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  1. Article ; Online: Encapsidated-CpG ODN Enhances Immunogenicity of Porcine Circovirus Type 2 Virus-like Particles

    Hansoongnern, Payuda / Phecharat, Nantawan / Wasanasuk, Ketkaew / Tommeurd, Wantanee / Chankeeree, Penpitcha / Lekcharoensuk, Chalermpol / Semkum, Ploypailin / Pinitkiatisakul, Sunan / Lekcharoensuk, Porntippa

    Veterinary Microbiology. 2022 Oct. 15, p.109583-

    2022  , Page(s) 109583–

    Abstract: A DNA fragment containing CpG motifs (CpG ODN) is one of the potent immunopotentiators used to improve vaccine efficacy. It can enhance a protective immunity by stimulating both innate and adaptive immune responses. In this study, we designed and ... ...

    Abstract A DNA fragment containing CpG motifs (CpG ODN) is one of the potent immunopotentiators used to improve vaccine efficacy. It can enhance a protective immunity by stimulating both innate and adaptive immune responses. In this study, we designed and constructed a recombinant plasmid carrying the combined CpG ODN to generate an immunopotentiator for boosting the immunogenicity of porcine circovirus type 2 (PCV2) virus-like particles (VLPs). The capsid protein of PCV2b was expressed in insect cells and purified by affinity chromatography. The purified capsid protein was incubated with the CpG ODN in the reaction that allowed VLPs formation and encapsidation of the CpG ODN to occur simultaneously. Morphology of the reassembled VLPs was similar to the PCV2 virions as observed using an electron microscope. When the CpG ODN-encapcidated VLPs was treated with DNase I, the VLPs could protect the packaged CpG ODN from the enzyme digestion. Moreover, we immunized mice subcutaneously with VLPs, CpG ODN-loaded VLPs, or phosphate buffer saline for three times at two-week intervals. The results showed that the CpG ODN-loaded VLPs could elicit significantly higher levels of PCV2-specific neutralizing antibodies and interferon gamma (IFN-γ) expression in the immunized mice compared to those conferred by the VLPs alone. Conclusively, we have proved that the CpG ODN incorporated in VLPs can serve as a potent immunopotentiator for PCV2 vaccine development.
    Keywords DNA fragmentation ; Porcine circovirus-2 ; affinity chromatography ; coat proteins ; deoxyribonucleases ; enzymatic reactions ; immunogenicity ; immunostimulants ; insects ; interferon-gamma ; microbiology ; oligodeoxyribonucleotides ; phosphates ; plasmids ; vaccine development ; vaccines ; CpG ODN ; PCV2 ; virus-like particles ; subunit vaccine ; immunization
    Language English
    Dates of publication 2022-1015
    Publishing place Elsevier B.V.
    Document type Article ; Online
    Note Pre-press version ; Use and reproduction
    ZDB-ID 753154-0
    ISSN 1873-2542 ; 0378-1135
    ISSN (online) 1873-2542
    ISSN 0378-1135
    DOI 10.1016/j.vetmic.2022.109583
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2917: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article ; Online: Encapsidated-CpG ODN enhances immunogenicity of porcine circovirus type 2 virus-like particles.

    Hansoongnern, Payuda / Phecharat, Nantawan / Wasanasuk, Ketkaew / Tommeurd, Wantanee / Chankeeree, Penpitcha / Lekcharoensuk, Chalermpol / Semkum, Ploypailin / Pinitkiatisakul, Sunan / Lekcharoensuk, Porntippa

    Veterinary microbiology

    2022  Volume 275, Page(s) 109583

    Abstract: A DNA fragment containing CpG motifs (CpG ODN) is one of the potent immunopotentiators used to improve vaccine efficacy. It can enhance a protective immunity by stimulating both innate and adaptive immune responses. In this study, we designed and ... ...

    Abstract A DNA fragment containing CpG motifs (CpG ODN) is one of the potent immunopotentiators used to improve vaccine efficacy. It can enhance a protective immunity by stimulating both innate and adaptive immune responses. In this study, we designed and constructed a recombinant plasmid carrying the combined CpG ODN to generate an immunopotentiator for boosting the immunogenicity of porcine circovirus type 2 (PCV2) virus-like particles (VLPs). The capsid protein of PCV2b was expressed in insect cells and purified by affinity chromatography. The purified capsid protein was incubated with the CpG ODN in the reaction that allowed VLPs formation and encapsidation of the CpG ODN to occur simultaneously. Morphology of the reassembled VLPs was similar to the PCV2 virions as observed using an electron microscope. When the CpG ODN-encapcidated VLPs was treated with DNase I, the VLPs could protect the packaged CpG ODN from the enzyme digestion. Moreover, we immunized mice subcutaneously with VLPs, CpG ODN-loaded VLPs, or phosphate buffer saline for three times at two-week intervals. The results showed that the CpG ODN-loaded VLPs could elicit significantly higher levels of PCV2-specific neutralizing antibodies and interferon gamma (IFN-γ) expression in the immunized mice compared to those conferred by the VLPs alone. Conclusively, we have proved that the CpG ODN incorporated in VLPs can serve as a potent immunopotentiator for PCV2 vaccine development.
    MeSH term(s) Animals ; Mice ; Adjuvants, Immunologic ; Antibodies, Viral ; Capsid Proteins ; Circoviridae Infections/prevention & control ; Circoviridae Infections/veterinary ; Circovirus ; Swine ; Swine Diseases/prevention & control ; Swine Diseases/virology ; Viral Vaccines ; CpG Islands
    Chemical Substances Adjuvants, Immunologic ; Antibodies, Viral ; Capsid Proteins ; Viral Vaccines
    Language English
    Publishing date 2022-10-18
    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.2022.109583
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2917: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  3. Article: The immunogenicity of the secretory GΔTM protein of bovine ephemeral fever virus stably expressed by mammalian cells

    Hansoongnern, Payuda / Kaewborisuth, Challika / Wasanasuk, Ketkaew / Chankeeree, Penpitcha / Poonsuk, Sukontip / Lekcharoensuk, Chalermpol / Lekcharoensuk, Porntippa

    Veterinary microbiology. 2019 June, v. 233

    2019  

    Abstract: Bovine ephemeral fever virus (BEFV) causes an acute febrile disease in cattle and water buffalo. The disease has an impact on dairy and beef production in tropical and subtropical countries. Vaccination is used for disease prevention and control. In this ...

    Abstract Bovine ephemeral fever virus (BEFV) causes an acute febrile disease in cattle and water buffalo. The disease has an impact on dairy and beef production in tropical and subtropical countries. Vaccination is used for disease prevention and control. In this study, we developed a recombinant lentivirus to produce mammalian stable cells expressing histidine-tagged BEFV G protein with a deleted transmembrane domain (GΔTM) as a secretory protein. In addition, guinea pigs were immunised with the purified GΔTM protein and booster immunised at a 3-week interval. The mammalian stable cells were able to continuously produce GΔTM protein for a minimum of 25 passages. All of the mammalian stable cells expressing GΔTM protein could react specifically with a BEFV convalescent bovine serum. Serum samples from the immunised guinea pigs could react strongly and specifically with the purified GΔTM protein. Moreover, post-immunised guinea pig sera contained antibodies that could neutralise BEFV. These results indicate that the G protein without a transmembrane domain can be used as a subunit vaccine for the prevention and control of BEFV. The availability of the mammalian stable cells, which constitutively express GΔTM protein, could facilitate the potential use of the secretory protein for BEFV diagnosis and vaccine development.
    Keywords Bovine ephemeral fever virus ; G-proteins ; Lentivirus ; antibodies ; beef cattle ; beef production ; blood serum ; buffaloes ; cattle diseases ; disease prevention ; guinea pigs ; immunogenicity ; milk production ; neutralization ; subunit vaccines ; vaccination ; vaccine development
    Language English
    Dates of publication 2019-06
    Size p. 113-117.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 753154-0
    ISSN 1873-2542 ; 0378-1135
    ISSN (online) 1873-2542
    ISSN 0378-1135
    DOI 10.1016/j.vetmic.2019.04.032
    Database NAL-Catalogue (AGRICOLA)

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2917: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article ; Online: The immunogenicity of the secretory GΔTM protein of bovine ephemeral fever virus stably expressed by mammalian cells.

    Hansoongnern, Payuda / Kaewborisuth, Challika / Wasanasuk, Ketkaew / Chankeeree, Penpitcha / Poonsuk, Sukontip / Lekcharoensuk, Chalermpol / Lekcharoensuk, Porntippa

    Veterinary microbiology

    2019  Volume 233, Page(s) 113–117

    Abstract: Bovine ephemeral fever virus (BEFV) causes an acute febrile disease in cattle and water buffalo. The disease has an impact on dairy and beef production in tropical and subtropical countries. Vaccination is used for disease prevention and control. In this ...

    Abstract Bovine ephemeral fever virus (BEFV) causes an acute febrile disease in cattle and water buffalo. The disease has an impact on dairy and beef production in tropical and subtropical countries. Vaccination is used for disease prevention and control. In this study, we developed a recombinant lentivirus to produce mammalian stable cells expressing histidine-tagged BEFV G protein with a deleted transmembrane domain (GΔTM) as a secretory protein. In addition, guinea pigs were immunised with the purified GΔTM protein and booster immunised at a 3-week interval. The mammalian stable cells were able to continuously produce GΔTM protein for a minimum of 25 passages. All of the mammalian stable cells expressing GΔTM protein could react specifically with a BEFV convalescent bovine serum. Serum samples from the immunised guinea pigs could react strongly and specifically with the purified GΔTM protein. Moreover, post-immunised guinea pig sera contained antibodies that could neutralise BEFV. These results indicate that the G protein without a transmembrane domain can be used as a subunit vaccine for the prevention and control of BEFV. The availability of the mammalian stable cells, which constitutively express GΔTM protein, could facilitate the potential use of the secretory protein for BEFV diagnosis and vaccine development.
    MeSH term(s) Animals ; Antibodies, Neutralizing/blood ; Antibodies, Viral/blood ; Cattle ; Cell Line ; Ephemeral Fever/immunology ; Ephemeral Fever/prevention & control ; Ephemeral Fever Virus, Bovine ; Female ; Glycoproteins/genetics ; Glycoproteins/immunology ; Guinea Pigs ; HEK293 Cells ; Humans ; Immunogenicity, Vaccine ; Transfection ; Vaccination ; Viral Proteins/genetics ; Viral Proteins/immunology ; Viral Vaccines/immunology
    Chemical Substances Antibodies, Neutralizing ; Antibodies, Viral ; Glycoproteins ; Viral Proteins ; Viral Vaccines ; BEFV G protein, Bovine ephemeral fever virus (148770-53-0)
    Language English
    Publishing date 2019-04-28
    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.2019.04.032
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 2917: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

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