Identification and characterization of Paracoccidioides lutzii proteins interacting with macrophages |
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Authors: | Mariana Vieira Tomazett Lílian Cristiane Baeza Juliano Domiraci Paccez Juliana Alves Parente-Rocha Fátima Ribeiro-Dias Célia Maria de Almeida Soares |
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Affiliation: | 1. Laboratório de Biologia Molecular, Instituto de Ciências Biológicas, Universidade Federal de Goiás, 74001-970, Goiânia, Goiás, Brazil;2. Centro de Ciências Médicas e Farmacêuticas, Universidade Estadual do Oeste do Paraná, 85819-110, Cascavel, Paraná, Brazil;3. Laboratório de Imunidade Natural, Instituto de Patologia Tropical e Saúde Pública, Universidade Federal de Goiás, 74605-050, Goiânia, Goiás, Brazil |
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Abstract: | Paracoccidioidomycosis (PCM), caused by thermodimorphic fungi of the Paracoccidioides genus, is a systemic disorder that involves the lungs and other organs. The adherence of pathogenic microorganisms to host tissues is an essential event in the onset of colonization and spread. The host–pathogen interaction is a complex interplay between the defense mechanisms of the host and the efforts of pathogenic microorganisms to colonize it. Therefore, the identification of fungi proteins interacting with host proteins is an important step understanding the survival strategies of the fungus within the host. In this paper, we used affinity chromatography based on surface proteomics (ACSP) to investigate the interactions of pathogen proteins with host surface molecules. Paracoccidioides lutzii extracts enriched of surface proteins were captured by chromatographic resin, which was immobilized with macrophage cell surface proteins, and identified by mass spectrometry. A total of 215 proteins of P. lutzii were identified interacting with macrophage proteins. In silico analysis classified those proteins according to the presence of sites for N- and O-glycosylation and secretion by classical and non-classical pathways. Serine proteinase (SP) and fructose-1,6-bisphosphate aldolase (FBA) were identified in our proteomics analysis. Immunolocalization assay and flow cytometry both showed an increase in the expression of these two proteins during host–pathogen interaction. |
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Keywords: | Corresponding author. Laboratório de Biologia Molecular, Departamento de Bioquímica e Biologia Molecular, Instituto de Ciências Biológicas, Universidade Federal de Goiás, Goiânia, 74690-900, Goiás, Brazil. Fax: +55 62 3521 1110. Macrophages Interaction Serine proteinase Fructose-1,6-Bisphosphate aldolase |
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