Lectin typing of methicillin-resistant Staphylococcus aureus

MUñTOZ, A.; Álvarez, Óscar García; Alonso, Beatriz; Llovo, J.

doi:10.1099/00222615-48-5-495

Cited by 7 publications

(5 citation statements)

References 24 publications

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“…Marine organisms are recognized as rich sources of diverse and biologically-active molecules, many lectins from red and green marine algae have been isolated and characterised to date from more than 40 species. Amongst activities of potential therapeutic and diagnostic interest are the inhibition of fungal growth [ 4 ], induction and inhibition of human lymphocyte transformation [ 5 ], identification of methacillin-resistant Streptococcus aureus [ 6 ], induction of mitogenic activity [ 7 ], antibiotic activity against marine vibrios [ 8 ], endothelium-dependent relaxation of the rat aorta [ 9 ], inhibition of platelet aggregation [ 10 ], and as an anti-HIV protein [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Modulation of the pharmacological effects of enzymatically-active PLA2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga

et al. 2008

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BackgroundAn interaction between lectins from marine algae and PLA2 from rattlesnake was suggested some years ago. We, herein, studied the effects elicited by a small isolectin (BTL-2), isolated from Bryothamnion triquetrum, on the pharmacological and biological activities of a PLA2 isolated from rattlesnake venom (Crotalus durissus cascavella), to better understand the enzymatic and pharmacological mechanisms of the PLA2 and its complex.ResultsThis PLA2 consisted of 122 amino acids (approximate molecular mass of 14 kDa), its pI was estimated to be 8.3, and its amino acid sequence shared a high degree of similarity with that of other neurotoxic and enzymatically-active PLA2s. BTL-2 had a molecular mass estimated in approximately 9 kDa and was characterized as a basic protein. In addition, BTL-2 did not exhibit any enzymatic activity.The PLA2 and BTL-2 formed a stable heterodimer with a molecular mass of approximately 24–26 kDa, estimated by molecular exclusion HPLC. In the presence of BTL-2, we observed a significant increase in PLA2 activity, 23% higher than that of PLA2 alone. BTL-2 demonstrated an inhibition of 98% in the growth of the Gram-positive bacterial strain, Clavibacter michiganensis michiganensis (Cmm), but only 9.8% inhibition of the Gram-negative bacterial strain, Xanthomonas axonopodis pv passiflorae (Xap). PLA2 decreased bacterial growth by 27.3% and 98.5% for Xap and Cmm, respectively, while incubating these two proteins with PLA2-BTL-2 inhibited their growths by 36.2% for Xap and 98.5% for Cmm.PLA2 significantly induced platelet aggregation in washed platelets, whereas BTL-2 did not induce significant platelet aggregation in any assay. However, BTL-2 significantly inhibited platelet aggregation induced by PLA2. In addition, PLA2 exhibited strong oedematogenic activity, which was decreased in the presence of BTL-2. BTL-2 alone did not induce oedema and did not decrease or abolish the oedema induced by the 48/80 compound.ConclusionThe unexpected results observed for the PLA2-BTL-2 complex strongly suggest that the pharmacological activity of this PLA2 is not solely dependent on the presence of enzymatic activity, and that other pharmacological regions may also be involved. In addition, we describe for the first time an interaction between two different molecules, which form a stable complex with significant changes in their original biological action. This opens new possibilities for understanding the function and action of crude venom, an extremely complex mixture of different molecules.

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Section: Introductionmentioning

confidence: 99%

Modulation of the pharmacological effects of enzymatically-active PLA2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga

et al. 2008

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“…Amongst the biological properties of algal lectins, there are many that have the potential for therapeutic and diagnostic application. Algal lectins have been shown to inhibit fungal growth (Melo et al, 1997), induce mitogenic activity (Kawakubo et al, 1999), and identify methicillinresistant strains of Staphylococcus aureus (Mun˜oz et al, 1999). In spite of the wide range of biological activity found with marine algal lectins, their functions within the host plant have not been established.…”

Section: Introductionmentioning

confidence: 98%

Micro-heterogeneity and molecular assembly of the haemagglutinins from the red algaeBryothamnion seaforthiiandB. triquetrumfrom the Caribbean Sea

Medina-Ramírez

Gibbs

Calvete

et al. 2007

European Journal of Phycology

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Haemagglutinins have been isolated from two red marine algae Bryothamnion seaforthii and B. triquetrum, which were harvested from the Caribbean Sea, Falcon State, Venezuela. The mass spectra of the haemagglutinins isolated from B. seaforthii showed five monomer peaks (9057.4-9088.8 Da) and those from B. triquetrum showed three peaks (8981.5-8990.2 Da). Isoelectric focusing, under denaturing conditions, gave rise to multiple bands for the haemagglutinins of both species but only one band was observed under native conditions. Gel permeation experiments suggest that the monomer haemagglutinins can readily associate to form dimers, trimers and tetramers. The haemagglutinins agglutinate papainized human A, B and O erythrocytes; the activity is inhibited by glycoconjugates, but not by simple sugars, and is maintained after heating to temperatures up to 90 C. The amino acid sequence of the haemagglutinin from B. seaforthii has been determined together with a partial sequence for that from B. triquetrum. The isolation, and some characterization, of haemagglutinins from B. seaforthii and B. triquetrum, collected from the Ceara coast of Brazil, have previously been reported. Some differences and similarities of these macromolecules obtained from the two different locations are discussed.

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“…Lectins are proteins of non-immune origin that bind specifically to carbohydrates. 7 The selectivity of lectins for microbial-surface sugars has been demonstrated for bacteria of the genera Staphylococcus, 8,9,10 Neisseria, 11,12,13 Haemophilus, 14 Campylobacter 15 and Streptococcus 16,17 as well as for protozoa 18 and yeasts of the genus Candida. 19,20,21,22 In the present study we evaluated our results about the use of lectins for the typing of clinical Candida isolates.…”

Section: Introductionmentioning

confidence: 99%

Lectin typing of five medically important Candida species

Muñoz¹,

Alonso²,

Álvarez³

et al. 2003

Mycoses

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This study reports the patterns of agglutination of 93 clinical Candida isolates by 14 commercial lectins. The isolates were of the species Candida albicans (55), C. tropicalis (12), C. guilliermondii (10). C. glabrata (eight) and C. parapsilosis (eight). Hundred percent of isolates were agglutinated, at least, by a panel of three lectins: Canavalia ensiformis (ConA), Lens culinaris (LCA) and Pisum sativum (PSA), all of them with alpha-D-mannose specificity. In addition, another panel of three lectins could distinguish between C. glabrata, C. tropicalis and C. albicans. Lectin typing may be of potential value for taxonomic and epidemiological studies of yeasts in clinical laboratories.

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Lectin typing of methicillin-resistant Staphylococcus aureus

Cited by 7 publications

References 24 publications

Modulation of the pharmacological effects of enzymatically-active PLA2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga

Modulation of the pharmacological effects of enzymatically-active PLA2 by BTL-2, an isolectin isolated from the Bryothamnion triquetrum red alga

Micro-heterogeneity and molecular assembly of the haemagglutinins from the red algaeBryothamnion seaforthiiandB. triquetrumfrom the Caribbean Sea

Lectin typing of five medically important Candida species

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