NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B |
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| Authors: | Moriah R. Beck Gregory T. DeKoster David P. Cistola William E. Goldman |
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| Affiliation: | Departments of Molecular Microbiology and;Biochemistry and Molecular Biophysics, Washington University in St Louis, St Louis, MO, USA.
Departments of;Biochemistry and Biophysics and;Microbiology and Immunology, University of North Carolina at Chapel Hill, Campus Box #7290, Chapel Hill, NC 27599, USA. |
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| Abstract: | 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. |
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