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A panel of monoclonal antibodies (Mabs) was raised against histoplasmin, the antigen derived from the mycelial phase of Histoplasma capsulatum var. capsulatum which contains the diagnostically useful H and M antigens. A number of Mabs were obtained which recognized a 70-75 kD component of an antigenic preparation of H. capsulatum var. capsulatum by Western blotting. When reacted with histoplasmin by Western blotting the Mabs recognized a similar 70-75 kD band, together with a series of higher molecular mass bands at approximately 130, 190 and 230 kD, a pattern which correlates strongly with both the published relative molecular mass (Mr) of the M antigen and the known subunit structure of the enzyme catalase. These Mabs were also shown to recognize a commercial preparation of Aspergillus niger catalase by ELISA. Other dimorphic fungi were also reactive with these Mabs by Western blotting, indicating the presence of common epitopes on the catalase molecules of these species.

The adhesion of microorganism to host cells or extracellular matrix (ECM) proteins is the first step in the establishment of an infectious process. Interaction between Paracoccidioides brasiliensis yeast cells and ECM proteins has been previously noted. In vivo, in the chronic phase of experimental paracoccidioidomycosis (PCM), laminin and fibronectin have been detected on the surface of yeast cells located inside granulomatous lesions. The aim of the present study was to examine the ability of P. brasiliensis yeast cells to interact with extracellular matrix proteins (laminin, fibrinogen and fibronectin) and to establish which molecules were involved in this interaction. Immunofluorescence microscopy and flow cytometry demonstrated that all three ECM proteins tested were able to bind to the surface of P. brasiliensis yeast cells. Treatment with trypsin, chymotrypsin, chitinase, proteinase K or different sugars resulted in no change in laminin binding. In addition, ligand affinity assays were performed using different yeast extracts (total homogenates, b-mercaptoethanol, SDS extracts). These assays demonstrated the presence of 19 and 32-kDa proteins in the cell wall with the ability to bind to laminin, fibrinogen and fibronectin. This interaction could be important in mediating attachment of the fungus to host tissues and may consequently play a role in the pathogenesis of PCM. COL0013709 COL0013746

In the last two decades, a variety of fungal antioxidants have attracted considerable interest, largely arising from their hypothetical role as virulence determinants. Melanin is a potent free radical scavenger and in Cryptococcus neoformans, there is now good evidence that the production of melanin is a significant virulence determinant. There is also recent evidence linking melanin biosynthesis to the virulence of Aspergillus fumigatus conidia. Superoxide dismutases are important housekeeping antioxidants and have an additional hypothetical role in virulence; however, although these enzymes have been biochemically characterized from Aspergillus and Cryptococcus, there is as yet no firm evidence that these enzymes are involved in pathogenicity. Catalase production may play some role in the virulence of Candida albicans but this enzyme has not been shown, as yet, to influence the virulence of A. fumigatus. There are some data supporting an antioxidant function for the acyclic hexitol mannitol in C. neoformans, but further investigations are required in this area. Research into the putative antioxidant activities of a range of other fungal enzymes, such as acid phosphatases, remains limited at this time.