Abstract

Paracoccidioides brasiliensis is a dimorphic fungus and the causative agent of paracoccidioidomycosis, the most prevalent mycosis in America Latina. The fungal cell wall is an initial point of contact with host cells, playing a key role in morphogenesis and pathogenesis. Iron is required by virtually all pathogenic microorganisms for growth and virulence. Therefore, in the present study, we analyzed the proteome of the surface proteins of P. brasiliensis during iron deprivation. The protein extracts were obtained after 24h of fungal growth in chemically defined minimal medium (MMcM) depleted of iron sources. The proteins of the cell wall were extracted by hot SDS and DTT. Two-dimensional gel electrophoresis was performed to evaluate the differential proteomic profile of the yeast cells upon iron deprivation with subsequent analysis of images. Mass spectra of tryptic peptides were taken with a MALDI-Q-TOF and identified by Mascot software. For differential expression analysis, statistical significance was estimated by ANOVA. Statistical analysis demonstrated 89 regulated proteins which were subjected to tryptic digestion and identification by mass spectrometry. It was identified 41proteins, of which 27 up regulated and 14 down regulated upon iron deprivation. Heat shock proteins, ATP synthase, enolase, actin, fosfoglicerate kinase, disulfide isomerase malate dehydrogenase were examples of proteins regulated in iron restriction found on the cell surface of P. brasiliensis. ਀䘀椀渀愀渀挀椀愀氀 猀甀瀀瀀漀爀琀㨀 䘀䤀一䔀倀 䌀一倀焀 愀渀搀 䌀䄀倀䔀匀⸀㰀⼀昀漀渀琀㸀㰀⼀瀀㸀㰀戀爀㸀㰀戀㸀䬀攀礀眀漀爀搀㨀 㰀⼀戀㸀☀渀戀猀瀀㬀倀爀漀琀攀漀洀攀Ⰰ 匀甀爀昀愀挀攀 倀爀漀琀攀椀渀猀Ⰰ 䤀爀漀渀㰀⼀琀搀㸀㰀⼀琀爀㸀㰀⼀琀愀戀氀攀㸀㰀⼀琀爀㸀㰀⼀琀搀㸀㰀⼀琀愀戀氀攀㸀㰀⼀戀漀搀礀㸀㰀⼀栀琀洀氀㸀