Cell walls of the dimorphic fungal pathogens Sporothrix schenckii and Sporothrix brasiliensis exhibit bilaminate structures and sloughing of extensive and intact layers

This work was supported by the Fundação Carlos Chagas de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ), grants E-26/202.974/2015 and Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), grants 229755/2013-5, Brazil. LMLB is a senior research fellow of CNPq and Faperj. NG acknowledged support from the Wellcome Trust (Trust (097377, 101873, 200208) and MRC Centre for Medical Mycology (MR/N006364/1). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Peer reviewedPublisher PD

CROSS-REACTIVE POLYSACCHARIDES FROM TRYPANOSOMA-CRUZI and FUNGI (ESPECIALLY DACTYLIUM-DENDROIDES)

ESCOLA PAULISTA MED,DISCIPLINA MICOL,RUA BOTUCATU 862,BR-04023 São Paulo,SP,BRAZILESCOLA PAULISTA MED,DISCIPLINA PARASITOL,BR-04023 São Paulo,SP,BRAZILUNIV FED PARANA,DEPT BIOQUIM,BR-80000 CURITABA,PARANA,BRAZILESCOLA PAULISTA MED,DISCIPLINA MICOL,RUA BOTUCATU 862,BR-04023 São Paulo,SP,BRAZILESCOLA PAULISTA MED,DISCIPLINA PARASITOL,BR-04023 São Paulo,SP,BRAZILESCOLA PAULISTA MED,DISCIPLINA MICOL,RUA BOTUCATU 862,BR-04023 São Paulo,SP,BRAZILESCOLA PAULISTA MED,DISCIPLINA PARASITOL,BR-04023 São Paulo,SP,BRAZILWeb of Scienc

A lectin from the lichenized Basidiomycete Dictyonema glabratum

A lectin with hemagglutinating activity has been isolated from an aqueous extract of the symbiotic phenotype of Dictyonema glabratum and its cyanobacterial photobiont Scytonema sp. The purified lectin had a pi of 6.8 and its molecular mass was investigated by electrospray ionization mass spectrometry, gel filtration and SDS-PAGE, which indicated its native conformation as a dimer formed by two identical subunits of 16540 Da. The lectin is a glycoprotein with a low degree of glycosylation, containing galactose, xylose, glucose and mannose as neutral monosaccharides, in addition to glucosamine, which could indicate both N- and O-linkages. Amino acid analysis showed the predominance of nonpolar residues such as phenylalanine. Agglutination of human erythrocytes required divalent cations, which is affected by addition of EDTA. The lectin was more stable at 30 degreesC or less for at least 1 h and between pH 5.0 and 7.0. Among the various compounds tested for hemagglutination inhibition, N-acetylgalactosamine was the most active. The potential role of this lectin in recognition of the compatible cyanobacterial photobiont is discussed

Structure of a glycoglucuronomannan from the low-viscosity gum of Vochysia lehmannii

The polysaccharide (VSP) from the gum exudate of quaruba (Vochysia lehmannii) had two components of almost identical M. centred at 24,800, as shown by HSPEC-MALLS. The presence of aggregates was shown since carboxy-reduction gave VSP-RED, which contained low molecular weight components with M-w 19,000 > 5800 and polydispersity ratios dn/dc 0.160 and 0.149, respectively. VSP formed low viscosity aqueous solutions and acid hydrolysis gave Man (30%), Ara (16%), Gal (10%), and Glc (14%). The latter arose partly from GlcA (30%). Methylation analysis revealed mainly neutral units of 2-O- (60%) and 2,3-di-O-substituted Manp (5%), and those of nomeducing ends (8%), 2-O- (3%), and 4-O-substituted Arap and/or 5-O-substituted Araf units (6%). VSP-RED contained Glc (45%), Man (35%), and Ara (13%) and methylation analysis indicated mainly 4-O-substituted Glcp (31%) and 2-O- (51%) and 2,3-di-O-substituted Manp units (5%). A predominant alternating structure for VSP was shown by its C-13 NMR spectrum, which contained 10 main signals and a small one of C-6 of GlcpA. This was confirmed by formation, on partial hydrolysis of VSP, of a tetrasaccharide, which was characterised by NMR spectroscopy and ESI-MS as beta-GlcpA-(1 --> 2)-alpha-Manp-(1 --> 4)-beta-GlcpA-(1 --> 2)-Man, which arose from the main chain, thus confirming VSP to be a glycoglucuronomannan. (C) 2004 Elsevier Ltd. All rights reserved

Structural features and anticoagulant activities of a novel natural low molecular weight heparin from the shrimp Penaeus brasiliensis

A natural low molecular weight heparin (8.5 kDa), with an anticoagulant activity of 95 IU/mg by the USP assay, was isolated from the shrimp Penaeus brasiliensis. the crustacean heparin was susceptible to both heparinase and heparitinase II from Flavobacterium heparinum forming tri- and di-sulfated disaccharides as the mammalian heparins. C-13 and H-1 NMR spectroscopy revealed that the shrimp heparin was enriched in both glucuronic and non-sulfated iduronic acid residues. the in vitro anticlotting activities in different steps of the coagulation cascade have shown that its anticoagulant action is mainly exerted through the inhibition of factor Xa and heparin cofactor II-mediated inhibition of thrombin. the shrimp heparin has also a potent in vivo antithrombotic activity comparable to the mammalian low molecular weight heparins. (C) 1999 Elsevier Science B.V. All rights reserved.Universidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, BrazilUniv Fed Rio Grande Norte, Dept Bioquim, Natal, RN, BrazilLoyola Med Sch, Dept Pathol, Maywood, IL USAUniv Fed Parana, Dept Bioquim, BR-80060000 Curitiba, Parana, BrazilUniversidade Federal de São Paulo, Escola Paulista Med, Dept Bioquim, BR-04044020 São Paulo, BrazilWeb of Scienc