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Semin Respir Infect. 1997 Sep;12(3):198-205.

Role of cell surface molecules of Blastomyces dermatitidis in the pathogenesis and immunobiology of blastomycosis.

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Department of Pediatrics, University of Wisconsin Medical School, Madison, USA.


The cell surface of pathogenic microbes is critical in directing their interactions with the host. The discovery of a 120 kd antigen/adhesin WI-1 on the yeast or parasitic form of Blastomyces dermatitidis has elucidated the molecular basis of host/pathogen interactions in blastomycosis. WI-1 has three structural domains: (1) an N-terminal hydrophobic domain that spans the cell membrane, (2) a C-terminal epidermal growth factor-like domain that may bind extracellular matrix, and (3) a central domain of many 24- or 25 amino-acid repeats arrayed in tandem. The repeat is homologous to invasin, a Yersinia adhesin, and binds CD11b/CD18 (CR3) and CD14 receptors on host cells. WI-1 expression is altered on genetically related strains of B dermatitidis differing in virulence and modulates how hypovirulent mutants interact with macrophages. WI-1 also evokes humoral and cell-mediated immune responses in acquired resistance to B dermatitidis that may help clear the fungus in the host. These observations on WI-1 provide new insight into a key pathogenic factor and antigen of the fungus and may ultimately help in designing new ways to diagnose, treat, and prevent blastomycosis.

[Indexed for MEDLINE]

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