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Your search keyword '"Rao, Zihe"' showing total 20 results
Start Over Author "Rao, Zihe" Journal journal of virology
20 results on '"Rao, Zihe"'

1. Crystal Structure of African Swine Fever Virus pS273R Protease and Implications for Inhibitor Design

Author

Li, Guobang, primary, Liu, Xiaoxia, additional, Yang, Mengyuan, additional, Zhang, Guangshun, additional, Wang, Zhengyang, additional, Guo, Kun, additional, Gao, Yuxue, additional, Jiao, Peng, additional, Sun, Jixue, additional, Chen, Cheng, additional, Wang, Hao, additional, Deng, Weilong, additional, Xiao, Huihe, additional, Li, Sizheng, additional, Wu, Haoru, additional, Wang, Ying, additional, Cao, Lin, additional, Jia, Zihan, additional, Shang, Luqing, additional, Yang, Cheng, additional, Guo, Yu, additional, and Rao, Zihe, additional

Published
2020
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6. Structures of Coxsackievirus A16 Capsids with Native Antigenicity: Implications for Particle Expansion, Receptor Binding, and Immunogenicity

Author

Ren, Jingshan, primary, Wang, Xiangxi, additional, Zhu, Ling, additional, Hu, Zhongyu, additional, Gao, Qiang, additional, Yang, Pan, additional, Li, Xuemei, additional, Wang, Junzhi, additional, Shen, Xinliang, additional, Fry, Elizabeth E., additional, Rao, Zihe, additional, and Stuart, David I., additional

Published
2015
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10. Nucleoside Monophosphate Complex Structures of the Endonuclease Domain from the Influenza Virus Polymerase PA Subunit Reveal the Substrate Binding Site inside the Catalytic Center

Author

Zhao, Cong, primary, Lou, Zhiyong, additional, Guo, Yu, additional, Ma, Ming, additional, Chen, Yutao, additional, Liang, Shuaiyi, additional, Zhang, Liang, additional, Chen, Shoudeng, additional, Li, Xuemei, additional, Liu, Yingfang, additional, Bartlam, Mark, additional, and Rao, Zihe, additional

Published
2009
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19. The Crystal Structure of Porcine Reproductive and Respiratory Syndrome Virus Nonstructural Protein Nsp1β Reveals a Novel Metal-Dependent Nuclease.

Author

Fei Xue, Yuna Sun, Liming Yan, Cong Zhao, Ji Chen, Bartlam, Mark, Xuemei Li, Zhiyong Lou, and Rao, Zihe

Subjects
*NIDOVIRUSES, *GENOMES, *CRYSTALS, *PAPAIN, *SWINE diseases
Abstract

Porcine reproductive and respiratory syndrome virus (PRRSV), a member of the Arteriviridae family of Nidovirales, is the causative agent of porcine reproductive and respiratory syndrome, which results in enormous economic losses in the swine industry. As the second protein encoded by the PRRSV genome, nsp1β cleaves itself from the downstream nsp2 protein via a C-terminal papain-like cysteine protease (PCP) domain. Although nsp1β is known to be involved in virulence, its precise role in the process of viral infection remains unclear. In this work, we describe the homodimeric crystal structure of PRRSV nsp1β in its natural, self-processed form. We show that the architecture of its N-terminal domain (NTD) adopts a fold closely resembling that of several known nucleases and has intrinsic nuclease activity that is strongly activated by manganese ions in vitro. Key features, however, distinguish nsp1β from characterized nucleases, including the C-terminal PCP domain (which is responsible for the self-release of nsp1β from nsp2), a linker domain (LKD) that connects the NTD and the PCP domain, and a C-terminal extension (CTE) that binds to and is stabilized by the putative substrate binding site of the PCPβ domain. Combined with the reported nuclear localization of this protein, these results shed light on the self-processing mode and precise biological function of nsp1β and thus offer a multitarget template for future drug discovery. [ABSTRACT FROM AUTHOR]

Published
2010
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20. Structural Adaptations of Norovirus GII.17/13/21 Lineage through Two Distinct Evolutionary Paths.

Author

Qian Y, Song M, Jiang X, Xia M, Meller J, Tan M, Chen Y, Li X, and Rao Z

Subjects
Binding Sites, Crystallography, X-Ray, Evolution, Molecular, Genetic Variation, Humans, Models, Molecular, Norovirus chemistry, Phylogeny, Protein Binding, Protein Conformation, Protein Domains, Viral Proteins metabolism, Blood Group Antigens metabolism, Mutation, Norovirus classification, Viral Proteins chemistry
Abstract

Human noroviruses (huNoVs), which cause epidemic acute gastroenteritis, recognize histo-blood group antigens (HBGAs) as host attachment factors affecting host susceptibility. HuNoVs are genetically diverse, containing at least 31 genotypes in the two major genogroups (genogroup I [GI] and GII). Three GII genotypes, GII genotype 17 (GII.17), GII.13, and GII.21, form a unique genetic lineage, in which the GII.17 genotype retains the conventional GII HBGA binding site (HBS), while the GII.13/21 genotypes acquire a completely new HBS. To understand the molecular bases behind these evolutionary changes, we solved the crystal structures of the HBGA binding protruding domains of (i) an early GII.17 variant (the 1978 variant) that does not bind or binds weakly to HBGAs, (ii) the new GII.17 variant (the 2014/15 variant) that binds A/B/H antigens strongly via an optimized GII HBS, and (iii) a GII.13 variant (the 2010 variant) that binds the Lewis a (Le a ) antigen via the new HBS. These serial, high-resolution structural data enable a comprehensive structural comparison to understand the evolutionary changes of the GII.17/13/21 lineage, including the emergence of the new HBS of the GII.13/21 sublineage and the possible HBS optimization of the recent GII.17 variant for an enhanced HBGA binding ability. Our study elucidates the structural adaptations of the GII.17/13/21 lineage through distinct evolutionary paths, which may allow a theory explaining huNoV adaptations and evolutions to be put forward. IMPORTANCE Our understanding of the molecular bases behind the interplays between human noroviruses and their host glycan ligands, as well as their evolutionary changes over time with alterations in their host ligand binding capability and host susceptibility, remains limited. By solving the crystal structures of the glycan ligand binding protruding (P) domains with or without glycan ligands of three representative noroviruses of the GII.17/13/21 genetic lineage, we elucidated the molecular bases of the human norovirus-glycan interactions of this special genetic lineage. We present solid evidence on how noroviruses of this genetic lineage evolved via different evolutionary paths to (i) optimize their glycan binding site for higher glycan binding function and (ii) acquire a completely new glycan binding site for new ligands. Our data shed light on the mechanism of the structural adaptations of human noroviruses through different evolutionary paths, facilitating our understanding of human norovirus adaptations, evolutions, and epidemiology., (Copyright © 2018 American Society for Microbiology.)

Published
2018
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