| Summary: | <p>Abstract</p> <p>Background</p> <p>The pathogenic fungus <it>Paracoccidioides brasiliensis </it>is the agent of paracoccidioidomycosis (PCM). This is a pulmonary mycosis acquired by inhalation of fungal airborne propagules that can disseminate to several organs and tissues leading to a severe form of the disease. Adhesion and invasion to host cells are essential steps involved in the internalization and dissemination of pathogens. Inside the host, <it>P. brasiliensis </it>may use the glyoxylate cycle for intracellular survival.</p> <p>Results</p> <p>Here, we provide evidence that the malate synthase of <it>P. brasiliensis </it>(<it>Pb</it>MLS) is located on the fungal cell surface, and is secreted. <it>Pb</it>MLS was overexpressed in <it>Escherichia coli</it>, and polyclonal antibody was obtained against this protein. By using Confocal Laser Scanning Microscopy, <it>Pb</it>MLS was detected in the cytoplasm and in the cell wall of the mother, but mainly of budding cells of the <it>P. brasiliensis </it>yeast phase. <it>Pb</it>MLSr and its respective polyclonal antibody produced against this protein inhibited the interaction of <it>P. brasiliensis </it>with <it>in vitro </it>cultured epithelial cells A549.</p> <p>Conclusion</p> <p>These observations indicated that cell wall-associated <it>Pb</it>MLS could be mediating the binding of fungal cells to the host, thus contributing to the adhesion of fungus to host tissues and to the dissemination of infection, behaving as an anchorless adhesin.</p>
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