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NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B
Author(s) -
Beck Moriah R.,
DeKoster Gregory T.,
Cistola David P.,
Goldman William E.
Publication year - 2009
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2009.06647.x
Subject(s) - biology , virulence , virulence factor , fungal protein , homology (biology) , protein structure , peptide sequence , homology modeling , calcium binding protein , biochemistry , calcium , microbiology and biotechnology , amino acid , gene , chemistry , enzyme , organic chemistry
Summary The fungal protein CBP ( c alcium b inding p rotein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum 's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four α‐helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells.