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Mannoproteins are important and abundant structural components of fungal cell walls. TheMP1 gene encodes a cell wall mannoprotein of the pathogenic fungusPenicillium marneffei . In the present study, we show that Mp1p is secreted into the cell culture supernatant at a level that can be detected by Western blotting. A sensitive enzyme-linked immunosorbent assay (ELISA) developed with antibodies against Mp1p was capable of detecting this protein from the cell culture supernatant ofP. marneffei at 104 cells/ml. The anti-Mp1p antibody is specific since it fails to react with any protein-form lysates ofCandida albicans ,Histoplasma capsulatum , orCryptococcus neoformans by Western blotting. In addition, this Mp1p antigen-based ELISA is also specific forP. marneffei since the cell culture supernatants of the other three fungi gave negative results. Finally, a clinical evaluation of sera from penicilliosis patients indicates that 17 of 26 (65%) patients are Mp1p antigen test positive. Furthermore, a Mp1p antibody test was performed with these serum specimens. The combined antibody and antigen tests forP. marneffei carry a sensitive of 88% (23 of 26), with a positive predictive value of 100% and a negative predictive value of 96%. The specificities of the tests are high since none of the 85 control sera was positive by either test.

Detection of Cell Wall Mannoprotein Mp1p in Culture Supernatants of Penicillium marneffei and in Sera of Penicilliosis Patients