scholarly journals Characterization of secreted aspartyl proteases in Candida parapsilosis

2020 ◽  
Author(s):  
Dhirendra Kumar Singh
Keyword(s):  
Candida Parapsilosis ◽  
Aspartyl Proteases

scholarly journals Characterization of Biofilm Formation and the Role of BCR1 in Clinical Isolates of Candida parapsilosis

2013 ◽  
Vol 13 (4) ◽  
pp. 438-451 ◽  
Author(s):  
Srisuda Pannanusorn ◽  
Bernardo Ramírez-Zavala ◽  
Heinrich Lünsdorf ◽  
Birgitta Agerberth ◽  
Joachim Morschhäuser ◽  
...  
Keyword(s):  
Biofilm Formation ◽  
Candida Parapsilosis ◽  
Clinical Isolates ◽  
Wild Type ◽  
Content Type ◽  
Initial Adhesion ◽  
High Level ◽  
Increased Susceptibility

ABSTRACT In Candida parapsilosis , biofilm formation is considered to be a major virulence factor. Previously, we determined the ability of 33 clinical isolates causing bloodstream infection to form biofilms and identified three distinct groups of biofilm-forming strains (negative, low, and high). Here, we establish two different biofilm structures among strains forming large amounts of biofilm in which strains with complex spider-like structures formed robust biofilms on different surface materials with increased resistance to fluconazole. Surprisingly, the transcription factor Bcr1, required for biofilm formation in Candida albicans and C. parapsilosis , has an essential role only in strains with low capacity for biofilm formation. Although BCR1 leads to the formation of more and longer pseudohyphae, it was not required for initial adhesion and formation of mature biofilms in strains with a high level of biofilm formation. Furthermore, an additional phenotype affected by BCR1 was the switch in colony morphology from rough to crepe, but only in strains forming high levels of biofilm. All bcr1 Δ/Δ mutants showed increased proteolytic activity and increased susceptibility to the antimicrobial peptides protamine and RP-1 compared to corresponding wild-type and complemented strains. Taken together, our results demonstrate that biofilm formation in clinical isolates of C. parapsilosis is both dependent and independent of BCR1 , but even in strains which showed a BCR1 -independent biofilm phenotype, BCR1 has alternative physiological functions.

scholarly journals First evidence and characterization of an uncoupling protein in fungi kingdom: CpUCP of Candida parapsilosis

FEBS Letters ◽  
2000 ◽  
Vol 467 (2-3) ◽  
pp. 145-149 ◽  
Author(s):  
Wiesława Jarmuszkiewicz ◽  
Graziela Milani ◽  
Fabiane Fortes ◽  
Angelica Z. Schreiber ◽  
Francis E. Sluse ◽  
...  
Keyword(s):  
Candida Parapsilosis ◽  
Uncoupling Protein

Trypanosoma cruzi: Isolation and characterization of aspartyl proteases

2009 ◽  
Vol 122 (2) ◽  
pp. 128-133 ◽  
Author(s):  
Rosa T. Pinho ◽  
Leila M. Beltramini ◽  
Carlos R. Alves ◽  
Salvatore G. De-Simone
Keyword(s):  
Trypanosoma Cruzi ◽  
Isolation And Characterization ◽  
Aspartyl Proteases

scholarly journals Biochemical characterization of an ecto-ATP diphosphohydrolase activity in Candida parapsilosis and its possible role in adenosine acquisition and pathogenesis

2010 ◽  
Vol 10 (6) ◽  
pp. 735-746 ◽  
Author(s):  
Tina Kiffer-Moreira ◽  
Maria Ester Fernandes Sampaio ◽  
Daniela S. Alviano ◽  
Flavia Axelband ◽  
Gabriele Vargas Cesar ◽  
...  
Keyword(s):  
Candida Parapsilosis ◽  
Biochemical Characterization ◽  
Atp Diphosphohydrolase

scholarly journals Characterization of the transcriptional response of Candida parapsilosis to the antifungal peptide MAF-1A

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e9767
Author(s):  
Rong Cheng ◽  
Wei Li ◽  
Klarke M. Sample ◽  
Qiang Xu ◽  
Lin Liu ◽  
...  
Keyword(s):  
Antifungal Activity ◽  
Candida Parapsilosis ◽  
Membrane Integrity ◽  
Transcriptional Response ◽  
Acid Synthesis ◽  
Sterol Synthesis ◽  
Antifungal Peptide ◽  
Amino Acid Synthesis ◽  
Cell Membrane Integrity

Candida parapsilosis is a major fungal pathogen that leads to sepsis. New and more effective antifungal agents are required due to the emergence of resistant fungal strains. MAF-1A is a cationic antifungal peptide isolated from Musca domestica that is effective against a variety of Candida species. However, the mechanism(s) of its antifungal activity remains undefined. Here, we used RNA-seq to identify differentially expressed genes (DEGs) in Candida parapsilosis following MAF-1A exposure. The early (6 h) response included 1,122 upregulated and 1,065 downregulated genes. Late (18 h) responses were associated with the increased expression of 101 genes and the decreased expression of 151 genes. Upon MAF-1A treatment for 18 h, 42 genes were upregulated and 25 genes were downregulated. KEGG enrichment showed that the DEGs in response to MAF-1A were mainly involved in amino acid synthesis and metabolism, oxidative phosphorylation, sterol synthesis, and apoptosis. These results indicate that MAF-1A exerts antifungal activity through interference with Candida parapsilosis cell membrane integrity and organelle function. This provides new insight into the interaction between Candida parapsilosis and this antimicrobial peptide and serves as a reference for future Candida parapsilosis therapies.

Characterization of biofilms formed by Candida parapsilosis, C. metapsilosis, and C. orthopsilosis

2010 ◽  
Vol 300 (4) ◽  
pp. 265-270 ◽  
Author(s):  
Ali Abdul Lattif ◽  
Pranab K. Mukherjee ◽  
Jyotsna Chandra ◽  
Kim Swindell ◽  
Shawn R. Lockhart ◽  
...  
Keyword(s):  
Candida Parapsilosis

scholarly journals Production, Characterization, and Epitope Mapping of a Monoclonal Antibody against Aspartic Proteinase ofCandida albicans

1999 ◽  
Vol 6 (3) ◽  
pp. 429-433 ◽  
Author(s):  
Byoung-Kuk Na ◽  
Gyung-Tae Chung ◽  
Chul-Yong Song
Keyword(s):  
Monoclonal Antibody ◽  
Candida Albicans ◽  
Candida Tropicalis ◽  
Cathepsin D ◽  
Epitope Mapping ◽  
Candida Parapsilosis ◽  
Aspartic Proteinase ◽  
Ofcandida Albicans ◽  
Human Cathepsin

ABSTRACT A monoclonal antibody (MAb; MAb CAP1) that was reactive with extracellular aspartic proteinase of Candida albicans (CAP) was produced. The MAb showed strong sensitivity and reactivity to CAP but not to the aspartic proteinases of Candida parapsilosis, Candida tropicalis, andAspergillus fumigatus or to human cathepsin D or porcine pepsin. The epitope of the CAP recognized by the MAb was the proteinaseous part of CAP and the putative epitope of the MAb was located in the Asp77 to Gly103 sequence. This antibody could be useful for the characterization of CAP and would be a valuable probe for the detection of CAP antigen in the sera of patients with invasive candidiasis.

Sign in / Sign up

Export Citation Format

Share Document