A recombinant receptor-binding domain of MERS-CoV in trimeric form protects human dipeptidyl peptidase 4 (hDPP4) transgenic mice from MERS-CoV infection

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A recombinant receptor-binding domain of MERS-CoV in trimeric form protects human dipeptidyl peptidase 4 (hDPP4) transgenic mice from MERS-CoV infection

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作者：Wanbo Tai^a ; ^b ; Guangyu Zhao^a ; Shihun Sun^a ; Yan Guo^a ; Yufei Wang^a ; ^b ; Xinrong Tao^c ; Chien-Te K. Tseng^c ; Fang Li^d ; Shibo Jiang^b ; ^e ; ^{sjiang@nybc.org" class="auth_mail" title="E-mail the corresponding author} ; Lanying ; Du^b ; ^{ldu@nybc.org" class="auth_mail" title="E-mail the corresponding author} ; Yusen Zhou^a ; ^{yszhou@bmi.ac.cn" class="auth_mail" title="E-mail the corresponding author}
关键词：MERS ; MERS-CoV ; Spike protein ; Receptor-binding domain ; Foldon trimerization motif ; Neutralization ; hDPP4-transgenic mice ; Protection
刊名：Virology
出版年：2016
出版时间：December 2016
年：2016
卷：499
期：Complete
页码：375-382
全文大小：1159 K

文摘

•: A trimeric MERS-CoV protein (RBD-Fd) was constructed by fusing viral RBD with foldon trimerization motif.
•: RBD-Fd bound strongly to dipeptidyl peptidase 4 (DPP4), the receptor of MERS-CoV, and RBD-specific neutralizing antibodies.
•: RBD-Fd induced robust and long-term neutralizing antibodies, cross-neutralizing MERS pseudovirus of divergent strains.
•: RBD-Fd potently protected hDPP4 transgenic mice from lethal MERS-CoV challenge.