Lectin Variation in Members of <i>Rhizoctonia</i> Species

Abstract

Isolates from two multinucleate Rhizoctonia species, namely Rhizoctonia solani and Rhizoctonia circinata, and binucleate Rhizoctonia spp., were evaluated for the presence of lectins, using human erythrocytes. Isolates from R. solani had similar lectins across the anastomosis groups. Agglutination profiles, however, revealed individual preferences for human blood types but with a general preference for type A over B and O. R. solani lectins had a general affinity for N-acetyl-D-galactosamine and mucin. Also, some isolates from the binucleate Rhizoctonia AG-DII, had lectins that showed strong affinity for glycoproteins, fetuin and mucin. There was no lectin activity in members of R. circinata. The lectins in members of the genus Rhizoctonia varied in content and character across the species sampled but had similar affinity for mucin. Furthermore, 62% of the self-anastomosing and 35% of the non-self anastomosing isolates tested showed lectin activity. The presence of lectins in both self-anastomosing and non-self anastomosing isolates suggests that lectins may not be directly involved in the recognition process in hyphal anastomosis.

Suppression subtractive hybridization and comparative expression of a pore-forming toxin and glycosyl hydrolase genes in Rhizoctonia solani during potato sprout infection

“…These processes include cellular signaling, differentiation, and host-pathogen interactions through the specific recognition of glycol conjugates of the host cell membrane by lectins present on the surface of the fungal wall (Guillot and Konska 1997;Hamshou et al 2007;Khan and Khan 2011). In accordance with our study, fungal lectins have been previously detected in the mycelium and sclerotia of R. solani strains of different anastomosis groups (Kellens and Peumans 1991;Mghalu et al 2004) with a reported role in fungal growth and development (Leonidas et al 2007). Additionally, R. solani lectins were revealed to act as storage proteins (Skamnaki et al 2013).…”

Lectins from Mycelia of Basidiomycetes

“…A number of studies are devoted to the lectins of plant pathogenic basidiomycetes, such as Athelia rorfsii (teleomorph: Sclerotium rolfsii ) and various Rhizoctonia species [ 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 ]. By the using of affinity chromatography, a lectin, RSA ( Rhizoctonia solani lectin), was isolated from Rhizoctonia solani mycelium [ 48 ].…”

Structural analysis of the Rhizoctonia solani agglutinin reveals a domain‐swapping dimeric assembly

“…The protein is not glycosylated . The lectin was detected in R. solani strains of many different anastomosis groups . Furthermore, a detailed analysis of the accumulation and distribution of the RSA in the mycelium and the sclerotia revealed that the lectin is developmentally regulated .…”

“…Basidiomycetes constitute a rich source of fungal lectins exhibiting var-ious carbohydrate-binding properties and structures [2]. Although fungal lectins have a role as storage proteins [2,3] and are also involved in morphogenesis and development of the fungi, their physiological importance remains enigmatic [4][5][6]. In 1987, Vranken et al [7] first reported the purification and characterization of a lectin from Rhizoctonia solani (RSA).…”

“…We determined the amino acid sequence of RSA and also determined the crystal structures of the free form and the RSA-N-acetylgalactosamine complex at 1.6 and 2. 2 A resolution, respectively. RSA is a homodimer comprised of two monomers adopting the b-trefoil fold.…”