Lectin activity in mycelial extracts of Fusarium species

Abstract

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.

New Rabbit Erythrocyte Specific Mycelial Lectins from Fusarium sp. with Complex Saccharide Specificity

“…In a recent report, the majority of the Fusarium sp. lectins have agglutinated only rabbit erythrocytes [36] which corroborate our findings. Lectins from Fusarium sp.…”

“…It is a well-known plant pathogen and sometimes it also causes various infections in humans. In earlier studies, our group has reported many lectin-positive Fusarium species [35,36]. The present work is an augmentation of our earlier work to investigate lectin activity in new Fusarium sp., which has not been investigated previously.…”

Sialic acid and biology of life: An introduction

“…A lectin has been reported to occur in Australian indigenous mushroom Psathyrella asperospora (P. asperospora) termed as PAL with cyotoxic properties on human colon cancer HT29 and monkey kidney VERO revealing binding preference toward N-acetylglucosamine (GlcNAc) and sialic acid (Neu5Ac) [175]. Most Fusarium lectins exhibit binding affinity to d-ribose, l-fucose, d-glucose, l-arabinose, d-mannitol, d-galactosamine hydrochloride, d-galacturonic acid, N-acetyl-d-galactosamine, N-acetylneuraminic acid, 2-deoxy-d-ribose, fetuin, asialofetuin, and bovine submaxillary mucin (BSM) [176].…”

Microscopy examination of red blood and yeast cell agglutination induced by bacterial lectins

“…The ability of lectins to selectively agglutinate red blood cells is utilized for human and animal blood group typing and subtyping [14–16]. Hemagglutination (HA) or yeast agglutination assay (YA) is used to search for new lectins of various organisms [17, 18] as well as for the rapid testing of lectin activity [19]. The agglutination of microbial cells often serves for studying the interactions between lectins and pathogens [20].…”

“…Agglutination (inhibition) assays were effectively utilized for testing agglutination activity and for specificity studies of non-purified lectins in homogenized mycelium [17], fish serum [21], shrimp plasma [27] or fish skin mucus [28]. Also, it was confirmed that this method can be used for testing recombinant lectins, which were produced by E .…”