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  1. Article ; Online: Genomic characteristics of an avipoxvirus 282E4 strain.

    Deng, Lingcong / Liu, Cunxia / Li, Letian / Hao, Pengfei / Wang, Maopeng / Jin, Ningyi / Yin, Ronglan / Du, Shouwen / Li, Chang

    Virus research

    2023  Volume 336, Page(s) 199218

    Abstract: Avipoxvirus 282E4 strain was extensively applied into recombinant vaccine vector to prevent other infectious diseases. However, little information on the genomic background, functional and genetic evolutionary of the isolate 282E4 strain was clarified. ... ...

    Abstract Avipoxvirus 282E4 strain was extensively applied into recombinant vaccine vector to prevent other infectious diseases. However, little information on the genomic background, functional and genetic evolutionary of the isolate 282E4 strain was clarified. The results showed that the linear genome of avipoxvirus 282E4 was 308,826 bp, containing 313 open reading frames (ORFs) and 12 new predicted ORFs. The 282E4 strain appears to encode two novel thymidine kinase proteins and two TGF-beta-like proteins that may be associated with the suppression of the host's antiviral response. Avipoxvirus 282E4 also encodes 57 ankyrin repeat proteins and 5 variola B22R-like proteins, which composed 7% of the avipoxvirus 282E4 genome. GO and KEGG analysis further revealed that 12 ORFs participate in viral transcription process, 7 ORFs may function during DNA repair, replication and biological synthesis, and ORF 208 is involved in the process of virus life cycle. Interestingly, phylogenetic analysis based on concatenated sequences p4b and DNA polymerase of avipoxviruses gene demonstrates that avipoxvirus 282E4 strain is divergent from known FWPV isolates and is similar to shearwater poxvirus (SWPV-1) that belongs to the CNPV-like virus. Sequencing avipoxvirus 282E4 is a significant step to judge the genetic position of avipoxviruses within the larger Poxviridae phylogenetic tree and provide a new insight into the genetic background of avipoxvirus 282E4 and interspecies transmission of poxviruses, meanwhile, explanation of gene function provides theoretical foundation for vaccine design with 282E4 strain as skeleton.
    Language English
    Publishing date 2023-09-13
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 605780-9
    ISSN 1872-7492 ; 0168-1702
    ISSN (online) 1872-7492
    ISSN 0168-1702
    DOI 10.1016/j.virusres.2023.199218
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Interaction of Nipah Virus F and G with the Cellular Protein Cortactin Discovered by a Proximity Interactome Assay.

    Cui, Chunmei / Hao, Pengfei / Jin, Chaozhi / Xu, Wang / Liu, Yuchen / Li, Letian / Du, Shouwen / Shang, Limin / Jin, Xin / Jin, Ningyi / Wang, Jian / Li, Chang

    International journal of molecular sciences

    2024  Volume 25, Issue 7

    Abstract: Nipah virus (NiV) is a highly lethal zoonotic virus with a potential large-scale outbreak, which poses a great threat to world health and security. In order to explore more potential factors associated with NiV, a proximity labeling method was applied to ...

    Abstract Nipah virus (NiV) is a highly lethal zoonotic virus with a potential large-scale outbreak, which poses a great threat to world health and security. In order to explore more potential factors associated with NiV, a proximity labeling method was applied to investigate the F, G, and host protein interactions systematically. We screened 1996 and 1524 high-confidence host proteins that interacted with the NiV fusion (F) glycoprotein and attachment (G) glycoprotein in HEK293T cells by proximity labeling technology, and 863 of them interacted with both F and G. The results of GO and KEGG enrichment analysis showed that most of these host proteins were involved in cellular processes, molecular binding, endocytosis, tight junction, and other functions. Cytoscape software (v3.9.1) was used for visual analysis, and the results showed that Cortactin (CTTN), Serpine mRNA binding protein 1 (SERBP1), and stathmin 1 (STMN1) were the top 20 proteins and interacted with F and G, and were selected for further validation. We observed colocalization of F-CTTN, F-SERBP1, F-STMN1, G-CTTN, G-SERBP1, and G-STMN1 using confocal fluorescence microscopy, and the results showed that CTTN, SERBP1, and STMN1 overlapped with NiV F and NiV G in HEK293T cells. Further studies found that CTTN can significantly inhibit the infection of the Nipah pseudovirus (NiVpv) into host cells, while SERBP1 and STMN1 had no significant effect on pseudovirus infection. In addition, CTTN can also inhibit the infection of the Hendra pseudovirus (HeVpv) in 293T cells. In summary, this study revealed that the potential host proteins interacted with NiV F and G and demonstrated that CTTN could inhibit NiVpv and HeVpv infection, providing new evidence and targets for the study of drugs against these diseases.
    MeSH term(s) Humans ; Nipah Virus ; Cortactin ; HEK293 Cells ; Endocytosis ; Glycoproteins
    Chemical Substances Cortactin ; Glycoproteins
    Language English
    Publishing date 2024-04-08
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms25074112
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  3. Article: The Magnesium Concentration in Yeast Extracts Is a Major Determinant Affecting Ethanol Fermentation Performance of

    Li, Runxia / Jin, Mingjie / Du, Jun / Li, Mian / Chen, Shouwen / Yang, Shihui

    Frontiers in bioengineering and biotechnology

    2020  Volume 8, Page(s) 957

    Abstract: Zymomonas ... ...

    Abstract Zymomonas mobilis
    Language English
    Publishing date 2020-08-31
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2719493-0
    ISSN 2296-4185
    ISSN 2296-4185
    DOI 10.3389/fbioe.2020.00957
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: IFITM3 inhibits severe fever with thrombocytopenia syndrome virus entry and interacts with viral Gc protein.

    Du, Shouwen / Wang, Yuhang / Wang, Jiamin / Ma, Yidan / Xu, Wang / Shi, Xiaoshuang / Li, Letian / Hao, Pengfei / Liu, Quan / Liao, Ming / Zhou, Boping / Jin, Ningyi / Wong, Yin K / Hu, Lifen / Wang, Jigang / Liu, Wei / Li, Chang

    Journal of medical virology

    2024  Volume 96, Issue 3, Page(s) e29491

    Abstract: Severe fever with thrombocytopenia syndrome (SFTS) is an emerging tick-borne hemorrhagic fever disease with high fatality rate of 10%-20%. Vaccines or specific therapeutic measures remain lacking. Human interferon inducible transmembrane protein 3 ( ... ...

    Abstract Severe fever with thrombocytopenia syndrome (SFTS) is an emerging tick-borne hemorrhagic fever disease with high fatality rate of 10%-20%. Vaccines or specific therapeutic measures remain lacking. Human interferon inducible transmembrane protein 3 (hIFITM3) is a broad-spectrum antiviral factor targeting viral entry. However, the antiviral activity of hIFITM3 against SFTS virus (SFTSV) and the functional mechanism of IFITM3 remains unclear. Here we demonstrate that endogenous IFITM3 provides protection against SFTSV infection and participates in the anti-SFTSV effect of type Ⅰ and Ⅲ interferons (IFNs). IFITM3 overexpression exhibits anti-SFTSV function by blocking Gn/Gc-mediated viral entry and fusion. Further studies showed that IFITM3 binds SFTSV Gc directly and its intramembrane domain (IMD) is responsible for this interaction and restriction of SFTSV entry. Mutation of two neighboring cysteines on IMD weakens IFITM3-Gc interaction and attenuates the antiviral activity of IFITM3, suggesting that IFITM3-Gc interaction may partly mediate the inhibition of SFTSV entry. Overall, our data demonstrate for the first time that hIFITM3 plays a critical role in the IFNs-mediated anti-SFTSV response, and uncover a novel mechanism of IFITM3 restriction of SFTSV infection, highlighting the potential of clinical intervention on SFTS disease.
    MeSH term(s) Humans ; Bunyaviridae Infections/immunology ; Membrane Proteins/immunology ; Phlebovirus ; RNA-Binding Proteins/immunology ; Severe Fever with Thrombocytopenia Syndrome/immunology ; Viral Proteins/metabolism ; Virus Internalization ; Antiviral Restriction Factors/immunology
    Chemical Substances IFITM3 protein, human ; Membrane Proteins ; RNA-Binding Proteins ; Viral Proteins ; Antiviral Restriction Factors
    Language English
    Publishing date 2024-02-25
    Publishing country United States
    Document type Journal Article
    ZDB-ID 752392-0
    ISSN 1096-9071 ; 0146-6615
    ISSN (online) 1096-9071
    ISSN 0146-6615
    DOI 10.1002/jmv.29491
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Generation and Evaluation of Recombinant Baculovirus Coexpressing

    Xu, Wang / Du, Shouwen / Li, Tiyuan / Wu, Shipin / Jin, Ningyi / Ren, Linzhu / Li, Chang

    Viral immunology

    2021  Volume 34, Issue 10, Page(s) 697–707

    Abstract: Porcine reproductive and respiratory syndrome virus (PRRSV) is the pathogen of the porcine reproductive and respiratory syndrome, which is one of the most economically devastating diseases of the swine industry. However, whether the inactivated vaccine ... ...

    Abstract Porcine reproductive and respiratory syndrome virus (PRRSV) is the pathogen of the porcine reproductive and respiratory syndrome, which is one of the most economically devastating diseases of the swine industry. However, whether the inactivated vaccine and modified live attenuated vaccines are effective in disease control is still controversial. Although several groups developed PRRSV virus-like particles (VLPs) as a vaccine against PRRSV, all these VLP-based vaccines targeted PRRSV-2, but not PRRSV-1 or both. Therefore, it is urgent to produce VLPs against PRRSV-1. In this study, we rescued recombinant baculovirus expressing
    MeSH term(s) Animals ; Antibodies, Viral ; Baculoviridae/genetics ; Porcine Reproductive and Respiratory Syndrome/prevention & control ; Porcine respiratory and reproductive syndrome virus/genetics ; Swine ; Viral Envelope Proteins/genetics ; Viral Vaccines/genetics
    Chemical Substances Antibodies, Viral ; Viral Envelope Proteins ; Viral Vaccines
    Language English
    Publishing date 2021-12-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 639075-4
    ISSN 1557-8976 ; 0882-8245
    ISSN (online) 1557-8976
    ISSN 0882-8245
    DOI 10.1089/vim.2021.0018
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: A Subunit Vaccine Candidate Composed of Mpox Virus A29L, M1R, A35R, and B6R Elicits Robust Immune Response in Mice.

    Yang, Xuetao / Yang, Xidan / Du, Shouwen / Hu, Congxia / Yang, Xiu / Wang, Xingyun / Hu, Xing / Rcheulishvili, Nino / Wang, Peng George / Lin, Jihui

    Vaccines

    2023  Volume 11, Issue 9

    Abstract: With no specific antiviral drugs and preventive vaccines against Mpox virus (MPXV), the epidemic has led to the declaration of a Public Health Emergency of International Concern. As a developmental direction for new vaccines, studies of subunit vaccines ... ...

    Abstract With no specific antiviral drugs and preventive vaccines against Mpox virus (MPXV), the epidemic has led to the declaration of a Public Health Emergency of International Concern. As a developmental direction for new vaccines, studies of subunit vaccines based upon MPXV antigen proteins are lacking. In this study, A29L, M1R, A35R, and B6R of MPXV were expressed and purified from a prokaryotic system. The four MPXV antigen proteins in combination were mixed with aluminum hydroxide or CpG7909 as adjuvant, and subsequently used to inoculate mice. The results of enzyme-linked immunosorbent assay (ELISA), flow cytometry analyses, and enzyme-linked immunospot (ELISPOT) assays indicated that A29L, M1R, A35R, and B6R elicited high-level antigen-specific antibodies and CD4
    Language English
    Publishing date 2023-08-25
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2703319-3
    ISSN 2076-393X
    ISSN 2076-393X
    DOI 10.3390/vaccines11091420
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  7. Article ; Online: Identification of a Novel Interferon Lambda Splice Variant in Chickens.

    Chen, Jing / Li, Peiheng / Zou, Wancheng / Jiang, Yuhang / Li, Letian / Hao, Pengfei / Gao, Zihan / Qu, Qiaoqiao / Pang, Zhaoxia / Zhuang, Xinyu / Nan, Fulong / Jin, Ningyi / Du, Shouwen / Li, Chang

    Journal of virology

    2023  Volume 97, Issue 3, Page(s) e0174322

    Abstract: Type III interferons (IFNLs) have critical roles in the host's innate immune system, also serving as the first line against pathogenic infections of mucosal surfaces. In mammals, several IFNLs have been reported; however, only limited data on the ... ...

    Abstract Type III interferons (IFNLs) have critical roles in the host's innate immune system, also serving as the first line against pathogenic infections of mucosal surfaces. In mammals, several IFNLs have been reported; however, only limited data on the repertoire of IFNLs in avian species is available. Previous studies showed only one member in chicken (chIFNL3). Herein, we identified a novel chicken IFNL for the first time, termed chIFNL3a, which contains 354 bp, and encodes 118 amino acids. The predicted protein is 57.1% amino acid identity with chIFNL. Genetic, evolutionary, and sequence analyses indicated that the new open reading frame (ORF) groups with type III chicken IFNs represent a novel splice variant. Compared to IFNs from different species, the new ORF is clustered within the type III IFNs group. Further study showed that chIFNL3a could activate a panel of IFN-regulated genes and function mediated by the IFNL receptor, and chIFNL3a markedly inhibited the replication of Newcastle disease virus (NDV) and influenza virus
    MeSH term(s) Animals ; Chickens ; Interferon Lambda ; Antiviral Agents/pharmacology ; Interferons/metabolism ; Orthomyxoviridae/metabolism ; Newcastle disease virus/metabolism ; Mammals
    Chemical Substances Interferon Lambda ; Antiviral Agents ; Interferons (9008-11-1)
    Language English
    Publishing date 2023-03-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.01743-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Interaction of species A rotavirus VP4 with the cellular proteins vimentin and actin related protein 2 discovered by a proximity interactome assay.

    Hao, Pengfei / Qu, Qiaoqiao / Pang, Zhaoxia / Li, Letian / Du, Shouwen / Shang, Limin / Jin, Chaozhi / Xu, Wang / Ha, Zhuo / Jiang, Yuhang / Chen, Jing / Gao, Zihan / Jin, Ningyi / Wang, Jian / Li, Chang

    Journal of virology

    2023  Volume 97, Issue 12, Page(s) e0137623

    Abstract: Importance: Rotavirus (RV) is an important zoonosis virus, which can cause severe diarrhea and extra-intestinal infection. To date, some proteins or carbohydrates have been shown to participate in the attachment or internalization of RV, including HGBAs, ...

    Abstract Importance: Rotavirus (RV) is an important zoonosis virus, which can cause severe diarrhea and extra-intestinal infection. To date, some proteins or carbohydrates have been shown to participate in the attachment or internalization of RV, including HGBAs, Hsc70, and integrins. This study attempted to indicate whether there were other proteins that would participate in the entry of RV; thus, the RV VP4-interacting proteins were identified by proximity labeling. After analysis and verification, it was found that VIM and ACTR2 could significantly promote the proliferation of RV in intestinal cells. Through further viral binding assays after knockdown, antibody blocking, and recombinant protein overexpression, it was revealed that both VIM and ACTR2 could promote RV replication.
    MeSH term(s) Animals ; Humans ; Actin-Related Protein 2/genetics ; Actin-Related Protein 2/metabolism ; Capsid Proteins/metabolism ; Intestines/cytology ; Protein Interaction Maps ; Rotavirus/chemistry ; Rotavirus/metabolism ; Vimentin/genetics ; Vimentin/metabolism ; Virus Internalization ; Virus Replication ; Protein Binding
    Chemical Substances Actin-Related Protein 2 ; Capsid Proteins ; Vimentin ; VP4 protein, Rotavirus
    Language English
    Publishing date 2023-11-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.01376-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: IFITM3 restricts RABV infection through inhibiting viral entry and mTORC1- dependent autophagy.

    Ma, Jiaqi / Tu, Zhongzhong / Du, Shouwen / Zhang, Xinying / Wang, Jie / Guo, Jianxiong / Feng, Ye / He, Hongbin / Wang, Hongmei / Li, Chang / Tu, Changchun / Liu, Yan

    Veterinary microbiology

    2023  Volume 284, Page(s) 109823

    Abstract: Rabies, which caused by rabies virus (RABV), is a zoonotic and life-threatening disease with 100% mortality, and there is no effective treatment thus far due to the unclear pathogenesis and less of treatment targets. Interferon-induced transmembrane ... ...

    Abstract Rabies, which caused by rabies virus (RABV), is a zoonotic and life-threatening disease with 100% mortality, and there is no effective treatment thus far due to the unclear pathogenesis and less of treatment targets. Interferon-induced transmembrane protein 3 (IFITM3) has recently been identified as an important anti-viral host effector induced by type I interferon. However, the role of IFITM3 in RABV infection has not been elucidated. In this study, we demonstrated that IFITM3 is a crucial restriction factor for RABV, the viral-induced IFITM3 significantly inhibited RABV replication, while knockdown of IFITM3 had the opposite effect. We then identified that IFNβ induces the upregulation of IFITM3 in the absence or presence of RABV infection, meanwhile, IFITM3 positively regulates RABV-triggered production of IFNβ in a feedback manner. In-depth research we found that IFITM3 not only inhibits the virus absorb and entry, but also inhibits viral replication through mTORC1-dependent autophagy. All these findings broaden our understanding of IFITM3 function and uncover a novel mechanism against RABV infection.
    MeSH term(s) Animals ; Rabies virus ; Rabies/veterinary ; Virus Internalization ; Virus Replication ; Interferon Type I/metabolism ; Autophagy
    Chemical Substances Interferon Type I
    Language English
    Publishing date 2023-06-28
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 753154-0
    ISSN 1873-2542 ; 0378-1135
    ISSN (online) 1873-2542
    ISSN 0378-1135
    DOI 10.1016/j.vetmic.2023.109823
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  10. Article ; Online: Evaluation and comparison of immune responses induced by two Mpox mRNA vaccine candidates in mice.

    Yang, Xidan / Hu, Congxia / Yang, Xuetao / Yang, Xiu / Hu, Xing / Wang, Xingyun / Liu, Cong / Yuan, Yuan / Du, Shouwen / Wang, Peng George / Lin, Jihui

    Journal of medical virology

    2023  Volume 95, Issue 10, Page(s) e29140

    Abstract: The epidemic of Mpox virus (MPXV) from May 2022 was once declared as a Public Health Emergency of International Concern by the World Health Organization. Vaccines play an important role in prevention of infectious diseases, and mRNA vaccine technology ... ...

    Abstract The epidemic of Mpox virus (MPXV) from May 2022 was once declared as a Public Health Emergency of International Concern by the World Health Organization. Vaccines play an important role in prevention of infectious diseases, and mRNA vaccine technology was proved to be a safe and effective platform with successful application in defense of coronavirus disease 2019. In this study, based on A29L, M1R, A35R, and B6R of MPXV, we developed two MPXV mRNA vaccine candidates, designated as MPXfus and MPXmix. The MPXfus was one-component, in which these four antigen proteins were linked in tandem by flexible linker and encoded by an individual mRNA as a fusion protein. The MPXmix was multicomponent containing four mRNA, and each mRNA encoded one antigen protein respectively. Mice were immunized with equal quality of MPXfus or MPXmix, delivered by lipid nanoparticles for evaluation and comparison of the immune responses induced by these two MPXV vaccine candidates. Results of immune response analyses indicated that both MPXfus and MPXmix could elicit high-level of antigen-specific antibodies and robust cellular immune response in mice. Moreover, results of virus neutralization assays suggested that sera from MPXfus- or MPXmix-immunized mice possessed high neutralizing activities against vaccinia virus. In addition, titers of antigen-specific antibody, levels of cellular immune response, and activities of neutralizing antibody against vaccinia virus induced by MPXfus and MPXmix presented no significant difference. In summary, this study provides valuable insights for further clinical development of one-component and multicomponent mRNA vaccine candidates for the prevention of MPXV and other orthomyxoviruses.
    MeSH term(s) Animals ; Mice ; Mpox (monkeypox) ; Antibodies, Neutralizing ; Vaccinia virus/genetics ; Immunity, Cellular ; RNA, Messenger/genetics ; Antibodies, Viral
    Chemical Substances Antibodies, Neutralizing ; RNA, Messenger ; Antibodies, Viral
    Language English
    Publishing date 2023-10-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 752392-0
    ISSN 1096-9071 ; 0146-6615
    ISSN (online) 1096-9071
    ISSN 0146-6615
    DOI 10.1002/jmv.29140
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