Taxonomic group: protista / Euglenozoa
(Phylum: Euglenozoa)
Host organism: Homo sapiens
Associated disease: infection due to Trypanosoma brucei [ICD11:
XN0C1 
]
NCBI PubMed ID: 25074286Publication DOI: 10.1042/BJ20140541Journal NLM ID: 2984726RPublisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
Correspondence: ymorita
microbio.umass.edu
Institutions: Laboratory of Immunoglycobiology, WPI Immunology Frontier Research Center, Osaka University, Osaka 565-0871, Japan, Department of Microbiology, University of Massachusetts, Amherst, MA 01003, U.S.A., Japan
PIGF is a protein involved in the ethanolamine phosphate (EtNP) transfer steps of glycosylphosphatidylinositol (GPI) biosynthesis. PIGF forms a heterodimer with either PIGG or PIGO, two enzymes that transfer an EtNP to the second or third mannoses of GPI respectively. Heterodimer formation is essential for stable and regulated expression of PIGO and PIGG, but the functional significance of PIGF remains obscure. In the present study, we show that PIGF binds to PIGO and PIGG through distinct molecular domains. Strikingly, C-terminal half of PIGF was sufficient for its binding to PIGO and PIGG and yet this truncation mutant could not complement the PIGF defective mutant cells, suggesting that heterodimer formation is not sufficient for PIGF function. Furthermore, we identified a highly conserved motif in PIGF and demonstrated that the motif is not involved in binding to PIGO or PIGG, but critical for its function. Finally, we identified a PIGF homologue from Trypanosoma brucei and showed that it binds specifically to the T. brucei PIGO homologue. These data together support the notion that PIGF plays a critical and evolutionary conserved role in the ethanolamine-phosphate transfer-step, which cannot be explained by its previously ascribed binding/stabilizing function. Potential roles of PIGF in GPI biosynthesis are discussed.
metabolism, Glycosylphosphatidylinositol, Trypanosoma brucei, membrane protein, ethanolamine phosphate transferase, PIGF
Structure type: oligomer
Location inside paper: p. 249, Fig. 1
Aglycon: lipid
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141829,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_474450,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72
Methods: PCR, SDS-PAGE, Western blotting, immunoprecipitation assay, clonind, FACS
NCBI Taxonomy refs (TaxIDs): 5691
Show glycosyltransferases
There is only one chemically distinct structure:
Taxonomic group: bacteria / Firmicutes
(Phylum: Firmicutes)
Associated disease: infection due to Streptococcus [ICD11:
XN3NM ]
NCBI PubMed ID: 35891202Publication DOI: 10.3390/vaccines10071034Journal NLM ID: 101629355Publisher: Basel, Switzerland: MDPI AG
Correspondence: F. Micoli <francesca.x.micoli
gsk.com>
Institutions: GSK Vaccines Institute for Global Health (GVGH), Via Fiorentina 1, 53100 Siena, Italy, The Sargent Centre for Process Systems Engineering, Department of Chemical Engineering, Imperial College London, South Kensington Campus, London SW7 2AZ, UK, Department of Chemical and Biological Engineering, The University of Sheffield, Mappin Street, Sheffield S1 3JD, UK, The National Institute for Biological Standards and Control (NIBSC), South Mimms EN6 3QG, UK
Group A Streptococcus (GAS) causes about 500,000 annual deaths globally, and no vaccines are currently available. The Group A Carbohydrate (GAC), conserved across all GAS serotypes, conjugated to an appropriate carrier protein, represents a promising vaccine candidate. Here, we explored the possibility to use Generalized Modules for Membrane Antigens (GMMA) as an alternative carrier system for GAC, exploiting their intrinsic adjuvant properties. Immunogenicity of GAC-GMMA conjugate was evaluated in different animal species in comparison to GAC-CRM197; and the two conjugates were also compared from a techno-economic point of view. GMMA proved to be a good alternative carrier for GAC, resulting in a higher immune response compared to CRM197 in different mice strains, as verified by ELISA and FACS analyses. Differently from CRM197, GMMA induced significant levels of anti-GAC IgG titers in mice also in the absence of Alhydrogel. In rabbits, a difference in the immune response could not be appreciated; however, antibodies from GAC-GMMA-immunized animals showed higher affinity toward purified GAC antigen compared to those elicited by GAC-CRM197. In addition, the GAC-GMMA production process proved to be more cost-effective, making this conjugate particularly attractive for low- and middle-income countries, where this pathogen has a huge burden.
vaccine, glycoconjugate, Group A Streptococcus, GMMA, Group A Carbohydrate
Structure type: polymer chemical repeating unit
Location inside paper: Fig. 1A, Fig. 1D
Trivial name: GAS-PS, GAC, GAC, group A carbohydrate, GAC-PS
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_127513,IEDB_131174,IEDB_131175,IEDB_131177,IEDB_133754,IEDB_135610,IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_143254,IEDB_151531,IEDB_2218296,IEDB_225177,IEDB_885823
Methods: SDS-PAGE, ELISA, HPAEC-PAD, antibody binding, statistical analysis, oxidation, conjugation, HPLC-SEC, reductive amination, immunogenicity studies, DLS, FACS, genetic engineering, GMMA-technology
Comments, role: GAC was chemically extracted from protein-mutant strain (GAS51∆M1) derived from the wild strain HRO-K-51 of Streptococcus sp. A
NCBI Taxonomy refs (TaxIDs): 1301Reference(s) to other database(s): GTC:G59445KA, GlycomeDB:
37806
Show glycosyltransferases
There is only one chemically distinct structure:
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