Tags

Type your tag names separated by a space and hit enter

The multifaceted roles of metabolic enzymes in the Paracoccidioides species complex.
Front Microbiol. 2014; 5:719.FM

Abstract

Paracoccidioides species are dimorphic fungi and are the etiologic agents of paracoccidioidomycosis, which is a serious disease that involves multiple organs. The many tissues colonized by this fungus suggest a variety of surface molecules involved in adhesion. A surprising finding is that most enzymes in the glycolytic pathway, tricarboxylic acid (TCA) cycle and glyoxylate cycle in Paracoccidioides spp. have adhesive properties that aid in interacting with the host extracellular matrix and thus act as 'moonlighting' proteins. Moonlighting proteins have multiple functions, which adds a dimension to cellular complexity and benefit cells in several ways. This phenomenon occurs in both eukaryotes and prokaryotes. For example, moonlighting proteins from the glycolytic pathway or TCA cycle can play a role in bacterial pathogenesis by either acting as proteins secreted in a conventional pathway and/or as cell surface components that facilitate adhesion or adherence. This review outlines the multifunctionality exhibited by many Paracoccidioides spp. enzymes, including aconitase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, isocitrate lyase, malate synthase, triose phosphate isomerase, fumarase, and enolase. We discuss the roles that moonlighting activities play in the virulence characteristics of this fungus and several other human pathogens during their interactions with the host.

Authors+Show Affiliations

Laboratório de Micologia Clínica, Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Araraquara, Brazil.Laboratório de Micologia Clínica, Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Araraquara, Brazil.Laboratório de Micologia Clínica, Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Araraquara, Brazil.Laboratório de Micologia Clínica, Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Araraquara, Brazil.Laboratório de Micologia Clínica, Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Araraquara, Brazil.Laboratório de Micologia Clínica, Departamento de Análises Clínicas, Faculdade de Ciências Farmacêuticas, Universidade Estadual Paulista Araraquara, Brazil.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

25566229

Citation

Marcos, Caroline M., et al. "The Multifaceted Roles of Metabolic Enzymes in the Paracoccidioides Species Complex." Frontiers in Microbiology, vol. 5, 2014, p. 719.
Marcos CM, de Oliveira HC, da Silva Jde F, et al. The multifaceted roles of metabolic enzymes in the Paracoccidioides species complex. Front Microbiol. 2014;5:719.
Marcos, C. M., de Oliveira, H. C., da Silva, J. d. e. . F., Assato, P. A., Fusco-Almeida, A. M., & Mendes-Giannini, M. J. (2014). The multifaceted roles of metabolic enzymes in the Paracoccidioides species complex. Frontiers in Microbiology, 5, 719. https://doi.org/10.3389/fmicb.2014.00719
Marcos CM, et al. The Multifaceted Roles of Metabolic Enzymes in the Paracoccidioides Species Complex. Front Microbiol. 2014;5:719. PubMed PMID: 25566229.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The multifaceted roles of metabolic enzymes in the Paracoccidioides species complex. AU - Marcos,Caroline M, AU - de Oliveira,Haroldo C, AU - da Silva,Julhiany de F, AU - Assato,Patrícia A, AU - Fusco-Almeida,Ana M, AU - Mendes-Giannini,Maria J S, Y1 - 2014/12/19/ PY - 2014/10/28/received PY - 2014/12/01/accepted PY - 2015/1/8/entrez PY - 2015/1/8/pubmed PY - 2015/1/8/medline KW - Paracoccidioides spp. KW - adhesins KW - glycolytic pathway and tricarboxylic acid cycle KW - glyoxylate cycle KW - moonlighting proteins KW - virulence SP - 719 EP - 719 JF - Frontiers in microbiology JO - Front Microbiol VL - 5 N2 - Paracoccidioides species are dimorphic fungi and are the etiologic agents of paracoccidioidomycosis, which is a serious disease that involves multiple organs. The many tissues colonized by this fungus suggest a variety of surface molecules involved in adhesion. A surprising finding is that most enzymes in the glycolytic pathway, tricarboxylic acid (TCA) cycle and glyoxylate cycle in Paracoccidioides spp. have adhesive properties that aid in interacting with the host extracellular matrix and thus act as 'moonlighting' proteins. Moonlighting proteins have multiple functions, which adds a dimension to cellular complexity and benefit cells in several ways. This phenomenon occurs in both eukaryotes and prokaryotes. For example, moonlighting proteins from the glycolytic pathway or TCA cycle can play a role in bacterial pathogenesis by either acting as proteins secreted in a conventional pathway and/or as cell surface components that facilitate adhesion or adherence. This review outlines the multifunctionality exhibited by many Paracoccidioides spp. enzymes, including aconitase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, isocitrate lyase, malate synthase, triose phosphate isomerase, fumarase, and enolase. We discuss the roles that moonlighting activities play in the virulence characteristics of this fungus and several other human pathogens during their interactions with the host. SN - 1664-302X UR - https://www.unboundmedicine.com/medline/citation/25566229/The_multifaceted_roles_of_metabolic_enzymes_in_the_Paracoccidioides_species_complex_ L2 - https://doi.org/10.3389/fmicb.2014.00719 DB - PRIME DP - Unbound Medicine ER -
Try the Free App:
Prime PubMed app for iOS iPhone iPad
Prime PubMed app for Android
Prime PubMed is provided
free to individuals by:
Unbound Medicine.