BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei

Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that i...
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Autor*in:	Riccardo Capelli [verfasserIn] Claudio Peri [verfasserIn] Riccardo Villa [verfasserIn] Arnone Nithichanon [verfasserIn] Oscar Conchillo-Solé [verfasserIn] Daniel Yero [verfasserIn] Paola Gagni [verfasserIn] Marcella Chiari [verfasserIn] Ganjana Lertmemongkolchai [verfasserIn] Marina Cretich [verfasserIn] Xavier Daura [verfasserIn] Martino Bolognesi [verfasserIn] Giorgio Colombo [verfasserIn] Louise J. Gourlay [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2018

Schlagwörter:	Burkholderia BPSL1626 antigen melioidosis reverse vaccinology crystal structure in silico epitope predictions type I fimbrial subunit

Übergeordnetes Werk:	In: Antibodies - MDPI AG, 2012, 7(2018), 3, p 26
Übergeordnetes Werk:	volume:7 ; year:2018 ; number:3, p 26

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/antib7030026

Katalog-ID:	DOAJ050682806

Internformat


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allfields	10.3390/antib7030026 doi (DE-627)DOAJ050682806 (DE-599)DOAJb688d07768414a0aa11920df4d580f3b DE-627 ger DE-627 rakwb eng RC581-607 Riccardo Capelli verfasserin aut BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 Å resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules. Burkholderia BPSL1626 antigen melioidosis reverse vaccinology crystal structure in silico epitope predictions type I fimbrial subunit Immunologic diseases. Allergy Claudio Peri verfasserin aut Riccardo Villa verfasserin aut Arnone Nithichanon verfasserin aut Oscar Conchillo-Solé verfasserin aut Daniel Yero verfasserin aut Paola Gagni verfasserin aut Marcella Chiari verfasserin aut Ganjana Lertmemongkolchai verfasserin aut Marina Cretich verfasserin aut Xavier Daura verfasserin aut Martino Bolognesi verfasserin aut Giorgio Colombo verfasserin aut Louise J. Gourlay verfasserin aut In Antibodies MDPI AG, 2012 7(2018), 3, p 26 (DE-627)718622065 (DE-600)2661514-9 20734468 nnns volume:7 year:2018 number:3, p 26 https://doi.org/10.3390/antib7030026 kostenfrei https://doaj.org/article/b688d07768414a0aa11920df4d580f3b kostenfrei http://www.mdpi.com/2073-4468/7/3/26 kostenfrei https://doaj.org/toc/2073-4468 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2018 3, p 26
spelling	10.3390/antib7030026 doi (DE-627)DOAJ050682806 (DE-599)DOAJb688d07768414a0aa11920df4d580f3b DE-627 ger DE-627 rakwb eng RC581-607 Riccardo Capelli verfasserin aut BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 Å resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules. Burkholderia BPSL1626 antigen melioidosis reverse vaccinology crystal structure in silico epitope predictions type I fimbrial subunit Immunologic diseases. Allergy Claudio Peri verfasserin aut Riccardo Villa verfasserin aut Arnone Nithichanon verfasserin aut Oscar Conchillo-Solé verfasserin aut Daniel Yero verfasserin aut Paola Gagni verfasserin aut Marcella Chiari verfasserin aut Ganjana Lertmemongkolchai verfasserin aut Marina Cretich verfasserin aut Xavier Daura verfasserin aut Martino Bolognesi verfasserin aut Giorgio Colombo verfasserin aut Louise J. Gourlay verfasserin aut In Antibodies MDPI AG, 2012 7(2018), 3, p 26 (DE-627)718622065 (DE-600)2661514-9 20734468 nnns volume:7 year:2018 number:3, p 26 https://doi.org/10.3390/antib7030026 kostenfrei https://doaj.org/article/b688d07768414a0aa11920df4d580f3b kostenfrei http://www.mdpi.com/2073-4468/7/3/26 kostenfrei https://doaj.org/toc/2073-4468 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2018 3, p 26
allfields_unstemmed	10.3390/antib7030026 doi (DE-627)DOAJ050682806 (DE-599)DOAJb688d07768414a0aa11920df4d580f3b DE-627 ger DE-627 rakwb eng RC581-607 Riccardo Capelli verfasserin aut BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 Å resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules. Burkholderia BPSL1626 antigen melioidosis reverse vaccinology crystal structure in silico epitope predictions type I fimbrial subunit Immunologic diseases. Allergy Claudio Peri verfasserin aut Riccardo Villa verfasserin aut Arnone Nithichanon verfasserin aut Oscar Conchillo-Solé verfasserin aut Daniel Yero verfasserin aut Paola Gagni verfasserin aut Marcella Chiari verfasserin aut Ganjana Lertmemongkolchai verfasserin aut Marina Cretich verfasserin aut Xavier Daura verfasserin aut Martino Bolognesi verfasserin aut Giorgio Colombo verfasserin aut Louise J. Gourlay verfasserin aut In Antibodies MDPI AG, 2012 7(2018), 3, p 26 (DE-627)718622065 (DE-600)2661514-9 20734468 nnns volume:7 year:2018 number:3, p 26 https://doi.org/10.3390/antib7030026 kostenfrei https://doaj.org/article/b688d07768414a0aa11920df4d580f3b kostenfrei http://www.mdpi.com/2073-4468/7/3/26 kostenfrei https://doaj.org/toc/2073-4468 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2018 3, p 26
allfieldsGer	10.3390/antib7030026 doi (DE-627)DOAJ050682806 (DE-599)DOAJb688d07768414a0aa11920df4d580f3b DE-627 ger DE-627 rakwb eng RC581-607 Riccardo Capelli verfasserin aut BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 Å resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules. Burkholderia BPSL1626 antigen melioidosis reverse vaccinology crystal structure in silico epitope predictions type I fimbrial subunit Immunologic diseases. Allergy Claudio Peri verfasserin aut Riccardo Villa verfasserin aut Arnone Nithichanon verfasserin aut Oscar Conchillo-Solé verfasserin aut Daniel Yero verfasserin aut Paola Gagni verfasserin aut Marcella Chiari verfasserin aut Ganjana Lertmemongkolchai verfasserin aut Marina Cretich verfasserin aut Xavier Daura verfasserin aut Martino Bolognesi verfasserin aut Giorgio Colombo verfasserin aut Louise J. Gourlay verfasserin aut In Antibodies MDPI AG, 2012 7(2018), 3, p 26 (DE-627)718622065 (DE-600)2661514-9 20734468 nnns volume:7 year:2018 number:3, p 26 https://doi.org/10.3390/antib7030026 kostenfrei https://doaj.org/article/b688d07768414a0aa11920df4d580f3b kostenfrei http://www.mdpi.com/2073-4468/7/3/26 kostenfrei https://doaj.org/toc/2073-4468 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2018 3, p 26
allfieldsSound	10.3390/antib7030026 doi (DE-627)DOAJ050682806 (DE-599)DOAJb688d07768414a0aa11920df4d580f3b DE-627 ger DE-627 rakwb eng RC581-607 Riccardo Capelli verfasserin aut BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 Å resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules. Burkholderia BPSL1626 antigen melioidosis reverse vaccinology crystal structure in silico epitope predictions type I fimbrial subunit Immunologic diseases. Allergy Claudio Peri verfasserin aut Riccardo Villa verfasserin aut Arnone Nithichanon verfasserin aut Oscar Conchillo-Solé verfasserin aut Daniel Yero verfasserin aut Paola Gagni verfasserin aut Marcella Chiari verfasserin aut Ganjana Lertmemongkolchai verfasserin aut Marina Cretich verfasserin aut Xavier Daura verfasserin aut Martino Bolognesi verfasserin aut Giorgio Colombo verfasserin aut Louise J. Gourlay verfasserin aut In Antibodies MDPI AG, 2012 7(2018), 3, p 26 (DE-627)718622065 (DE-600)2661514-9 20734468 nnns volume:7 year:2018 number:3, p 26 https://doi.org/10.3390/antib7030026 kostenfrei https://doaj.org/article/b688d07768414a0aa11920df4d580f3b kostenfrei http://www.mdpi.com/2073-4468/7/3/26 kostenfrei https://doaj.org/toc/2073-4468 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 7 2018 3, p 26
language	English
source	In Antibodies 7(2018), 3, p 26 volume:7 year:2018 number:3, p 26
sourceStr	In Antibodies 7(2018), 3, p 26 volume:7 year:2018 number:3, p 26
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Burkholderia BPSL1626 antigen melioidosis reverse vaccinology crystal structure in silico epitope predictions type I fimbrial subunit Immunologic diseases. Allergy
isfreeaccess_bool	true
container_title	Antibodies
authorswithroles_txt_mv	Riccardo Capelli @@aut@@ Claudio Peri @@aut@@ Riccardo Villa @@aut@@ Arnone Nithichanon @@aut@@ Oscar Conchillo-Solé @@aut@@ Daniel Yero @@aut@@ Paola Gagni @@aut@@ Marcella Chiari @@aut@@ Ganjana Lertmemongkolchai @@aut@@ Marina Cretich @@aut@@ Xavier Daura @@aut@@ Martino Bolognesi @@aut@@ Giorgio Colombo @@aut@@ Louise J. Gourlay @@aut@@
publishDateDaySort_date	2018-01-01T00:00:00Z
hierarchy_top_id	718622065
id	DOAJ050682806
language_de	englisch
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callnumber-first	R - Medicine
author	Riccardo Capelli
spellingShingle	Riccardo Capelli misc RC581-607 misc Burkholderia misc BPSL1626 antigen misc melioidosis misc reverse vaccinology misc crystal structure misc in silico epitope predictions misc type I fimbrial subunit misc Immunologic diseases. Allergy BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei
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topic_title	RC581-607 BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei Burkholderia BPSL1626 antigen melioidosis reverse vaccinology crystal structure in silico epitope predictions type I fimbrial subunit
topic	misc RC581-607 misc Burkholderia misc BPSL1626 antigen misc melioidosis misc reverse vaccinology misc crystal structure misc in silico epitope predictions misc type I fimbrial subunit misc Immunologic diseases. Allergy
topic_unstemmed	misc RC581-607 misc Burkholderia misc BPSL1626 antigen misc melioidosis misc reverse vaccinology misc crystal structure misc in silico epitope predictions misc type I fimbrial subunit misc Immunologic diseases. Allergy
topic_browse	misc RC581-607 misc Burkholderia misc BPSL1626 antigen misc melioidosis misc reverse vaccinology misc crystal structure misc in silico epitope predictions misc type I fimbrial subunit misc Immunologic diseases. Allergy
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title	BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei
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title_full	BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei
author_sort	Riccardo Capelli
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author_browse	Riccardo Capelli Claudio Peri Riccardo Villa Arnone Nithichanon Oscar Conchillo-Solé Daniel Yero Paola Gagni Marcella Chiari Ganjana Lertmemongkolchai Marina Cretich Xavier Daura Martino Bolognesi Giorgio Colombo Louise J. Gourlay
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title_sort	bpsl1626: reverse and structural vaccinology reveal a novel candidate for vaccine design against burkholderia pseudomallei
callnumber	RC581-607
title_auth	BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei
abstract	Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 Å resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules.
abstractGer	Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 Å resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules.
abstract_unstemmed	Due to significant advances in computational biology, protein prediction, together with antigen and epitope design, have rapidly moved from conventional methods, based on experimental approaches, to in silico-based bioinformatics methods. In this context, we report a reverse vaccinology study that identified a panel of 104 candidate antigens from the Gram-negative bacterial pathogen Burkholderia pseudomallei, which is responsible for the disease melioidosis. B. pseudomallei can cause fatal sepsis in endemic populations in the tropical regions of the world and treatment with antibiotics is mostly ineffective. With the aim of identifying potential vaccine candidates, we report the experimental validation of predicted antigen and type I fimbrial subunit, BPSL1626, which we show is able to recognize and bind human antibodies from the sera of Burkholderia infected patients and to stimulate T-lymphocytes in vitro. The prerequisite for a melioidosis vaccine, in fact, is that both antibody- and cell-mediated immune responses must be triggered. In order to reveal potential antigenic regions of the protein that may aid immunogen re-design, we also report the crystal structure of BPSL1626 at 1.9 Å resolution on which structure-based epitope predictions were based. Overall, our data suggest that BPSL1626 and three epitope regions here-identified can represent viable candidates as potential antigenic molecules.
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container_issue	3, p 26
title_short	BPSL1626: Reverse and Structural Vaccinology Reveal a Novel Candidate for Vaccine Design Against Burkholderia pseudomallei
url	https://doi.org/10.3390/antib7030026 https://doaj.org/article/b688d07768414a0aa11920df4d580f3b http://www.mdpi.com/2073-4468/7/3/26 https://doaj.org/toc/2073-4468
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author2Str	Claudio Peri Riccardo Villa Arnone Nithichanon Oscar Conchillo-Solé Daniel Yero Paola Gagni Marcella Chiari Ganjana Lertmemongkolchai Marina Cretich Xavier Daura Martino Bolognesi Giorgio Colombo Louise J. Gourlay
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up_date	2024-07-03T16:11:29.521Z
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