Characterization, Occurrence, and Molecular Cloning of a Lectin from<i>Grifola frondosa</i>: Jacalin-Related Lectin of Fungal Origin

Nagata, Yoshiho; Yamashita, M; Honda, Hiroaki; Akabane, Junko; Uehara, K.; Saito, Akihiro; Sumisa, Futoshi; Nishibori, Kozo; Oodaira, Yasuo

doi:10.1271/bbb.69.2374

Cited by 23 publications

(15 citation statements)

References 21 publications

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“…From fruiting bodies of the basidiomycetes Hygrophorus russula and Grifola frondosa, two mannose-specific lectins, termed H. russula lectin (HRL) and G. frondosa lectin (GFL), were isolated and characterized (Nagata et al 2005;Suzuki et al 2012). The amino acid sequence of these proteins is related to that of Jacalin from plants, and some plant members of this lectin family have recently been shown to protect the producing plants from herbivorous insects (Al Atalah et al 2014).…”

Section: Additional Families Of Potential Fungal Defense Lectinsmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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Fruiting bodies or sporocarps of dikaryotic (ascomycetous and basidiomycetous) fungi, commonly referred to as mushrooms, are often rich in entomotoxic and nematotoxic proteins that include lectins and protease inhibitors. These protein toxins are thought to act as effectors of an innate defense system of mushrooms against animal predators including fungivorous insects and nematodes. In this review, we summarize current knowledge about the structures, target molecules, and regulation of the biosynthesis of the best characterized representatives of these fungal defense proteins, including galectins, beta-trefoil-type lectins, actinoporin-type lectins, beta-propeller-type lectins and beta-trefoil-type chimerolectins, as well as mycospin and mycocypin families of protease inhibitors. We also present an overview of the phylogenetic distribution of these proteins among a selection of fungal genomes and draw some conclusions about their evolution and physiological function. Finally, we present an outlook for future research directions in this field and their potential applications in medicine and crop protection.

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Section: Additional Families Of Potential Fungal Defense Lectinsmentioning

confidence: 99%

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Sabotič

Ohm

Künzler

2015

Appl Microbiol Biotechnol

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“…Cloning and structural analysis revealed that the hemolytic Laetiporus sulphureus lectin also contains a distantly related ricin-B domain but due to the presence of an in tandem arrayed hemolytic domain should be classified into a distinct (sub) family [10,11]. Other recently discovered families of fungal lectins are represented by the mycelial aggregatespecific lectins from Pleurotus cornucopiae [12], the Grifola frondosa fruit body lectin [13], the Flammulina velutipes immunomodulatory protein [14], the lectin from Rhizopus stolonifer [15], and the Psathyrella velutina fruit body lectin [16]. In addition, putative expressed proteins closely related to the snowdrop (Galanthus nivalis) lectin family have been identified in several fungal species [17,18].…”

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The Sclerotinia sclerotiorum agglutinin represents a novel family of fungal lectins remotely related to the Clostridium botulinum non-toxin haemagglutinin HA33/A

et al. 2007

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Previous studies indicated that sclerotes of the phytopathogenic Ascomycete Sclerotinia sclerotiorum contain a lectin that based on its molecular structure, specificity and N-terminal amino acid sequence could not be classified yet into any lectin family. Using a combination of molecular cloning, frontal affinity chromatography and molecular modelling the identity of the S. sclerotiorum agglutinin (SSA) was analyzed. Molecular cloning demonstrated that SSA shares no sequence similarity with any known fungal lectin or protein. The lectin is synthesized as a 153 amino acid polypeptide without signal peptide and undergoes apart from the removal of the N-terminal methionine no further processing. Frontal affinity chromatography revealed that the binding site of SSA primarily accommodates a non-reducing terminal GalNAc with a preference for the alpha- over the beta-anomer. SSA also strongly interacts with both glycolipid type glycans with terminal non-reducing Gal or GalNAc and galactosylated N-glycans. SSA shares a residual sequence similarity with part of the non-toxin haemagglutinin HA33/A from Clostridium botulinum. Molecular modeling using the three-dimensional structure of HA33/A as a template indicated that SSA can fold into a similar beta-trefoil domain. Though these results should be interpreted with care it is tempting to speculate that the Sclerotiniaceae lectins thus appear to be structurally related to the ricin-B superfamily. All evidence suggests that SSA represents a novel family of fungal lectins with a unique sequence and sugar-binding properties. Taking into account that orthologues of SSA are fairly common within the family Sclerotiniaceae but could not be identified in any other fungal species one can reasonably conclude that SSA-type lectins are confined to a small taxonomic group of the Ascomycota.

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“…For jacalin-related lectins (pfam01419), the situation is less clear. Recent reports claimed that the zymogen granule membrane protein 16 found in mouse, rat, and a few other vertebrates, as well as the lectin from the mushroom Grifola frondosa, belong to the jacalin family (Nagata et al, 2005). However, the residual sequence identities are low, suggesting that, even if a common ancestral domain occurred in an early eukaryote, parallel evolution eventually led to distantly related modern animal and fungal homologs of the plant jacalins.…”

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A Novel Family of Lectins Evolutionarily Related to Class V Chitinases: An Example of Neofunctionalization in Legumes

et al. 2006

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A lectin has been identified in black locust (Robinia pseudoacacia) bark that shares approximately 50% sequence identity with plant class V chitinases but is essentially devoid of chitinase activity. Specificity studies indicated that the black locust chitinase-related agglutinin (RobpsCRA) preferentially binds to high-mannose N-glycans comprising the proximal pentasaccharide core structure. Closely related orthologs of RobpsCRA could be identified in the legumes Glycine max, Medicago truncatula, and Lotus japonicus but in no other plant species, suggesting that this novel lectin family most probably evolved in an ancient legume species or possibly an earlier ancestor. This identification of RobpsCRA not only illustrates neofunctionalization in plants, but also provides firm evidence that plants are capable of developing a sugar-binding domain from an existing structural scaffold with a different activity and accordingly sheds new light on the molecular evolution of plant lectins.

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Characterization, Occurrence, and Molecular Cloning of a Lectin fromGrifola frondosa: Jacalin-Related Lectin of Fungal Origin

Cited by 23 publications

References 21 publications

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

Entomotoxic and nematotoxic lectins and protease inhibitors from fungal fruiting bodies

The Sclerotinia sclerotiorum agglutinin represents a novel family of fungal lectins remotely related to the Clostridium botulinum non-toxin haemagglutinin HA33/A

A Novel Family of Lectins Evolutionarily Related to Class V Chitinases: An Example of Neofunctionalization in Legumes

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