Table 3.
Acession number | Protein | Expression status | Log (Fold Change) | Adjusted p-value |
---|---|---|---|---|
UPs | ||||
Lipid metabolism | ||||
C1G2K1 | Glycerol-3-phosphate dehydrogenase | UP(12) | 1,924377 | 0,02212 |
Cell cycle | ||||
C1G5E7 | Replication factor C subunit 3 | UP(8) | 4,474333 | 0,018531 |
Transport | ||||
C1G785 | GTP-binding protein ypt5 | UP(12) | 1,864712 | 0,030992 |
DOWNs | ||||
Gene/protein regulation | ||||
C1G0E5 | 40S ribosomal protein S14 | DOWN(8) | -5,76095 | 0,001957 |
C1G5P0 | pre-mRNA-splicing helicase BRR2 [EC:3.6.4.13] | DOWN(D) | -4,64777 | 2,39E-05 |
C1G0P0 | molecular chaperone DnaK | DOWN(12) | -2,42964 | 0,026103 |
Energy metabolism | ||||
C1G294 | succinyl-CoA synthetase alpha subunit [EC:6.2.1.4 6.2.1.5] | DOWN(D) | -3,29572 | 0,003605 |
C1G2P3 | enoyl-CoA hydratase [EC:4.2.1.17] | DOWN(D) | -4,37849 | 2,82E-05 |
C1G2W2 | Pyruvate kinase (EC 2.7.1.40) | DOWN(D) | -5,32367 | 0,00092 |
C1GM03 | Cytochrome b-c1 complex subunit 2 | DOWN(D) | -4,10832 | 0,000135 |
Transport | ||||
C1FZ88 | importin subunit alpha-6/7 | DOWN(8) | -4,36192 | 0,003272 |
C1GAF5 | Coatomer subunit alpha | DOWN(8) | -2,60008 | 0,001756 |
C1GJS2 | Phosphatidylinositol transfer protein SFH5 (PITP SFH5) | DOWN(D) | -7,21769 | 1,52E-05 |
Amino acid metabolism | ||||
C1G3V5 | Aspartate aminotransferase (EC 2.6.1.1) | DOWN(12) | -5,05193 | 7,6E-05 |
C1GBD8 | 3-oxoacid CoA-transferase [EC:2.8.3.5] | DOWN(8) | -6,39235 | 5,76E-05 |
C1GBT4 | 1-pyrroline-5-carboxylate dehydrogenase [EC:1.2.1.88] | DOWN(8) | -6,07164 | 0,00025 |
Virulence factor | ||||
C1GKT9 | Thioredoxin domain-containing protein | DOWN(8) | -6,48413 | 3,21E-05 |
C1G7K8 | cytochrome c peroxidase [EC:1.11.1.5] | DOWN(D) | -3,10035 | 0,000272 |
C1GJI2 | Superoxide dismutase [Cu-Zn] | DOWN(D) | -3,5651 | 0,00071 |
Other metabolisms | ||||
C1GG77 | Carboxypeptidase Y homolog A (EC 3.4.16.5) | DOWN(D) | -2,92665 | 0,00822 |
C1GJM4 | Vacuolar aminopeptidase I | DOWN(D) | -4,32296 | 0,000825 |
Granulomatous lesions were extracted from two to four mice from three independent infections at eight weeks and twelve weeks after being infected with 1x106 P. brasiliensis yeasts. After lysing the animal cells, the fungal proteins were extracted and digested with trypsin and resolubilized in 0.1% formic acid. Peptides were analyzed by LC-MS/MS and proteins identified by MaxQuant software. Proteins containing more than two unique peptides had their intensity normalized by log2, then quantile normalized within each experimental repeat. The limma package was used for differentially abundant proteins analysis and GO, KEGG and FungiDB were used for functional analysis. The Table shows the differentially abundant proteins with the values of Log (Fold change) and adjusted p-value. The expression status column represents the upregulated or downregulated proteins for the eight-week infection group (8), the twelve-week infection group (12), and the proteins that were differentially expressed in both infection groups were combined and reanalyzed, resulting in an expression status designation for the disease (D).