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Parlane NA, Compton BJ, Hayman CM, Painter GF, Basaraba RJ, Heiser A, Buddle BM
Phosphatidylinositol di-mannoside and derivates modulate the immune response to and efficacy of a tuberculosis protein vaccine against Mycobacterium bovis infection
Vaccine 30(3) (2012)
580-588
|
a-D-Manp-(1-6)-+ Pam-(1-2)-+
| |
a-D-Manp-(1-2)-L-myoIno-(1--P--3)--D-Gro-(1-1)-Pam |
Show graphically |
Mycobacterium bovis
(later renamed to: Mycobacterium tuberculosis var. bovis)
(NCBI TaxID 1765,
species name lookup)
Taxonomic group: bacteria / Actinobacteria
(Phylum: Actinobacteria)
Associated disease: infection due to Mycobacterium bovis [ICD11:
XN8AB 
];
infection due to Mycobacterium tuberculosis [ICD11:
XN1N2 ]
NCBI PubMed ID: 22120192Publication DOI: 10.1016/j.vaccine.2011.11.055Journal NLM ID: 8406899Publisher: Elsevier
Correspondence: bryce.buddle
agresearch.co.nz
Institutions: AgResearch, Hopkirk Research Institute, Grasslands Research Centre, Palmerston North, New Zealand, Carbohydrate Chemistry Team, Industrial Research Limited, Lower Hutt, New Zealand, Department of Microbiology, Immunology & Pathology, Colorado State University, Fort Collins, USA
Mycobacterium bovis infects a wide range of hosts, including domestic livestock, wildlife, and humans. Development of an effective vaccine protecting against bovine tuberculosis would provide a cost-effective tuberculosis control strategy. The objective of this study was to investigate the ability of phosphatidylinositol di-mannoside (PIM(2)) and its derivatives to modulate cell-mediated immunity in vivo in a bovine tuberculosis mouse model in response to a relevant antigen, namely a fusion protein of mycobacterial proteins Ag85A and ESAT-6. The addition of synthetic PIM(2) to the vaccine resulted in a significant reduction in lung bacterial counts and a cytokine profile indicating a Th 1 type immune response. The addition of the other PIM(2) derivatives to the vaccine or the fusion protein alone did not result in reduced lung bacterial counts; moreover, the addition of PIM(2)ME appeared to negate the induction of an antigen-specific interferon-γ response and protection against tuberculosis. In conclusion, this study provides further evidence that PIMs can function as potent adjuvants for protein or sub-unit vaccines, but subtle structural differences among PIMs can markedly alter the type of immune response induced.
vaccine, tuberculosis, cattle, Mycobacterium bovis, phosphatidylinositol mannoside
Structure type: oligomer
Location inside paper: Fig.1, PIM2
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_141181,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72
Methods: ELISA, biological assays, extraction, chromatography, measurement of cytokines, hydrogenolysis
Biological activity: Ag:ES + PIM2 had the lowest mean lung bacterial counts, indicating an association between reduced lung bacterial counts and reduced lung pathology.
Related record ID(s): 45706, 45707, 45708
NCBI Taxonomy refs (TaxIDs): 1765
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There is only one chemically distinct structure:
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Parlane NA, Compton BJ, Hayman CM, Painter GF, Basaraba RJ, Heiser A, Buddle BM
Phosphatidylinositol di-mannoside and derivates modulate the immune response to and efficacy of a tuberculosis protein vaccine against Mycobacterium bovis infection
Vaccine 30(3) (2012)
580-588
|
Pam-(1-2)-+
|
a-D-Manp-(1-3)-+ |
| |
a-D-Manp-(1-2)-D-Gro-(1-3)-D-Gro-(1-1)-Pam |
Show graphically |
Mycobacterium bovis
(later renamed to: Mycobacterium tuberculosis var. bovis)
(NCBI TaxID 1765,
species name lookup)
Taxonomic group: bacteria / Actinobacteria
(Phylum: Actinobacteria)
Associated disease: infection due to Mycobacterium bovis [ICD11:
XN8AB ];
infection due to Mycobacterium tuberculosis [ICD11:
XN1N2 ]
NCBI PubMed ID: 22120192Publication DOI: 10.1016/j.vaccine.2011.11.055Journal NLM ID: 8406899Publisher: Elsevier
Correspondence: bryce.buddle
agresearch.co.nz
Institutions: AgResearch, Hopkirk Research Institute, Grasslands Research Centre, Palmerston North, New Zealand, Carbohydrate Chemistry Team, Industrial Research Limited, Lower Hutt, New Zealand, Department of Microbiology, Immunology & Pathology, Colorado State University, Fort Collins, USA
Mycobacterium bovis infects a wide range of hosts, including domestic livestock, wildlife, and humans. Development of an effective vaccine protecting against bovine tuberculosis would provide a cost-effective tuberculosis control strategy. The objective of this study was to investigate the ability of phosphatidylinositol di-mannoside (PIM(2)) and its derivatives to modulate cell-mediated immunity in vivo in a bovine tuberculosis mouse model in response to a relevant antigen, namely a fusion protein of mycobacterial proteins Ag85A and ESAT-6. The addition of synthetic PIM(2) to the vaccine resulted in a significant reduction in lung bacterial counts and a cytokine profile indicating a Th 1 type immune response. The addition of the other PIM(2) derivatives to the vaccine or the fusion protein alone did not result in reduced lung bacterial counts; moreover, the addition of PIM(2)ME appeared to negate the induction of an antigen-specific interferon-γ response and protection against tuberculosis. In conclusion, this study provides further evidence that PIMs can function as potent adjuvants for protein or sub-unit vaccines, but subtle structural differences among PIMs can markedly alter the type of immune response induced.
vaccine, tuberculosis, cattle, Mycobacterium bovis, phosphatidylinositol mannoside
Structure type: oligomer
Location inside paper: Fig.1, PGM2
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_141181,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72
Methods: ELISA, biological assays, extraction, chromatography, measurement of cytokines, hydrogenolysis
Biological activity: The mean IgG1 titer for Ag:ES + PGM2 was significantly greater than that for Ag:ES + PIM2 post vaccination.
Related record ID(s): 45705, 45707, 45708
NCBI Taxonomy refs (TaxIDs): 1765
Show glycosyltransferases
There is only one chemically distinct structure:
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Parlane NA, Compton BJ, Hayman CM, Painter GF, Basaraba RJ, Heiser A, Buddle BM
Phosphatidylinositol di-mannoside and derivates modulate the immune response to and efficacy of a tuberculosis protein vaccine against Mycobacterium bovis infection
Vaccine 30(3) (2012)
580-588
|
a-D-Manp-(1-6)-+ Pam-(1-2)-+
| |
Pam-(1-6)-a-D-Manp-(1-2)-L-myoIno-(1--P--3)--D-Gro-(1-1)-C19 |
Show graphically |
Mycobacterium bovis
(later renamed to: Mycobacterium tuberculosis var. bovis)
(NCBI TaxID 1765,
species name lookup)
Taxonomic group: bacteria / Actinobacteria
(Phylum: Actinobacteria)
Associated disease: infection due to Mycobacterium bovis [ICD11:
XN8AB ];
infection due to Mycobacterium tuberculosis [ICD11:
XN1N2 ]
NCBI PubMed ID: 22120192Publication DOI: 10.1016/j.vaccine.2011.11.055Journal NLM ID: 8406899Publisher: Elsevier
Correspondence: bryce.buddle
agresearch.co.nz
Institutions: AgResearch, Hopkirk Research Institute, Grasslands Research Centre, Palmerston North, New Zealand, Carbohydrate Chemistry Team, Industrial Research Limited, Lower Hutt, New Zealand, Department of Microbiology, Immunology & Pathology, Colorado State University, Fort Collins, USA
Mycobacterium bovis infects a wide range of hosts, including domestic livestock, wildlife, and humans. Development of an effective vaccine protecting against bovine tuberculosis would provide a cost-effective tuberculosis control strategy. The objective of this study was to investigate the ability of phosphatidylinositol di-mannoside (PIM(2)) and its derivatives to modulate cell-mediated immunity in vivo in a bovine tuberculosis mouse model in response to a relevant antigen, namely a fusion protein of mycobacterial proteins Ag85A and ESAT-6. The addition of synthetic PIM(2) to the vaccine resulted in a significant reduction in lung bacterial counts and a cytokine profile indicating a Th 1 type immune response. The addition of the other PIM(2) derivatives to the vaccine or the fusion protein alone did not result in reduced lung bacterial counts; moreover, the addition of PIM(2)ME appeared to negate the induction of an antigen-specific interferon-γ response and protection against tuberculosis. In conclusion, this study provides further evidence that PIMs can function as potent adjuvants for protein or sub-unit vaccines, but subtle structural differences among PIMs can markedly alter the type of immune response induced.
vaccine, tuberculosis, cattle, Mycobacterium bovis, phosphatidylinositol mannoside
Structure type: oligomer
Location inside paper: Fig.1, AcPIM2
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_141181,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72
Methods: ELISA, biological assays, extraction, chromatography, measurement of cytokines, hydrogenolysis
Biological activity: AcPIM2 offered no advantage as compared to PIM2 for promoting protective immune response against TB.
Related record ID(s): 45705, 45706, 45708
NCBI Taxonomy refs (TaxIDs): 1765
Show glycosyltransferases
There is only one chemically distinct structure:
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Parlane NA, Compton BJ, Hayman CM, Painter GF, Basaraba RJ, Heiser A, Buddle BM
Phosphatidylinositol di-mannoside and derivates modulate the immune response to and efficacy of a tuberculosis protein vaccine against Mycobacterium bovis infection
Vaccine 30(3) (2012)
580-588
|
a-D-Manp-(1-6)-+ Subst-(1-2)-+
| |
a-D-Manp-(1-2)-L-myoIno-(1--P--3)--D-Gro-(1-1)-Pam
Subst = hexadecanol = SMILES CCCCCCCCCCCCCCC{1}CO |
Show graphically |
Mycobacterium bovis
(later renamed to: Mycobacterium tuberculosis var. bovis)
(NCBI TaxID 1765,
species name lookup)
Taxonomic group: bacteria / Actinobacteria
(Phylum: Actinobacteria)
Associated disease: infection due to Mycobacterium bovis [ICD11:
XN8AB ];
infection due to Mycobacterium tuberculosis [ICD11:
XN1N2 ]
NCBI PubMed ID: 22120192Publication DOI: 10.1016/j.vaccine.2011.11.055Journal NLM ID: 8406899Publisher: Elsevier
Correspondence: bryce.buddle
agresearch.co.nz
Institutions: AgResearch, Hopkirk Research Institute, Grasslands Research Centre, Palmerston North, New Zealand, Carbohydrate Chemistry Team, Industrial Research Limited, Lower Hutt, New Zealand, Department of Microbiology, Immunology & Pathology, Colorado State University, Fort Collins, USA
Mycobacterium bovis infects a wide range of hosts, including domestic livestock, wildlife, and humans. Development of an effective vaccine protecting against bovine tuberculosis would provide a cost-effective tuberculosis control strategy. The objective of this study was to investigate the ability of phosphatidylinositol di-mannoside (PIM(2)) and its derivatives to modulate cell-mediated immunity in vivo in a bovine tuberculosis mouse model in response to a relevant antigen, namely a fusion protein of mycobacterial proteins Ag85A and ESAT-6. The addition of synthetic PIM(2) to the vaccine resulted in a significant reduction in lung bacterial counts and a cytokine profile indicating a Th 1 type immune response. The addition of the other PIM(2) derivatives to the vaccine or the fusion protein alone did not result in reduced lung bacterial counts; moreover, the addition of PIM(2)ME appeared to negate the induction of an antigen-specific interferon-γ response and protection against tuberculosis. In conclusion, this study provides further evidence that PIMs can function as potent adjuvants for protein or sub-unit vaccines, but subtle structural differences among PIMs can markedly alter the type of immune response induced.
vaccine, tuberculosis, cattle, Mycobacterium bovis, phosphatidylinositol mannoside
Structure type: oligomer
Location inside paper: Fig.1, PIM2Me
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130701,IEDB_141181,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72
Methods: ELISA, biological assays, extraction, chromatography, measurement of cytokines, hydrogenolysis
Biological activity: The Ag:ES + PIM2ME group had significantly higher mean lung and spleen bacterial counts than the Ag:ES + PIM2 group and clearly lower, although not statistically significant, mean antigenspecific IFN-γ response, However, the mean antigen-specific IFN-γ response for the Ag:ES + PIM2ME group was significantly lower than that for the AgES + n.e.PIM2.
Related record ID(s): 45705, 45706, 45707
NCBI Taxonomy refs (TaxIDs): 1765
Show glycosyltransferases
There is only one chemically distinct structure:
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