectin-1 are unknown. Moreover, the 3D structures of BV gD and the BV gD-receptor complex have not been determined. In this study, we propose a reliable model of the interaction of the BV gD with receptor using bioinformatics tools. RESULTS: The three-dimensional structures of two BV gD-receptor complexes were constructed using homology modelling and docking strategy. Based on the models of these complexes, the BV gD receptor interaction patterns were calculated. The results showed that the interface between the BV gD and nectin-1 molecule is not geometrically complementary. The computed molecular interactions indicated that two terminal extensions were the main region of BV gD that binds to nectin-1 and that hydrophobic contacts between the two molecules play key roles in their recognition and binding. The constructed BV gD-HVEM complex model showed that this complex had a lower shape complementarity value and a smaller interface area compared with the HSV-1 gD-HVEM complex, and the number of intermolecular interactions between BV gD-HVEM were fewer than that of HSV-1 gD-HVEM complex. These results could explain why HVEM does not function as a receptor for BV gD. CONCLUSION: In this study, we present structural model for the BV gD in a complex with its receptor. Some features predicted by this model can explain previously reported experimental data. This complex model may lead to a better understanding of the function of BV gD and its interaction with receptor and will improve our understanding of the activation of the BV fusion and entry process.
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spelling pubmed-41062292014-07-23 Herpes B virus gD interaction with its human receptor – an in silico analysis approach Li, Lingke Qiu, Zhengliang Li, Yan Liang, Feng Ye, Huahu Cai, Yongqin Guo, Wanfeng Li, Yan Yue, Junjie Theor Biol Med Model Research BACKGROUND: The glycoprotein D (gD) is essential for Herpes B virus (BV) entry into mammalian cells. Nectin-1, an HSV-1 gD receptor, is found to be the receptor which mediated BV induced cell-cell fusion, while HVEM does not mediate fusion by BV glycoprotein. However, the specific sequence and structural requirements of the BV gD for the recognition of and binding to Nectin-1 are unknown. Moreover, the 3D structures of BV gD and the BV gD-receptor complex have not been determined. In this study, we propose a reliable model of the interaction of the BV gD with receptor using bioinformatics tools. RESULTS: The three-dimensional structures of two BV gD-receptor complexes were constructed using homology modelling and docking strategy. Based on the models of these complexes, the BV gD receptor interaction patterns were calculated. The results showed that the interface between the BV gD and nectin-1 molecule is not geometrically complementary. The computed molecular interactions indicated that two terminal extensions were the main region of BV gD that binds to nectin-1 and that hydrophobic contacts between the two molecules play key roles in their recognition and binding. The constructed BV gD-HVEM complex model showed that this complex had a lower shape complementarity value and a smaller interface area compared with the HSV-1 gD-HVEM complex, and the number of intermolecular interactions between BV gD-HVEM were fewer than that of HSV-1 gD-HVEM complex. These results could explain why HVEM does not function as a receptor for BV gD. CONCLUSION: In this study, we present structural model for the BV gD in a complex with its receptor. Some features predicted by this model can explain previously reported experimental data. This complex model may lead to a better understanding of the function of BV gD and its interaction with receptor and will improve our understanding of the activation of the BV fusion and entry process. BioMed Central 2014-06-06 /pmc/articles/PMC4106229/ /pubmed/24902525 http://dx.doi.org/10.1186/1742-4682-11-27 Text en Copyright © 2014 Li et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/4.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research
Li, Lingke
Qiu, Zhengliang
Li, Yan
Liang, Feng
Ye, Huahu
Cai, Yongqin
Guo, Wanfeng
Li, Yan
Yue, Junjie
Herpes B virus gD interaction with its human receptor – an in silico analysis approach
title Herpes B virus gD interaction with its human receptor – an in silico analysis approach
title_full Herpes B virus gD interaction with its human receptor – an in silico analysis approach
title_fullStr Herpes B virus gD interaction with its human receptor – an in silico analysis approach
title_full_unstemmed Herpes B virus gD interaction with its human receptor – an in silico analysis approach
title_short Herpes B virus gD interaction with its human receptor – an in silico analysis approach
title_sort herpes b virus gd interaction with its human receptor – an in silico analysis approach
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4106229/
https://www.ncbi.nlm.nih.gov/pubmed/24902525
http://dx.doi.org/10.1186/1742-4682-11-27
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