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Toledo MS, Tagliari L, Suzuki E, Silva CM, Straus AH, Takahashi HK
Effect of anti-glycosphingolipid monoclonal antibodies in pathogenic fungal growth and differentiation. Characterization of monoclonal antibody MEST-3 directed to Manp α1→3Manp α1→2IPC
BMC Microbiology 10 (2010)
47
Paracoccidioides brasiliensis Pb18
(NCBI TaxID 502780,
species name lookup)
Sporothrix schenckii 65
(Ancestor NCBI TaxID 29908,
species name lookup)
Histoplasma capsulatum 496
(Ancestor NCBI TaxID 5037,
species name lookup)
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: yeast,
myceliumAssociated disease: infection due to Paracoccidioides brasiliensis [ICD11:
XN5UX 
];
infection due to Sporothrix schenckii [ICD11:
XN6GM 
];
infection due to Histoplasma capsulatum [ICD11:
XN8VH 
]
NCBI PubMed ID: 20156351Publication DOI: 10.1186/1471-2180-10-47Journal NLM ID: 100966981Publisher: Biomed Central
Correspondence: takahashi.bioq

epm.br
Institutions: Division of Glycoconjugate Immunochemistry, Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, São Paulo, SP, Brazil
Background Studies carried out during the 1990's demonstrated the presence of fungal glycoinositol phosphorylceramides (GIPCs) with unique structures, some of them showed reactivity with sera of patients with histoplasmosis, paracoccidioidomycosis or aspergillosis. It was also observed that fungal GIPCs were able to inhibit T lymphocyte proliferation "in vitro", and studies regarding the importance of these molecules to fungal survival showed that many species of fungi are vulnerable to inhibitors of sphingolipid biosynthesis. Results In this paper, we describe a detailed characterization of an IgG2a monoclonal antibody (mAb), termed MEST-3, directed to the Paracoccidioides brasiliensis glycolipid antigen Pb-2 (Manp α1→3Manp α1→2IPC). mAb MEST-3 also recognizes GIPCs bearing the same structure in other fungi. Studies performed on fungal cultures clearly showed the strong inhibitory activity of MEST-3 on differentiation and colony formation of Paracoccidioides brasiliensis, Histoplasma capsulatum and Sporothrix schenckii. Similar inhibitory results were observed when these fungi where incubated with a different mAb, which recognizes GIPCs bearing terminal residues of β-D-galactofuranose linked to mannose (mAb MEST-1). On the other hand, mAb MEST-2 specifically directed to fungal glucosylceramide (GlcCer) was able to promote only a weak inhibition on fungal differentiation and colony formation. Conclusions These results strongly suggest that mAbs directed to specific glycosphingolipids are able to interfere on fungal growth and differentiation. Thus, studies on surface distribution of GIPCs in yeast and mycelium forms of fungi may yield valuable information regarding the relevance of glycosphingolipids in processes of fungal growth, morphological transition and infectivity.
monoclonal antibodies, Paracoccidioides brasiliensis, monoclonal antibody MEST-3, glycosylinositol
Structure type: oligomer
Location inside paper: abstract, table 1, Pb-2
Compound class: glycosphingolipid, glycoinositolphosphoryl ceramide (GIPC)
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_44,SB_67,SB_72
Methods: periodate oxidation, ELISA, serological methods, genetic methods, UV, extraction, HPTLC, binding assays, immunofluorescence analyses, dialysis, fungal differentiation
Biological activity: mAb MEST-3 recognized glycolipid antigen Pb-2
Comments, role: GIPCs was extracted from mycelium forms of P. brasiliensis and from yeast forms of P. brasiliensis, S. schenckii and H. capsulatum.
Related record ID(s): 41946, 42155, 42156
NCBI Taxonomy refs (TaxIDs): 502780,
29908,
5037
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There is only one chemically distinct structure:
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Toledo MS, Tagliari L, Suzuki E, Silva CM, Straus AH, Takahashi HK
Effect of anti-glycosphingolipid monoclonal antibodies in pathogenic fungal growth and differentiation. Characterization of monoclonal antibody MEST-3 directed to Manp α1→3Manp α1→2IPC
BMC Microbiology 10 (2010)
47
Sporothrix schenckii 65
(Ancestor NCBI TaxID 29908,
species name lookup)
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: myceliumAssociated disease: infection due to Sporothrix schenckii [ICD11:
XN6GM 
]
NCBI PubMed ID: 20156351Publication DOI: 10.1186/1471-2180-10-47Journal NLM ID: 100966981Publisher: Biomed Central
Correspondence: takahashi.bioq

epm.br
Institutions: Division of Glycoconjugate Immunochemistry, Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, São Paulo, SP, Brazil
Background Studies carried out during the 1990's demonstrated the presence of fungal glycoinositol phosphorylceramides (GIPCs) with unique structures, some of them showed reactivity with sera of patients with histoplasmosis, paracoccidioidomycosis or aspergillosis. It was also observed that fungal GIPCs were able to inhibit T lymphocyte proliferation "in vitro", and studies regarding the importance of these molecules to fungal survival showed that many species of fungi are vulnerable to inhibitors of sphingolipid biosynthesis. Results In this paper, we describe a detailed characterization of an IgG2a monoclonal antibody (mAb), termed MEST-3, directed to the Paracoccidioides brasiliensis glycolipid antigen Pb-2 (Manp α1→3Manp α1→2IPC). mAb MEST-3 also recognizes GIPCs bearing the same structure in other fungi. Studies performed on fungal cultures clearly showed the strong inhibitory activity of MEST-3 on differentiation and colony formation of Paracoccidioides brasiliensis, Histoplasma capsulatum and Sporothrix schenckii. Similar inhibitory results were observed when these fungi where incubated with a different mAb, which recognizes GIPCs bearing terminal residues of β-D-galactofuranose linked to mannose (mAb MEST-1). On the other hand, mAb MEST-2 specifically directed to fungal glucosylceramide (GlcCer) was able to promote only a weak inhibition on fungal differentiation and colony formation. Conclusions These results strongly suggest that mAbs directed to specific glycosphingolipids are able to interfere on fungal growth and differentiation. Thus, studies on surface distribution of GIPCs in yeast and mycelium forms of fungi may yield valuable information regarding the relevance of glycosphingolipids in processes of fungal growth, morphological transition and infectivity.
monoclonal antibodies, Paracoccidioides brasiliensis, monoclonal antibody MEST-3, glycosylinositol
Structure type: oligomer
Location inside paper: Ss-M2, fig.2
Compound class: glycosphingolipid, glycoinositolphosphoryl ceramide (GIPC)
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_152206,IEDB_164174,IEDB_983930,SB_197,SB_44,SB_67,SB_72
Methods: periodate oxidation, ELISA, serological methods, genetic methods, UV, extraction, HPTLC, binding assays, immunofluorescence analyses, dialysis, fungal differentiation
Biological activity: Glycosylinositol was not able to inhibit MEST-3 binding to Pb-2.
Comments, role: Glycosylinositol derived from Ss-M2 of mycelium forms of S. schenckii.
Related record ID(s): 41721, 42155, 42156
NCBI Taxonomy refs (TaxIDs): 29908
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There is only one chemically distinct structure:
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Toledo MS, Tagliari L, Suzuki E, Silva CM, Straus AH, Takahashi HK
Effect of anti-glycosphingolipid monoclonal antibodies in pathogenic fungal growth and differentiation. Characterization of monoclonal antibody MEST-3 directed to Manp α1→3Manp α1→2IPC
BMC Microbiology 10 (2010)
47
Paracoccidioides brasiliensis Pb18
(NCBI TaxID 502780,
species name lookup)
Sporothrix schenckii 65
(Ancestor NCBI TaxID 29908,
species name lookup)
Histoplasma capsulatum 496
(Ancestor NCBI TaxID 5037,
species name lookup)
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: yeast,
myceliumAssociated disease: infection due to Paracoccidioides brasiliensis [ICD11:
XN5UX 
];
infection due to Sporothrix schenckii [ICD11:
XN6GM 
];
infection due to Histoplasma capsulatum [ICD11:
XN8VH 
]
NCBI PubMed ID: 20156351Publication DOI: 10.1186/1471-2180-10-47Journal NLM ID: 100966981Publisher: Biomed Central
Correspondence: takahashi.bioq

epm.br
Institutions: Division of Glycoconjugate Immunochemistry, Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, São Paulo, SP, Brazil
Background Studies carried out during the 1990's demonstrated the presence of fungal glycoinositol phosphorylceramides (GIPCs) with unique structures, some of them showed reactivity with sera of patients with histoplasmosis, paracoccidioidomycosis or aspergillosis. It was also observed that fungal GIPCs were able to inhibit T lymphocyte proliferation "in vitro", and studies regarding the importance of these molecules to fungal survival showed that many species of fungi are vulnerable to inhibitors of sphingolipid biosynthesis. Results In this paper, we describe a detailed characterization of an IgG2a monoclonal antibody (mAb), termed MEST-3, directed to the Paracoccidioides brasiliensis glycolipid antigen Pb-2 (Manp α1→3Manp α1→2IPC). mAb MEST-3 also recognizes GIPCs bearing the same structure in other fungi. Studies performed on fungal cultures clearly showed the strong inhibitory activity of MEST-3 on differentiation and colony formation of Paracoccidioides brasiliensis, Histoplasma capsulatum and Sporothrix schenckii. Similar inhibitory results were observed when these fungi where incubated with a different mAb, which recognizes GIPCs bearing terminal residues of β-D-galactofuranose linked to mannose (mAb MEST-1). On the other hand, mAb MEST-2 specifically directed to fungal glucosylceramide (GlcCer) was able to promote only a weak inhibition on fungal differentiation and colony formation. Conclusions These results strongly suggest that mAbs directed to specific glycosphingolipids are able to interfere on fungal growth and differentiation. Thus, studies on surface distribution of GIPCs in yeast and mycelium forms of fungi may yield valuable information regarding the relevance of glycosphingolipids in processes of fungal growth, morphological transition and infectivity.
monoclonal antibodies, Paracoccidioides brasiliensis, monoclonal antibody MEST-3, glycosylinositol
Structure type: monomer
Location inside paper: abstract, table 1
Trivial name: glucosylceramide, Glc-Cer
Compound class: glycolipid, glycosphingolipid, cerebroside
Contained glycoepitopes: IEDB_137339,IEDB_142488,IEDB_146664,IEDB_983931,SB_192,SB_5
Methods: periodate oxidation, ELISA, serological methods, genetic methods, UV, extraction, HPTLC, binding assays, immunofluorescence analyses, dialysis, fungal differentiation
Comments, role: GIPCs was extracted from mycelium and yeast forms of P. brasiliensis, S. schenckii and H. capsulatum.
Related record ID(s): 41721, 41946, 42156
NCBI Taxonomy refs (TaxIDs): 502780,
29908,
5037Reference(s) to other database(s): CCSD:
48834, CBank-STR:914
Show glycosyltransferases
There is only one chemically distinct structure:
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Toledo MS, Tagliari L, Suzuki E, Silva CM, Straus AH, Takahashi HK
Effect of anti-glycosphingolipid monoclonal antibodies in pathogenic fungal growth and differentiation. Characterization of monoclonal antibody MEST-3 directed to Manp α1→3Manp α1→2IPC
BMC Microbiology 10 (2010)
47
|
/Variants 0/-D-Manp
/Variants 0/ is:
b-D-Galf-(1-6)-
OR (exclusively)
b-D-Galf-(1-3)- |
Show graphically |
Paracoccidioides brasiliensis Pb18
(NCBI TaxID 502780,
species name lookup)
Histoplasma capsulatum 496
(Ancestor NCBI TaxID 5037,
species name lookup)
Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: yeast,
myceliumAssociated disease: infection due to Paracoccidioides brasiliensis [ICD11:
XN5UX 
];
infection due to Histoplasma capsulatum [ICD11:
XN8VH 
]
NCBI PubMed ID: 20156351Publication DOI: 10.1186/1471-2180-10-47Journal NLM ID: 100966981Publisher: Biomed Central
Correspondence: takahashi.bioq

epm.br
Institutions: Division of Glycoconjugate Immunochemistry, Department of Biochemistry, Universidade Federal de São Paulo/Escola Paulista de Medicina, São Paulo, SP, Brazil
Background Studies carried out during the 1990's demonstrated the presence of fungal glycoinositol phosphorylceramides (GIPCs) with unique structures, some of them showed reactivity with sera of patients with histoplasmosis, paracoccidioidomycosis or aspergillosis. It was also observed that fungal GIPCs were able to inhibit T lymphocyte proliferation "in vitro", and studies regarding the importance of these molecules to fungal survival showed that many species of fungi are vulnerable to inhibitors of sphingolipid biosynthesis. Results In this paper, we describe a detailed characterization of an IgG2a monoclonal antibody (mAb), termed MEST-3, directed to the Paracoccidioides brasiliensis glycolipid antigen Pb-2 (Manp α1→3Manp α1→2IPC). mAb MEST-3 also recognizes GIPCs bearing the same structure in other fungi. Studies performed on fungal cultures clearly showed the strong inhibitory activity of MEST-3 on differentiation and colony formation of Paracoccidioides brasiliensis, Histoplasma capsulatum and Sporothrix schenckii. Similar inhibitory results were observed when these fungi where incubated with a different mAb, which recognizes GIPCs bearing terminal residues of β-D-galactofuranose linked to mannose (mAb MEST-1). On the other hand, mAb MEST-2 specifically directed to fungal glucosylceramide (GlcCer) was able to promote only a weak inhibition on fungal differentiation and colony formation. Conclusions These results strongly suggest that mAbs directed to specific glycosphingolipids are able to interfere on fungal growth and differentiation. Thus, studies on surface distribution of GIPCs in yeast and mycelium forms of fungi may yield valuable information regarding the relevance of glycosphingolipids in processes of fungal growth, morphological transition and infectivity.
monoclonal antibodies, Paracoccidioides brasiliensis, monoclonal antibody MEST-3, glycosylinositol
Structure type: fragment of a bigger structure
Location inside paper: abstract, table 1
Compound class: glycosphingolipid
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_137485,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_983930,SB_44,SB_67,SB_72
Methods: periodate oxidation, ELISA, serological methods, genetic methods, UV, extraction, HPTLC, binding assays, immunofluorescence analyses, dialysis, fungal differentiation
Comments, role: GIPCs was extracted from mycelium forms of P. brasiliensis and yeast forms of P. brasiliensis and H. capsulatum.
Related record ID(s): 41721, 41946, 42155
NCBI Taxonomy refs (TaxIDs): 502780,
5037
Show glycosyltransferases
There is only one chemically distinct structure:
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