Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain

Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) is an infectious virus that was first reported in 2012. The MERS-CoV genome encodes four major structural proteins, among which the spike (S) protein has a key role in viral infection and pathogenesis. The receptor-binding domain (RBD) o...

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Main Authors: Yusen Zhou, Yang Yang, Jingwei Huang, Shibo Jiang, Lanying Du
Format: Article
Language:English
Published: MDPI AG 2019-01-01
Series:Viruses
Subjects:
Online Access:http://www.mdpi.com/1999-4915/11/1/60
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spelling doaj-eb262522cd344bb08c7ae12791cb3f432020-11-25T01:28:59ZengMDPI AGViruses1999-49152019-01-011116010.3390/v11010060v11010060Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding DomainYusen Zhou0Yang Yang1Jingwei Huang2Shibo Jiang3Lanying Du4State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, ChinaDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USALindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USALindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USALindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10065, USAMiddle East respiratory syndrome (MERS) coronavirus (MERS-CoV) is an infectious virus that was first reported in 2012. The MERS-CoV genome encodes four major structural proteins, among which the spike (S) protein has a key role in viral infection and pathogenesis. The receptor-binding domain (RBD) of the S protein contains a critical neutralizing domain and is an important target for development of MERS vaccines and therapeutics. In this review, we describe the relevant features of the MERS-CoV S-protein RBD, summarize recent advances in the development of MERS-CoV RBD-based vaccines and therapeutic antibodies, and illustrate potential challenges and strategies to further improve their efficacy.http://www.mdpi.com/1999-4915/11/1/60CoronavirusMERS-CoVspike proteinreceptor-binding domainvaccinestherapeutics
collection DOAJ
language English
format Article
sources DOAJ
author Yusen Zhou
Yang Yang
Jingwei Huang
Shibo Jiang
Lanying Du
spellingShingle Yusen Zhou
Yang Yang
Jingwei Huang
Shibo Jiang
Lanying Du
Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
Viruses
Coronavirus
MERS-CoV
spike protein
receptor-binding domain
vaccines
therapeutics
author_facet Yusen Zhou
Yang Yang
Jingwei Huang
Shibo Jiang
Lanying Du
author_sort Yusen Zhou
title Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
title_short Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
title_full Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
title_fullStr Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
title_full_unstemmed Advances in MERS-CoV Vaccines and Therapeutics Based on the Receptor-Binding Domain
title_sort advances in mers-cov vaccines and therapeutics based on the receptor-binding domain
publisher MDPI AG
series Viruses
issn 1999-4915
publishDate 2019-01-01
description Middle East respiratory syndrome (MERS) coronavirus (MERS-CoV) is an infectious virus that was first reported in 2012. The MERS-CoV genome encodes four major structural proteins, among which the spike (S) protein has a key role in viral infection and pathogenesis. The receptor-binding domain (RBD) of the S protein contains a critical neutralizing domain and is an important target for development of MERS vaccines and therapeutics. In this review, we describe the relevant features of the MERS-CoV S-protein RBD, summarize recent advances in the development of MERS-CoV RBD-based vaccines and therapeutic antibodies, and illustrate potential challenges and strategies to further improve their efficacy.
topic Coronavirus
MERS-CoV
spike protein
receptor-binding domain
vaccines
therapeutics
url http://www.mdpi.com/1999-4915/11/1/60
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