Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us Oct (2007); 0: Gpm1p is a factor H, FHL-1 and plasminogen-binding surface protein of Candida albicans- Poltermann S, Kunert A, von der Heide M, Eck R, Hartmann A, Zipfel PF Infection Biology, Leibniz Institute for Natural Product Research and Infection Biology, Jena D 07745- Abstract: The human pathogenic yeast Candida albicans utilizes host complement regulators for immune evasion- Here we identify the first fungal protein that binds Factor H and FHL-1- By screening a protein array of 4088 proteins of Saccharomyces cerevisiae, phosphoglycerate mutase -ScGpm1p- was identified as a Factor H and FHL-1-binding protein- The homologous C- albicans Gpm1p -CaGpm1p- was cloned and recombinantly expressed as a 36 kDa His-tagged protein- Purified CaGpm1p binds the host complement regulators Factor H and FHL-1, but not C4BP- The CaGpm1p-binding regions in the host proteins were localized- FHL-1 binds via SCRs 6-7 and Factor H utilizes two contact regions which are located in SCRs 6-7 and in SCRs 19-20- In addition, recombinant CaGpm1p binds plasminogen via lysine residues and three linear, internal plasminogen-binding regions were identified using a peptide-spot assay- CaGpm1p is a surface protein as demonstrated by immunostaining and flow cytometry- A C- albicans gpm1--- mutant strain was generated which did not grow on glucose supplemented, but on ethanol and glycerol supplemented media- Reduced binding of Factor H and plasminogen to the null mutant strain, is in agreement with the presence of additional binding proteins- Attached to CaGpm1p each of the three host plasma proteins is functionally active- Factor H and FHL-1 show cofactor activity for cleavage of C3b and bound plasminogen is converted by uPA to proteolytically active plasmin- Thus the surface-expressed CaGpm1p is a virulence factor, which utilizes the host Factor H, FHL-1 and plasminogen for immune evasion and degradation of extracellular matrices- [PUBMED: 17959597] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.