DppV, a member of the dipeptidyl-peptidase family in A fumigatus

DppV, a member of the dipeptidyl-peptidase family in A. fumigatus, is identical to one of the principal antigens used in the diagnosis of IA. Moreover, DppV can generate protection responses, and improve the survival rate of Aspergillus-infected mice [28]. DppV can also bind with collagen or other human proteins and degrade them, which can damage the host. Recombinant DppV has shown a great potential in the serodiagnosis of IA in immunocompromised and immunocompetent patients [35]. NAD-dependent malate dehydrogenase, a key enzyme in glycometabolism that catalyze the reversible conversion

between malate and oxaloacetate, was reported recently as an allergen of A. fumigatus and A. versicolor [29]. Malate dehydrogenase was also shown to be a Paracoccidioides YM155 solubility dmso brasileinsis immunogenic protein [36] as well as a Candida albicans immunogen [32]. Aspartyl aminopeptidase, an enzyme that specifically degrades only amino-terminal acidic amino acids from peptides, was recently reported as an antigen of A. fumigatus [30] . TR of A. fumigatus has been described as an extracellular antigenic protein by two recent studies [30, 31]. In one former

study, the secreted fraction of two geographically different strains (190/96 and DAYA) of A. fumigatus were used to identify new immunogenic selleck chemicals molecules reacting with pooled ABPA patient sera (IgG and IgE). TR was only detected on 2DE immunoblots of the secreted proteome of the DAYA strain probed with the IgE antibody fraction from pooled ABPA check details PtdIns(3,4)P2 patients sera [31]. This result suggested that TR might not be a good biomarker for ABPA. In another study, the immunosecretome of A. fumigatus was detected using pooled patient sera (total n = 22 patients [ABPA, n = 11; aspergilloma, n = 5; IA, n = 6]). The immunoreactive intensity of TR was lower than most other proteins [30]. A possible explanation is that the anti-TR antibody titers were not high in pooled sera because most cases included in the study were not IA. Although

investigators in other laboratories recently noted the antigenic nature of TR [30, 31], no study has found shown diagnostic value for TR in non-neutropenic patients with IA. We showed that TR (spot no. 2A-2 M) had the strongest immunoreactivity with patient sera. TR, a component of the gliotoxin biosynthetic cluster, provides self protection to A. fumigatus against gliotoxin [37, 38]. This protein has been described as an extracellular protein of A. fumigatus by Singh and Kumar [30, 31]. However, Schrettl et al. showed that GliT is preferentially localized in the cytoplasm and nuclei by a GFP-GliT construct [38]. To predict whether or not GliT is actively secreted into the culture supernatant, we used two bioinformatic tools (SignalP and WoLF PSORT) to analyze its localization. Our results support the findings of Singh and Kumar [30, 31].

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