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  1. Artikel ; Online: Crystal structure of the ATPase domain of porcine circovirus type 2 Rep protein.

    Guan, Shuaiyin / Li, Zhen / Han, Yang / Tian, Ang / Zhou, Saisai / Chen, Huanchun / Peng, Guiqing / Song, Yunfeng

    The Journal of general virology

    2024  Band 105, Heft 3

    Abstract: PCV2 belongs to the ... ...

    Abstract PCV2 belongs to the genus
    Mesh-Begriff(e) Swine ; Animals ; Circovirus/genetics ; Adenosine Triphosphatases/genetics ; Crystallography, X-Ray ; DNA Helicases/genetics ; DNA Replication
    Chemische Substanzen Adenosine Triphosphatases (EC 3.6.1.-) ; DNA Helicases (EC 3.6.4.-)
    Sprache Englisch
    Erscheinungsdatum 2024-03-20
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 219316-4
    ISSN 1465-2099 ; 0022-1317
    ISSN (online) 1465-2099
    ISSN 0022-1317
    DOI 10.1099/jgv.0.001972
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Crystal structure of the dimerized of porcine circovirus type II replication-related protein Rep'.

    Guan, Shuaiyin / Tian, Ang / Jing, Haobo / Yuan, Honggen / Jia, Hanxiao / Shi, Yuejun / Chen, Huanchun / Cao, Shengbo / Peng, Guiqing / Song, Yunfeng

    Proteins

    2023  Band 91, Heft 8, Seite(n) 1130–1139

    Abstract: Porcine circovirus type 2 (PCV2) can cause porcine circovirus-associated disease (PCVAD), which causes significant economic losses to the global pig industry annually. There are no effective antiviral drugs used to control and treat PCV2, and prevention ... ...

    Abstract Porcine circovirus type 2 (PCV2) can cause porcine circovirus-associated disease (PCVAD), which causes significant economic losses to the global pig industry annually. There are no effective antiviral drugs used to control and treat PCV2, and prevention is mainly obtained through vaccination. PCV2 genome replicates through the rolling circle replication (RCR) mechanism involving Rep and Rep', so analyzing the holistic structure of Rep and Rep' will help us better understand the replication process of PCV2. However, there are no reports on the integral structure of Rep' and Rep, which seriously hinders the research of the viral replication. By using the x-ray diffraction method, the structure of the Rep' dimer was resolved by us in this study. Structural analysis revealed that Rep' is a dimer formed by the interaction of the C-terminal domain. The two Rep' form a positively charged groove, which may play an essential role in the viral binding of dsDNA. Together, this study help to understand the replication process of the virus and may also provide new insights into the development of antiviral drugs.
    Mesh-Begriff(e) Animals ; Swine ; Viral Proteins/chemistry ; Circovirus/genetics ; Circovirus/metabolism ; Virus Replication/genetics
    Chemische Substanzen Viral Proteins
    Sprache Englisch
    Erscheinungsdatum 2023-05-12
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 806683-8
    ISSN 1097-0134 ; 0887-3585
    ISSN (online) 1097-0134
    ISSN 0887-3585
    DOI 10.1002/prot.26498
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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