2018年第一期JVI国内学者文章汇总

rentianyixu · 发表于 2018-1-13 20:20:54

1. The Postfusion Structure of the Heartland Virus Gc Glycoprotein Supports Taxonomic Separation of the Bunyaviral Families Phenuiviridae and Hantaviridae

[size=0.85em]aState Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, China
[size=0.85em]bResearch Network of Immunity and Health (RNIH), Beijing Institutes of Life Science, Chinese Academy of Sciences, Beijing, China
[size=0.85em]cCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China
[size=0.85em]dShenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital, Shenzhen, China
[size=0.85em]eCenter for Influenza Research and Early-Warning, Chinese Academy of Sciences, Beijing, China
[size=0.85em]fNational Institute for Viral Disease Control and Prevention, Chinese Center for Disease Control and Prevention (China CDC), Beijing, China

ABSTRACT

Heartland virus (HRTV) is an emerging human pathogen that belongs to the newly defined family Phenuiviridae, order Bunyavirales. Gn and Gc are two viral surface glycoproteins encoded by the M segment and are required for early events during infection. HRTV delivers its genome into the cytoplasm by fusion of the viral envelope and endosomal membranes under low-pH conditions. Here, we describe the crystal structure of HRTV Gc in its postfusion conformation. The structure shows that Gc displays a typical class II fusion protein conformation, and the overall structure is identical to severe fever with thrombocytopenia syndrome virus (SFTSV) Gc, which also belongs to the Phenuiviridae family. However, our structural analysis indicates that the hantavirus Gc presents distinct features in the aspects of subdomain orientation, N-linked glycosylation, the interaction pattern between protomers, and the fusion loop conformation. This suggests their family-specific subunit arrangement during the fusogenic process and supports the recent taxonomic revision of bunyaviruses. Our results provide insights into the comprehensive comparison of class II membrane fusion proteins in two bunyavirus families, yielding valuable information for treatments against these human pathogens.

Address correspondence to Wen-Hai Feng, whfeng@cau.edu.cn, or George Fu Gao, gaof@im.ac.cn.
Y.Z. and Y.W. contributed equally to this work.
Citation Zhu Y, Wu Y, Chai Y, Qi J, Peng R, Feng W-H, Gao GF. 2018. The postfusion structure of the heartland virus Gc glycoprotein supports taxonomic separation of the bunyaviral families Phenuiviridae andHantaviridae. J Virol 92:e01558-17.https://doi.org/10.1128/JVI.01558-17.

rentianyixu · 发表于 2018-1-13 20:22:25

2.Rice Stripe Tenuivirus Has a Greater Tendency To Use the Prime-and-Realign Mechanism in Transcription of Genomic than in Transcription of Antigenomic Template RNAs

[size=0.85em]aFujian Province Key Laboratory of Plant Virology, Institute of Plant Virology, Fujian Agriculture and Forestry University, Fuzhou, Fujian, China
[size=0.85em]bState Key Laboratory of Ecological Pest Control for Fujian and Taiwan Crops, Fuzhou, China

ABSTRACT

Most segmented negative-sense RNA viruses employ a process termed cap snatching, during which they snatch capped RNA leaders from host cellular mRNAs and use the snatched leaders as primers for transcription, leading to the synthesis of viral mRNAs with 5′ heterogeneous sequences (HSs). With traditional methods, only a few HSs can be determined, and identification of their donors is difficult. Here, the mRNA 5′ ends of Rice stripe tenuivirus (RSV) and Rice grassy stunt tenuivirus (RGSV) and those of their host rice were determined by high-throughput sequencing. Millions of tenuiviral HSs were obtained, and a large number of them mapped to the 5′ ends of corresponding host cellular mRNAs. Repeats of the dinucleotide AC, which are complementary to the U1G2 of the tenuiviral template 3′-U1G2U3G4UUUCG, were found to be prevalent at the 3′ termini of tenuiviral HSs. Most of these ACs did not match host cellular mRNAs, supporting the idea that tenuiviruses use the prime-and-realign mechanism during cap snatching. We previously reported a greater tendency of RSV than RGSV to use the prime-and-realign mechanism in transcription with leaders cap snatched from a coinfecting reovirus. Besides confirming this observation in natural tenuiviral infections, the data here additionally reveal that RSV has a greater tendency to use this mechanism in transcribing genomic than in transcribing antigenomic templates. The data also suggest that tenuiviruses cap snatch host cellular mRNAs from translation- and photosynthesis-related genes, and capped RNA leaders snatched by tenuiviruses base pair with U1/U3 or G2/G4of viral templates. These results provide unprecedented insights into the cap-snatching process of tenuiviruses.

Address correspondence to Zhenguo Du, duzhenguo1228@163.com, or Zujian Wu, wuzujian@126.com.
X.L. and J.J. contributed equally to this work.
Citation Liu X, Jin J, Qiu P, Gao F, Lin W, Xie G, He S, Liu S, Du Z, Wu Z. 2018.Rice stripe tenuivirus has a greater tendency to use the prime-and-realign mechanism in transcription of genomic than in transcription of antigenomic template RNAs. J Virol 92:e01414-17.https://doi.org/10.1128/JVI.01414-17.

rentianyixu · 发表于 2018-1-13 20:24:33

3.Residues 28 to 39 of the Extracellular Loop 1 of Chicken Na+/H+ Exchanger Type I Mediate Cell Binding and Entry of Subgroup J Avian Leukosis Virus

[size=0.85em]aDivision of Avian Infectious Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China
[size=0.85em]bVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA
[size=0.85em]cJiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Disease and Zoonoses, Yangzhou, China

ABSTRACT

Chicken Na+/H+ exchanger type I (chNHE1), a multispan transmembrane protein, is a cellular receptor of the subgroup J avian leukosis virus (ALV-J). To identify the functional determinants of chNHE1 responsible for the ALV-J receptor activity, a series of chimeric receptors was created by exchanging the extracellular loops (ECL) of human NHE1 (huNHE1) and chNHE1 and by ECL replacement with a hemagglutinin (HA) tag. These chimeric receptors then were used in binding and entry assays to map the minimal ALV-J gp85-binding domain of chNHE1. We show that ECL1 of chNHE1 (chECL1) is the critical functional ECL that interacts directly with ALV-J gp85; ECL3 is also involved in ALV-J gp85 binding. Amino acid residues 28 to 39 of the N-terminal membrane-proximal region of chECL1 constitute the minimal domain required for chNHE1 binding of ALV-J gp85. These residues are sufficient to mediate viral entry into ALV-J nonpermissive cells. Point mutation analysis revealed that A30, V33, W38, and E39 of chECL1 are the key residues mediating the binding between chNHE1 and ALV-J gp85. Further, the replacement of residues 28 to 39 of huNHE1 with the corresponding chNHE1 residues converted the nonfunctional ALV-J receptor huNHE1 to a functional one. Importantly, soluble chECL1 and huECL1 harboring chNHE1 residues 28 to 39 both could effectively block ALV-J infection. Collectively, our findings indicate that residues 28 to 39 of chNHE1 constitute a domain that is critical for receptor function and mediate ALV-J entry.

Address correspondence to Xiaomei Wang, xmw@hvri.ac.cn, or Yulong Gao,gaoyulong@caas.cn.
X.G. and Y.Z. contributed equally to this work.
Citation Guan X, Zhang Y, Yu M, Ren C, Gao Y, Yun B, Liu Y, Wang Y, Qi X, Liu C, Cui H, Zhang Y, Gao L, Li K, Pan Q, Zhang B, Wang X, Gao Y. 2018. Residues 28 to 39 of the extracellular loop 1 of chicken Na+/H+ exchanger type I mediate cell binding and entry of subgroup J avian leukosis virus. J Virol 92:e01627-17. https://doi.org/10.1128/JVI.01627-17.

rentianyixu · 发表于 2018-1-13 20:26:21

4.Distinct Roles of Cellular ESCRT-I and ESCRT-III Proteins in Efficient Entry and Egress of Budded Virions of Autographa californica Multiple Nucleopolyhedrovirus

[size=0.85em]aState Key Laboratory of Crop Stress Biology for Arid Areas, Key Laboratory of Northwest Loess Plateau Crop Pest Management of Ministry of Agriculture, College of Plant Protection, Northwest A&F University, Yangling, Shaanxi, China
[size=0.85em]bBoyce Thompson Institute, Cornell University, Ithaca, New York, USA

ABSTRACT

The endosomal sorting complex required for transport (ESCRT) machinery is necessary for budding of many enveloped viruses. Recently, it was demonstrated that Vps4, the key regulator for recycling of the ESCRT-III complex, is required for efficient infection by the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV). However, ESCRT assembly, regulation, and function are complex, and little is known regarding the details of participation of specific ESCRT complexes in AcMNPV infection. In this study, the core components of ESCRT-I (Tsg101 and Vps28) and ESCRT-III (Vps2B, Vps20, Vps24, Snf7, Vps46, and Vps60) were cloned from Spodoptera frugiperda. Using a viral complementation system and RNA interference (RNAi) assays, we found that ESCRT-I and ESCRT-III complexes are required for efficient entry of AcMNPV into insect cells. In cells knocking down or overexpressing dominant negative (DN) forms of the components of ESCRT-I and ESCRT-III complexes, entering virions were partially trapped within the cytosol. To examine only egress, cells were transfected with the double-stranded RNA (dsRNA) targeting an individual ESCRT-I or ESCRT-III gene and viral bacmid DNA or viral bacmid DNA that expressed DN forms of ESCRT-I and ESCRT-III components. We found that ESCRT-III components (but not ESCRT-I components) are required for efficient nuclear egress of progeny nucleocapsids. In addition, we found that several baculovirus core or conserved proteins (Ac11, Ac76, Ac78, GP41, Ac93, Ac103, Ac142, and Ac146) interact with Vps4 and components of ESCRT-III. We propose that these viral proteins may form an “egress complex” that is involved in recruiting ESCRT-III components to a virus egress domain on the nuclear membrane.

Address correspondence to Zhaofei Li, zhaofeili73@outlook.com.
Q. Yue and Q. Yu contributed equally to this work.
Citation Yue Q, Yu Q, Yang Q, Xu Y, Guo Y, Blissard GW, Li Z. 2018. Distinct roles of cellular ESCRT-I and ESCRT-III proteins in efficient entry and egress of budded virions of Autographa californica multiple nucleopolyhedrovirus. J Virol 92:e01636-17. https://doi.org/10.1128/JVI.01636-17.
Supplemental material for this article may be found athttps://doi.org/10.1128/JVI.01636-17.

rentianyixu · 发表于 2018-1-13 20:28:06

5.Innate Sensing of Influenza A Virus Hemagglutinin Glycoproteins by the Host Endoplasmic Reticulum (ER) Stress Pathway Triggers a Potent Antiviral Response via ER-Associated Protein Degradation

[size=0.85em]aHarbin Veterinary Research Institute, CAAS-Michigan State University Joint Laboratory of Innate Immunity, State Key Laboratory of Veterinary Biotechnology, Chinese Academy of Agricultural Sciences, Harbin, China
[size=0.85em]bDepartment of Microbiology and Molecular Genetics, Michigan State University, East Lansing, Michigan, USA

ABSTRACT

Innate immunity provides an immediate defense against infection after host cells sense danger signals from microbes. Endoplasmic reticulum (ER) stress arises from accumulation of misfolded/unfolded proteins when protein load overwhelms the ER folding capacity, which activates the unfolded protein response (UPR) to restore ER homeostasis. Here, we show that a mechanism for antiviral innate immunity is triggered after the ER stress pathway senses viral glycoproteins. When hemagglutinin (HA) glycoproteins from influenza A virus (IAV) are expressed in cells, ER stress is induced, resulting in rapid HA degradation via proteasomes. The ER-associated protein degradation (ERAD) pathway, an important UPR function for destruction of aberrant proteins, mediates HA degradation. Three class I α-mannosidases were identified to play a critical role in the degradation process, including EDEM1, EDEM2, and ERManI. HA degradation requires either ERManI enzymatic activity or EDEM1/EDEM2 enzymatic activity when ERManI is not expressed, indicating that demannosylation is a critical step for HA degradation. Silencing of EDEM1, EDEM2, and ERManI strongly increases HA expression and promotes IAV replication. Thus, the ER stress pathway senses influenza HA as “nonself” or misfolded protein and sorts HA to ERAD for degradation, resulting in inhibition of IAV replication.

Address correspondence to Yong-Hui Zheng, zhengyo@msu.edu.
D.A.F. and B.W. contributed equally to this work.
Citation Frabutt DA, Wang B, Riaz S, Schwartz RC, Zheng Y-H. 2018. Innate sensing of influenza A virus hemagglutinin glycoproteins by the host endoplasmic reticulum (ER) stress pathway triggers a potent antiviral response via ER-associated protein degradation. J Virol 92:e01690-17.https://doi.org/10.1128/JVI.01690-17.

rentianyixu · 发表于 2018-1-13 20:29:30

6.MicroRNA gga-miR-130b Suppresses Infectious Bursal Disease Virus Replication via Targeting of the Viral Genome and Cellular Suppressors of Cytokine Signaling 5

[size=0.85em]aState Key Laboratory of Agrobiotechnology, Beijing, China
[size=0.85em]bKey Laboratory of Animal Epidemiology and Zoonosis, Ministry of Agriculture, Beijing, China
[size=0.85em]cCollege of Veterinary Medicine, China Agricultural University, Beijing, China

ABSTRACT

MicroRNAs (miRNAs) are small noncoding RNAs that regulate gene expression posttranscriptionally through silencing or degrading their targets, thus playing important roles in the immune response. However, the role of miRNAs in the host response against infectious bursal disease virus (IBDV) infection is not clear. In this study, we show that the expression of a series of miRNAs was significantly altered in DF-1 cells after IBDV infection. We found that the miRNA gga-miR-130b inhibited IBDV replication via targeting the specific sequence of IBDV segment A and enhanced the expression of beta interferon (IFN-β) by targeting suppressors of cytokine signaling 5 (SOCS5) in host cells. These findings indicate that gga-miR-130b-3p plays a crucial role in host defense against IBDV infection.

Address correspondence to Shijun J. Zheng, sjzheng@cau.edu.cn.
Citation Fu M, Wang B, Chen X, He Z, Wang Y, Li X, Cao H, Zheng SJ. 2018. MicroRNA gga-miR-130b suppresses infectious bursal disease virus replication via targeting of the viral genome and cellular suppressors of cytokine signaling 5. J Virol 92:e01646-17. https://doi.org/10.1128/JVI.01646-17.

rentianyixu · 发表于 2018-1-13 20:31:29

7.Structure, Immunogenicity, and Protective Mechanism of an Engineered Enterovirus 71-Like Particle Vaccine Mimicking 80S Empty Capsid

Xiaoli Wanga,d, Zhiqiang Kua,d, Xiang Zhangb,d, Xiaohua Yea, Jinhuan Chenb,d, Qingwei Liua, Wei Zhanga,d, Chao Zhanga, Zhenglin Fub,c, Xia Jina, Yao Congb,c and Zhong Huanga
aUnit of Vaccinology and Antiviral Strategies, CAS Key Laboratory of Molecular Virology and Immunology, Institut Pasteur of Shanghai, Chinese Academy of Sciences, Shanghai, China
bNational Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, China
cShanghai Science Research Center, Chinese Academy of Sciences, Shanghai, China
dUniversity of Chinese Academy of Sciences, Beijing, China

ABSTRACT

Enterovirus 71 (EV71) is the major causative agent of severe hand, foot, and mouth disease, which affects millions of young children in the Asia-Pacific region annually. In this study, we engineered a novel EV71 virus-like particle (VLP) that lacks VP4 (therefore designated VLPΔVP4) and investigated its structure, antigenicity, and vaccine potential. The cryo-electron microscopy (cryo-EM) structure of VLPΔVP4 was reconstructed to 3.71-Å resolution. Results from structural and biochemical analyses revealed that VLPΔVP4 resembles the end product of the viral uncoating process, the 80S empty capsid. VLPΔVP4 is able to elicit high-titer neutralizing antibodies and to fully protect mice against lethal viral challenge. Mechanistic studies showed that, at the cellular level, the anti-VLPΔVP4 sera exert neutralization effects at both pre- and postattachment stages by inhibiting both virus attachment and internalization, and at the molecular level, the antisera can block multiple interactions between EV71 and its key receptors. Our study gives a better understanding of EV71 capsid assembly and provides important information for the design and development of new-generation vaccines for EV71, and perhaps for other enteroviruses, as well.

Address correspondence to Yao Cong, cong@sibcb.ac.cn, or Zhong Huang, huangzhong@ips.ac.cn.
X.W., Z.K., and X.Z. contributed equally to this work.
Citation Wang X, Ku Z, Zhang X, Ye X, Chen J, Liu Q, Zhang W, Zhang C, Fu Z, Jin X, Cong Y, Huang Z. 2018. Structure, immunogenicity, and protective mechanism of an engineered enterovirus 71-like particle vaccine mimicking 80S empty capsid. J Virol 92:e01330-17. https://doi.org/10.1128/JVI.01330-17.

		自动登录	找回密码
密码			立即注册