Immunomodulatory and Therapeutic Potential of a Mycelial Lectin from Aspergillus nidulans

Singh, Ram Sarup; Bhari, Ranjeeta; Rana, Vikas; Tiwary, Ashok K.

doi:10.1007/s12010-011-9281-4

Cited by 20 publications

(6 citation statements)

References 38 publications

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“…The expression of lectins by pathogenic microorganisms has been correlated to the organism attachment and invasion to host tissues (Mendes-Giannini et al, 2000; Singh et al, 2011). Interestingly, Hc has components with lectin activity on the yeast surface that can bind to surface molecules on murine macrophages (Taylor et al, 1998; Duarte-Escalante et al, 2003).…”

Section: Yeast Cell Surfacementioning

confidence: 99%

Surface architecture of Histoplasma capsulatum

Guimarães

Cerqueira²,

Nosanchuk

2011

Front. Microbio.

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The dimorphic fungal pathogen Histoplasma capsulatum is the most frequent cause of clinically significant fungal pneumonia in humans. H. capsulatum virulence is achieved, in part, through diverse and dynamic alterations to the fungal cell surface. Surface components associated with H. capsulatum pathogenicity include carbohydrates, lipids, proteins, and melanins. Here, we describe the various structures comprising the cell surface of H. capsulatum that have been associated with virulence and discuss their involvement in the pathobiology of disease.

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Section: Yeast Cell Surfacementioning

confidence: 99%

Surface architecture of Histoplasma capsulatum

Guimarães

Cerqueira²,

Nosanchuk

2011

Front. Microbio.

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“…Few of them have also been evidenced to possess mitogenic 22 , 23 , 24 and immunomodulatory properties. 25 …”

Section: Introductionmentioning

confidence: 99%

Lectin activity in mycelial extracts of Fusarium species

Bhari

Kaur

Singh

2016

Brazilian Journal of Microbiology

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Lectins are non-immunogenic carbohydrate-recognizing proteins that bind to glycoproteins, glycolipids, or polysaccharides with high affinity and exhibit remarkable ability to agglutinate erythrocytes and other cells. In the present study, ten Fusarium species previously not explored for lectins were screened for the presence of lectin activity. Mycelial extracts of F. fujikuroi, F. beomiformii, F. begoniae, F. nisikadoi, F. anthophilum, F. incarnatum, and F. tabacinum manifested agglutination of rabbit erythrocytes. Neuraminidase treatment of rabbit erythrocytes increased lectin titers of F. nisikadoi and F. tabacinum extracts, whereas the protease treatment resulted in a significant decline in agglutination by most of the lectins. Results of hapten inhibition studies demonstrated unique carbohydrate specificity of Fusarium lectins toward O-acetyl sialic acids. Activity of the majority of Fusarium lectins exhibited binding affinity to d-ribose, l-fucose, d-glucose, l-arabinose, d-mannitol, d-galactosamine hydrochloride, d-galacturonic acid, N-acetyl-d-galactosamine, N-acetyl-neuraminic acid, 2-deoxy-d-ribose, fetuin, asialofetuin, and bovine submaxillary mucin. Melibiose and N-glycolyl neuraminic acid did not inhibit the activity of any of the Fusarium lectins. Mycelial extracts of F. begoniae, F. nisikadoi, F. anthophilum, and F. incarnatum interacted with most of the carbohydrates tested. F. fujikuroi and F. anthophilum extracts displayed strong interaction with starch. The expression of lectin activity as a function of culture age was investigated. Most species displayed lectin activity on the 7th day of cultivation, and it varied with progressing of culture age.

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“…Additionally, the lectin promoted an antianaphylactic effect and prevented Arthus reaction in vivo; a therapeutic potential against ulcerative colitis was observed in rats pretreated with the lectin via intraperitoneal injection that showed better recovery comparing with posttreated rats. The high specificity of this lectin for N-acetylgalactosamine (GalNAc) residues on epithelial cells could trigger the therapeutic effect [56]. …”

Section: Lectin Induced Mechanisms Of Immunological and Inflammatomentioning

confidence: 99%

Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications

Coelho

Silva

Lima

et al. 2017

Evidence-Based Complementary and Alternative Medicine

161

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Lectins are proteins extensively used in biomedical applications with property to recognize carbohydrates through carbohydrate-binding sites, which identify glycans attached to cell surfaces, glycoconjugates, or free sugars, detecting abnormal cells and biomarkers related to diseases. These lectin abilities promoted interesting results in experimental treatments of immunological diseases, wounds, and cancer. Lectins obtained from virus, microorganisms, algae, animals, and plants were reported as modulators and tool markers in vivo and in vitro; these molecules also play a role in the induction of mitosis and immune responses, contributing for resolution of infections and inflammations. Lectins revealed healing effect through induction of reepithelialization and cicatrization of wounds. Some lectins have been efficient agents against virus, fungi, bacteria, and helminths at low concentrations. Lectin-mediated bioadhesion has been an interesting characteristic for development of drug delivery systems. Lectin histochemistry and lectin-based biosensors are useful to detect transformed tissues and biomarkers related to disease occurrence; antitumor lectins reported are promising for cancer therapy. Here, we address lectins from distinct sources with some biological effect and biotechnological potential in the diagnosis and therapeutic of diseases, highlighting many advances in this growing field.

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Immunomodulatory and Therapeutic Potential of a Mycelial Lectin from Aspergillus nidulans

Cited by 20 publications

References 38 publications

Surface architecture of Histoplasma capsulatum

Surface architecture of Histoplasma capsulatum

Lectin activity in mycelial extracts of Fusarium species

Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications

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