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Proteome profiling of the dimorphic fungus Penicillium marneffei extracellular proteins and identification of glyceraldehyde‐3‐phosphate dehydrogenase as an important adhesion factor for conidial attachment
Author(s) -
Lau Susanna K. P.,
Tse Herman,
Chan Joanna S. Y.,
Zhou Anna C.,
Curreem Shirly O. T.,
Lau Candy C. Y.,
Yuen KwokYung,
Woo Patrick C. Y.
Publication year - 2013
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12566
Subject(s) - penicillium marneffei , microbiology and biotechnology , glyceraldehyde 3 phosphate dehydrogenase , biology , dimorphic fungus , extracellular , proteome , yeast , dehydrogenase , immunology , biochemistry , enzyme , virus , coinfection
Despite being the most important thermal dimorphic fungus causing systemic mycosis in Southeast Asia, the pathogenic mechanisms of Penicillium marneffei remain largely unknown. By comparing the extracellular proteomes of P. marneffei in mycelial and yeast phases, we identified 12 differentially expressed proteins among which glyceraldehyde‐3‐phosphate dehydrogenase ( GAPDH ) and heat shock protein 60 ( HSP 60) were found to be upregulated in mycelial and yeast phases respectively. Based on previous findings in other pathogens, we hypothesized that these two extracellular proteins may be involved in adherence during P. marneffei –host interaction. Using inhibition assays with recombinant GAPDH (r GAPDH ) proteins and anti‐r GAPDH sera, we demonstrated that adhesion of P. marneffei conidia to fibronectin and laminin was inhibited by r GAPDH or rabbit anti‐r GAPDH serum in a dose‐dependent manner. Similarly, a dose‐dependent inhibition of conidial adherence to A549 pneumocytes by r GAPDH or rabbit anti‐r GAPDH serum was observed, suggesting that P. marneffei GAPDH can mediate binding of conidia to human extracellular matrix proteins and pneumocytes. However, HSP 60 did not exhibit similar inhibition on conidia adherence, and neither GAPDH nor HSP 60 exhibited inhibition on adherence to J774 or THP‐1 macrophage cell lines. This report demonstrates GAPDH as an adherence factor in P. marneffei by mediating conidia adherence to host bronchoalveolar epithelium during the early establishment phase of infection.