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Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
Published on: June 7, 2020
Molecular chaperones in the Paracoccidioides brasiliensis transcriptome
André Moraes Nicola1, Rosângela Vieira Andrade, Ildinete Silva-Pereira
1Instituto de Biologia, Departamento de Biologia Celular, Universidade de Brasília, Campus Universitário Darcy Ribeiro, Asa Norte, 70910-900 Brasília, DF, Brazil.
Abstract:
Paracoccidioides brasiliensis is a thermally dimorphic and a human pathogenic fungus. Our group has partially sequenced its transcriptome and generated a database of mycelial and yeast PbAESTs (P. brasiliensis assembled expressed sequence tags). In the present review we describe the identification of PbAESTs encoding molecular chaperones. These proteins, involved in protein folding and renaturation, are also implicated in several other biological processes, where the dimorphic transition is of particular interest. Another important issue concerning these proteins refers to their participation in the immunopathogenicity of infectious diseases. We have found 438 ESTs (184 in mycelium and 253 in yeast) encoding P. brasiliensis molecular chaperones and their co-chaperones, which were clustered in 48 genes. These genes were classified in families, corresponding to three small chaperones, nine HSP40s, 10 HSP60s, seven HSP70s, five HSP90s, four HSP100s, and 10 other chaperones. These results greatly increase the knowledge on P. brasiliensis molecular chaperones, since only eight of such proteins had been previously characterized.
Insights
This study identified 438 P. brasiliensis expressed sequence tags encoding molecular chaperones and co-chaperones. These findings expand our understanding of chaperone proteins in this pathogenic fungus.
Area of Science:
- Mycology
- Molecular Biology
- Pathogenomics
Background:
- Paracoccidioides brasiliensis is a thermally dimorphic, pathogenic fungus.
- Molecular chaperones are crucial for protein folding, cellular stress response, and virulence.
- Understanding chaperone roles is key to addressing paracoccidioidomycosis.
Purpose of the Study:
- To identify and characterize molecular chaperones and co-chaperones in Paracoccidioides brasiliensis.
- To expand the knowledge base of P. brasiliensis expressed sequence tags (ESTs).
- To investigate the potential role of chaperones in fungal dimorphism and immunopathogenicity.
Main Methods:
- Partial sequencing of the P. brasiliensis transcriptome.
- Generation of a database of mycelial and yeast PbAESTs.
- Bioinformatic analysis for identification and classification of chaperone-encoding ESTs.
Main Results:
- Identification of 438 ESTs encoding chaperones and co-chaperones, clustered into 48 genes.
- Classification into families: small chaperones (3), HSP40 (9), HSP60 (10), HSP70 (7), HSP90 (5), HSP100 (4), and other chaperones (10).
- Significant expansion of known P. brasiliensis molecular chaperones, with only eight previously characterized.
Conclusions:
- This study significantly enhances the understanding of molecular chaperones in P. brasiliensis.
- The identified chaperones are potential targets for understanding fungal dimorphism and pathogenicity.
- Further research into these chaperones could inform novel therapeutic strategies against paracoccidioidomycosis.
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