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1.
J Enzyme Inhib Med Chem ; 29(1): 12-7, 2014 Feb.
Article in English | MEDLINE | ID: mdl-23323991

ABSTRACT

Abstract Lippia alba (Miller) N.E. Brown is an aromatic plant known locally as "Erva-cidreira-do-campo" that has great importance in Brazilian folk medicine. The aim of our study was to evaluate the antidermatophytic potential of linalool-rich essential oil (EO) from L. alba and analyze the ability of this EO to inhibit peptidase and keratinase activities, which are important virulence factors in dermatophytes. The minimum inhibitory concentrations (MICs) of L. alba EO were 39, 156 and 312 µg/mL against Trichophyton rubrum, Epidermophyton floccosum and Microsporum gypseum, respectively. To evaluate the influence of L. alba EO on the proteolytic and keratinolytic activities of these dermatophytes, specific inhibitory assays were performed. The results indicated that linalool-rich EO from L. alba inhibited the activity of proteases and keratinases secreted from dermatophytes, and this inhibition could be a possible mechanism of action against dermatophytes. Due to the effective antidermatophytic activity of L. alba EO, further experiments should be performed to explore the potential of this linalool-rich EO as an alternative antifungal therapy.


Subject(s)
Arthrodermataceae/enzymology , Lippia/chemistry , Monoterpenes/analysis , Oils, Volatile/pharmacology , Peptide Hydrolases/drug effects , Protease Inhibitors/pharmacology , Acyclic Monoterpenes , Electrophoresis, Polyacrylamide Gel , Hydrogen-Ion Concentration , Microbial Sensitivity Tests , Oils, Volatile/chemistry
2.
Mycopathologia ; 176(3-4): 183-9, 2013 Oct.
Article in English | MEDLINE | ID: mdl-23943428

ABSTRACT

The possible role of sialic acids in host cells-fungi interaction and their association with glycoproteins were evaluated using a clinical isolate of the dimorphic fungus Mucor polymorphosporus. Lectin-binding assays with spores and yeast cells denoted the presence of surface sialoglycoconjugates containing 2,3- and 2,6-linked sialylglycosyl groups. Western blotting with peroxidase-labeled Limulus polyphemus agglutinin revealed the occurrence of different sialoglycoprotein types in both cell lysates and cell wall protein extracts of mycelia, spores, and yeasts of M. polymorphosporus. Sialic acids contributed to the surface negative charge of spores and yeast forms as evaluated by adherence to a cationic substrate. Sialidase-treated spores were less resistant to phagocytosis by human neutrophils and monocytes from healthy individuals than control (untreated) fungal suspensions. The results suggest that sialic acids are terminal units of various glycoproteins of M. polymorphosporus, contributing to negative charge of yeasts and spore cells and protecting infectious propagules from destruction by host cells.


Subject(s)
Blood/immunology , Mucor/chemistry , Mucor/immunology , Phagocytes/immunology , Phagocytosis/drug effects , Sialoglycoproteins/immunology , Sialoglycoproteins/metabolism , Humans , Hyphae/chemistry , Hyphae/immunology , Lectins/metabolism , Mucor/isolation & purification , Mucormycosis/microbiology , Protein Binding , Spores, Fungal/chemistry , Spores, Fungal/immunology , Static Electricity
3.
Med Mycol ; 48(2): 278-84, 2010 Mar.
Article in English | MEDLINE | ID: mdl-20141371

ABSTRACT

Complement activation by spores of Mucor ramosissimus, Mucor plumbeus and Mucor circinelloides was studied using absorbed human serum in the presence or absence of chelators (EGTA or EDTA). We found that the spore caused full complement activation when incubated with EGTA-Mg2+ or without chelators, indicating that the alternative pathway is mainly responsible for this response. In order to compare activation profiles from each species, ELISAs for C3 and C4 fragments, mannan binding lectin (MBL), C-reactive protein (CRP) and IgG studies were carried out. All proteins were present on the species tested. Immunofluorescence tests demonstrated the presence of C3 fragments on the surface of all samples, which were confluent throughout fungal surfaces. The same profile of C3, C4, MBL, CRP and IgG deposition, observed in all species, suggests a similar activation behavior for these species.


Subject(s)
Complement Activation/immunology , Mucor/physiology , Spores, Fungal/immunology , C-Reactive Protein/metabolism , Complement C3/metabolism , Complement C4/metabolism , Edetic Acid , Egtazic Acid , Enzyme-Linked Immunosorbent Assay , Fluorescent Antibody Technique, Direct , Humans , Immunoglobulin G/metabolism , Mannose-Binding Lectin/metabolism , Mucor/immunology
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