Identification of human plasma proteins associated with the cell wall of the pathogenic fungus<i>Paracoccidioides brasiliensis</i>

Longo, Larissa V. G.; Nakayasu, Ernesto; Matsuo, Alisson L.; Silva, Roberta Peres da; Sobreira, Tiago J. P.; Vallejo, Milene C.; Ganiko, Luciane; Almeida, Igor C.; Puccia, Rosana

doi:10.1111/1574-6968.12097

Cited by 11 publications

(8 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[16][17][18] P. brasiliensis is also known to produce a variety of proteinases. 19,20 The aspartyl proteinases, also known as acid proteases, constitute one of the 4 superfamilies of proteolytic enzymes. They are generally similar to pepsin and show specificity for preferential cleavage at peptide bonds between hydrophobic amino acid residues.…”

Section: Introductionmentioning

confidence: 99%

In vitro Paracoccidioides brasiliensisbiofilm and gene expression of adhesins and hydrolytic enzymes

et al. 2015

View full text Add to dashboard Cite

Paracoccidioides species are dimorphic fungi that initially infect the lungs but can also spread throughout the body. The spreading infection is most likely due to the formation of a biofilm that makes it difficult for the host to eliminate the infection. Biofilm formation is crucial for the development of infections and confines the pathogen to an extracellular matrix. Its presence is associated with antimicrobial resistance and avoidance of host defenses. This current study provides the first description of biofilm formation by Paracoccidioides brasiliensis (Pb18) and an analysis of gene expression, using real-time PCR, associated with 3 adhesins and 2 hydrolytic enzymes that could be associated with the virulence profile. Biofilm formation was analyzed using fluorescence microscopy, scanning electron microscopy (SEM) and confocal laser scanning microscopy (CLSM). Metabolic activity was determined using the XTT reduction assay. P. brasiliensis was able to form mature biofilm in 144 h with a thickness of 100 μm. The presence of a biofilm was found to be associated with an increase in the expression of adhesins and enzymes. GP43, enolase, GAPDH and aspartyl proteinase genes were over-expressed, whereas phospholipase was down-regulated in biofilm. The characterization of biofilm formed by P. brasiliensis may contribute to a better understanding of the pathogenesis of paracoccidioidomycosis as well as the search for new therapeutic alternatives; while improving the effectiveness of treatment.

show abstract

Section: Introductionmentioning

confidence: 99%

In vitro Paracoccidioides brasiliensisbiofilm and gene expression of adhesins and hydrolytic enzymes

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Cell wall purification was performed as previously described for Paracoccidioides brasiliensis (Longo et al. ). Briefly, yeast cell pellets were washed three times in phosphate‐buffered saline solution and mechanically broken in a cell disruptor (B. Braun Biotech International GmBH, Melsungen, Germany) in the presence of glass beads (425–600 μm; Sigma‐Aldrich).…”

Section: Methodsmentioning

confidence: 99%

Characterization of Lipids and Proteins Associated to the Cell Wall of the Acapsular Mutant Cryptococcus neoformans Cap 67

Longo

Nakayasu

Pires

et al. 2015

J Eukaryotic Microbiology

Self Cite

View full text Add to dashboard Cite

Cryptococcus neoformans is an opportunistic human pathogen that causes life-threatening meningitis. In this fungus, the cell wall is exceptionally not the outermost structure due to the presence of a surrounding polysaccharide capsule, which has been highly studied. Considering that there is little information about C. neoformans cell wall composition, we aimed at describing proteins and lipids extractable from this organelle, using as model the acapsular mutant C. neoformans cap 67. Purified cell wall preparations were extracted with either chloroform/methanol or hot SDS. Total lipids fractionated in silica gel 60 were analyzed by electrospray ionization-tandem mass spectrometry (ESI-MS/MS), while trypsin digested proteins were analyzed by liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS). We detected 25 phospholipid species among phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, phosphatidylinositol, and phosphatidic acid. Two glycolipid species were identified as monohexosyl ceramides. We identified 192 non-covalently linked proteins belonging to different metabolic processes. Most proteins were classified as secretory, mainly via nonclassical mechanisms, suggesting a role for extracellular vesicles in transwall transportation. In concert with that, orthologs from 86% of these proteins have previously been reported both in fungal cell wall and/or in extracellular vesicles. The possible role of the presently described structures in fungal-host relationship is discussed.

show abstract

“…Longo et al identified the ceruloplasmin bound to the cell wall of P . brasiliensis [ 38 ]. Ceruloplasmin is responsible for transporting 70% of the total copper in human serum and exhibits a copper-dependent oxidase activity, which possibly oxidizes Fe 2+ to Fe 3+ , thereby participating in iron transport.…”

Section: Discussionmentioning

confidence: 99%

Ceruloplasmin, transferrin and apolipoprotein A-II play important role in treatment's follow-up of paracoccidioidomycosis patients

et al. 2018

View full text Add to dashboard Cite

Paracoccidioidomycosis (PCM) is a systemic disease caused by thermodymorphic fungi of the Paracoccidioides brasiliensis complex, (Paracoccidioides spp.). Patients with PCM reveal specific cellular immune impairment. Despite the effective treatment, quiescent fungi can lead to relapse, usually late, the serological diagnosis of which has been deficient. The present study was carried out with the objective of investigating a biomarker for the identification of PCM relapse and another molecule behaving as an immunological recovery biomarker; therefore, it may be used as a cure criterion. In the evolutionary analysis of the proteins identified in PCM patients, comparing those that presented with those that did not reveal relapse, 29 proteins were identified. The interactions observed between the proteins, using transferrin and haptoglobin, as the main binding protein, were strong with all the others. Patient follow-up suggests that cerulosplamin may be a marker of relapse and that transferrin and apolipoprotein A-II may contribute to the evaluation of the treatment efficacy and avoiding a premature decision.

show abstract

Identification of human plasma proteins associated with the cell wall of the pathogenic fungusParacoccidioides brasiliensis

Cited by 11 publications

References 49 publications

In vitro Paracoccidioides brasiliensisbiofilm and gene expression of adhesins and hydrolytic enzymes

In vitro Paracoccidioides brasiliensisbiofilm and gene expression of adhesins and hydrolytic enzymes

Characterization of Lipids and Proteins Associated to the Cell Wall of the Acapsular Mutant Cryptococcus neoformans Cap 67

Ceruloplasmin, transferrin and apolipoprotein A-II play important role in treatment's follow-up of paracoccidioidomycosis patients

Contact Info

Product

Resources

About