Journal articles: 'Fungal Lectin'

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Lebreton, Annie, François Bonnardel, Yu-Cheng Dai, Anne Imberty, Francis M. Martin, and Frédérique Lisacek. "A Comprehensive Phylogenetic and Bioinformatics Survey of Lectins in the Fungal Kingdom." Journal of Fungi 7, no. 6 (June 7, 2021): 453. http://dx.doi.org/10.3390/jof7060453.

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Fungal lectins are a large family of carbohydrate-binding proteins with no enzymatic activity. They play fundamental biological roles in the interactions of fungi with their environment and are found in many different species across the fungal kingdom. In particular, their contribution to defense against feeders has been emphasized, and when secreted, lectins may be involved in the recognition of bacteria, fungal competitors and specific host plants. Carbohydrate specificities and quaternary structures vary widely, but evidence for an evolutionary relationship within the different classes of fungal lectins is supported by a high degree of amino acid sequence identity. The UniLectin3D database contains 194 fungal lectin 3D structures, of which 129 are characterized with a carbohydrate ligand. Using the UniLectin3D lectin classification system, 109 lectin sequence motifs were defined to screen 1223 species deposited in the genomic portal MycoCosm of the Joint Genome Institute. The resulting 33,485 putative lectin sequences are organized in MycoLec, a publicly available and searchable database. These results shed light on the evolution of the lectin gene families in fungi.

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Wimmerova, Michaela, Edward Mitchell, Jean-Frederic Sanchez, Catherine Gautier, and Anne Imberty. "Crystal Structure of Fungal Lectin." Journal of Biological Chemistry 278, no. 29 (May 5, 2003): 27059–67. http://dx.doi.org/10.1074/jbc.m302642200.

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Sabotič and Kos. "CNL–Clitocybe nebularis Lectin—The Fungal GalNAcβ1-4GlcNAc-Binding Lectin." Molecules 24, no. 23 (November 20, 2019): 4204. http://dx.doi.org/10.3390/molecules24234204.

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Clitocybe nebularis lectin (CNL) is present in fruiting bodies of clouded agaric along with several similar isolectins that are all small and stable proteins. It is a beta-trefoil type lectin forming homodimers that are essential for its functionality. It binds specifically N,N’-diacetyllactosediamine (GalNAcβ1-4GlcNAc, LacDiNac) and human blood group A determinant-containing glycan epitopes. Its most probable function is to defend fruiting bodies against predators and parasites. In addition, an endogenous regulatory function is possible for CNL, as indicated by its interaction with fungal protease inhibitors sharing the beta-trefoil fold. CNL is toxic to insects, nematodes and amoebae, as well as to leukemic T-cell lines. Bivalent carbohydrate binding is essential for the toxicity of CNL, against both invertebrates and cancer-derived cell lines. In addition, CNL exhibits potent immunostimulation of human dendritic cells, resulting in a strong T helper cell type 1 response. Based on its unique characteristics, CNL is a promising candidate for applications in human and veterinary medicine as well as in agriculture, for plant protection.

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Gutiérrez-Aguirre, Ion, Peter Trontelj, Peter Maček, Jeremy H. Lakey, and Gregor Anderluh. "Membrane binding of zebrafish actinoporin-like protein: AF domains, a novel superfamily of cell membrane binding domains." Biochemical Journal 398, no. 3 (August 29, 2006): 381–92. http://dx.doi.org/10.1042/bj20060206.

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Actinoporins are potent eukaryotic pore-forming toxins specific for sphingomyelin-containing membranes. They are structurally similar to members of the fungal fruit-body lectin family that bind cell-surface exposed Thomsen–Friedenreich antigen. In the present study we found a number of sequences in public databases with similarity to actinoporins. They originate from three animal and two plant phyla and can be classified in three families according to phylogenetic analysis. The sequence similarity is confined to a region from the C-terminal half of the actinoporin molecule and comprises the membrane binding site with a highly conserved P-[WYF]-D pattern. A member of this novel actinoporin-like protein family from zebrafish was cloned and expressed in Escherichia coli. It displays membrane-binding behaviour but does not have permeabilizing activity or sphingomyelin specificity, two properties typical of actinoporins. We propose that the three families of actinoporin-like proteins and the fungal fruit-body lectin family comprise a novel superfamily of membrane binding proteins, tentatively called AF domains (abbreviated from actinoporin-like proteins and fungal fruit-body lectins).

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Wanchoo, Arun, Michael W. Lewis, and Nemat O. Keyhani. "Lectin mapping reveals stage-specific display of surface carbohydrates in in vitro and haemolymph-derived cells of the entomopathogenic fungus Beauveria bassiana." Microbiology 155, no. 9 (September 1, 2009): 3121–33. http://dx.doi.org/10.1099/mic.0.029157-0.

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The entomopathogenic fungus Beauveria bassiana and its insect host target represent a model system with which to examine host–pathogen interactions. Carbohydrate epitopes on the surfaces of fungal cells play diverse roles in processes that include adhesion, non-self recognition and immune invasion with respect to invertebrate hosts. B. bassiana produces a number of distinct cell types that include aerial conidia, submerged conidia, blastospores and haemolymph-derived cells termed in vivo blastospores or hyphal bodies. In order to characterize variations in the surface carbohydrate epitopes among these cells, a series of fluorescently labelled lectins, combined with confocal microscopy and flow cytometry to quantify the response, was used. Aerial conidia displayed the most diverse lectin binding characteristics, showing reactivity against concanavalin A (ConA), Galanthus nivalis (GNL), Griffonia simplicifolia (GSII), Helix pomatia (HPA), Griffonia simplicifolia isolectin (GSI), peanut agglutinin (PNA), Ulex europaeus agglutinin I (UEAI) and wheatgerm agglutinin (WGA), and weak reactivity against Ricinus communis I (RCA), Sambucus nigra (SNA), Limax flavus (LFA) and Sophora japonica (SJA) lectins. Lectin binding to submerged conidia was similar to that to aerial conidia, except that no reactivity against UEAI, HPA and SJA was noted, and WGA appeared to bind strongly at specific polar spots. In contrast, the majority of in vitro blastospores were not bound by ConA, GNL, GSII, GSI, SNA, UEAI, LFA or SJA, with PNA binding in large patches, and some polarity in WGA binding noted. Significant changes in lectin binding also occurred after aerial conidial germination and in cells grown on either lactose or trehalose. For germinated conidia, differential lectin binding was noted between the conidial base, the germ tube and the hyphal tip. Fungal cells isolated from the haemolymph of the infected insect hosts Manduca sexta and Heliothis virescens appeared to shed most carbohydrate epitopes, displaying binding only to the GNL, PNA and WGA lectins. Ultrastructural examination of the haemolymph-derived cells revealed the presence of a highly ordered outermost brush-like structure not present on any of the in vitro cells. Haemolymph-derived hyphal bodies placed into rich broth medium showed expression of several surface carbohydrate epitopes, most notably showing increased PNA binding and strong binding by the RCA lectin. These data indicate robust and diverse production of carbohydrate epitopes on different developmental stages of fungal cells and provide evidence that surface carbohydrates are elaborated in infection-specific patterns.

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Jiang, Na, Yuqing Wang, Jing Zhou, Ruxiao Zheng, Xiao Yuan, Miaomiao Wu, Jinku Bao, and Chuanfang Wu. "A novel mannose-binding lectin from Liparis nervosa with anti-fungal and anti-tumor activities." Acta Biochimica et Biophysica Sinica 52, no. 10 (August 27, 2020): 1081–92. http://dx.doi.org/10.1093/abbs/gmaa090.

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Abstract Plant lectins are carbohydrate-binding proteins with nonimmune origin, which can reversibly bind with carbohydrates, agglutinate cells, and precipitate polysaccharides and glycoconjugates. Plant lectins have attracted much attention for their anti-virus, anti-proliferation, and pro-apoptosis properties. Thus the exploration of new lectins has received special attention. Here we purified a mannose-binding lectin from the rhizomes of Liparis nervosa by ion exchange chromatography on DEAE-Sepharose, affinity chromatography on Mannose-Sepharose 4B, and gel filtration chromatography on Sephacryl S-100. The purified L. nervosa lectin (LNL) was identified to be a monomeric protein with a molecular mass of 13 kDa. LNL exhibited hemagglutinating activity towards rabbit erythrocytes, and its activity could be strongly inhibited by D-mannose, N-acetyl glucosamine and thyroglobulin. In vitro experiments showed that LNL exhibited a comparable anti-fungal activity against Piricularia oryzae (Cavara), Bipolaris maydis, Fusarium graminearum, and Sclerotium rolfsii, and anti-proliferation activity against tumor cells by inducing apoptosis. The full-length cDNA sequence of LNL is 715 bp in length and contains a 525 bp open reading frame (ORF) encoding a 110-residue mature protein. It was predicted to have three mannose-binding conserved motifs ‘QXDXNXVXY’. The binding pattern of LNL was further revealed by homology modeling and molecular docking. We demonstrated that LNL is not only a potential therapeutic candidate against tumor but also a new anti-fungal agent.

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Benhamou, N., N. Gilboa-Garber, J. Trudel, and A. Asselin. "A new lectin-gold complex for ultrastructural localization of galacturonic acids." Journal of Histochemistry & Cytochemistry 36, no. 11 (November 1988): 1403–11. http://dx.doi.org/10.1177/36.11.3049790.

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We report the development of a cytochemical affinity technique for detection of galacturonic acids at the ultrastructural level. The highly purified gonad lectin from Aplysia depilans (AGL) was tagged with colloidal gold particles and used for labeling carbohydrates in resin-embedded sections of various plant and fungal tissues. Patterns of AGL binding sites were compared to those obtained with a D-galactose-specific lectin, Ricinus communis agglutinin I. Differences in labeling patterns were noted, indicating that the lectins exhibited differential carbohydrate binding. In addition, the considerable loss of labeling over isolated wheat coleoptile walls treated for removal of pectin, after incubation with the AGL-gold complex, strongly suggested an affinity of AGL for pectic substances. A series of cytochemical controls, including sugar inhibition tests, has proven the specificity of the technique and the high affinity of AGL towards galacturonic acids. The potential value of this new lectin for ultrastructural studies on cell wall pectic substances in plant biology and pathology is demonstrated.

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Odiegwu C.N.C, Emenuga V. N., Ogamba S. E., Obi C. M., and Ejike C. E. "Microbial agglutination and lymphocyte blastogenesis potentials of isolated Achatina achatina snail lectin." World Journal of Advanced Research and Reviews 9, no. 1 (January 30, 2021): 104–13. http://dx.doi.org/10.30574/wjarr.2021.9.1.0505.

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Lectins are involved in recognition phenomena and their ability to bind particular Carbohydrate structures are the key to their biological functions. Bacteria typically attaches to prospective host cell membranes in receptors with lectin like sugar specificity. This is of great importance as the adherence of bacteria to host tissue surfaces is the initial event in bacterial infection. Lectins are also known to play important roles in immune system by recognizing carbohydrates that are found exclusively on pathogens, or that are inaccessible on host cells. This ability of lectins to selectively bind or agglutinate specific sugars have made them useful tools for the characterization of certain cell types or fragments, to detect cells in different states of development, to distinguish normal from tumour cells and to separate different cell types by affinity chromatography. A total of 120 samples of local Achatina achatina snail specie were collected, authenticated at the Zoology Department of the University of Nigeria, Nsukka and 80mls of pooled crude Lectin extract was obtained. Purifications were performed on 20mls of the crude extract in three steps viz, Ammonium sulphate precipitation and Dialysis (Partial purifications), Con A Sepharose 4B affinity chromatography column (Complete purification). The affinity purified lectin was used in all the tests conducted in this research. The crude, partially and complete/affinity purified lectin extracts were subjected to Haemagglutination and Protein Assay tests. The Molecular weight was deduced by Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) method. The microbial agglutination potentials of the lectin was assessed by testing typed bacterial organisms viz, Salmonella typhimurium, Escherichia coli, Lactobacilli acidophilus, Pseudomonas aeruginosa, Staphylococcus aureus, Klebsiella aeruginosa and four typed fungal organisms: Aspergillus niger, Trichophyton mentagrophytes, Candida albicans and A. flavus. The lectin’s Lymphocyte blastogenesis activities was determined by its incubation with human lymphocytes for mitogenic stimulation assay. The results of the research showed as follows: On complete/affinity purification, 15mls of pure sample containing only the high molecular weight lectin was obtained. On standardization, the respective haemagglutination tests on the crude, partially and affinity purified lectin showed preferential agglutinations with Blood group A type. Only S. typhimurium (+++), E. coli (+) and L. acidophilus (+) reacted with the lectin but in different strengths. Incubation of the lectin with lymphocytes from human serum showed that it has the ability to stimulate lymphocytes to undergo mitosis. This research has therefore succeeded in assessing the Microbial agglutination and Lymphocyte blastogenesis potentials of the isolated and characterised A. achatina snail lectin.

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Plavec, Tina Vida, Abida Zahirović, Petra Zadravec, Jerica Sabotič, and Aleš Berlec. "Lectin-Mediated Binding of Engineered Lactococcus lactis to Cancer Cells." Microorganisms 9, no. 2 (January 22, 2021): 223. http://dx.doi.org/10.3390/microorganisms9020223.

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Lectins have been increasingly utilized as carriers for targeted drug delivery based on their specific binding to glycans located on mammalian cells. This study employed two lectins, B subunit of bacterial Shiga holotoxin (Stx1B) and fungal Clitocybe nebularis lectin (CNL), for surface display on the lactic acid bacterium Lactococcus lactis. The specific adhesion of these engineered, lectin-displaying L. lactis to cancer cells was evaluated. The expression and surface display of both lectins on L. lactis were demonstrated by western blotting and flow cytometry, respectively. MTS assays revealed that recombinant Stx1B had no effect on Caco-2 cell viability at concentrations of ≤25 µg/mL, whereas CNL was non-toxic even at relatively high concentrations of ≤250 µg/mL. Stx1B bound to Caco-2, HT-29 and HeLa cells after 1 h of incubation. CNL bound to Caco-2 cells and recognized several glycoproteins in HT-29 and Caco-2 cell homogenates of which a 70 kDa protein predominated. Confocal microscopy revealed adhesion of Stx1B-displaying L. lactis to HeLa, Caco-2, and, to a lesser extent, HT-29 cells; CNL-displaying L. lactis showed a relatively similar level of adherence to HT-29 and Caco-2 cells. Thus, lectin-displaying L. lactis might serve as a carrier in targeted drug delivery when coupled to a therapeutic moiety.

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10

Barak, R., and I. Chet. "Lectin ofSclerotium rolfsii: its purification and possible function in fungal-fungal interaction." Journal of Applied Bacteriology 69, no. 1 (July 1990): 101–12. http://dx.doi.org/10.1111/j.1365-2672.1990.tb02917.x.

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11

Rodriguez-de la Noval, Claudia, Susana Ruiz Mendoza, Diego de Souza Gonçalves, Marina da Silva Ferreira, Leandro Honorato, José Mauro Peralta, Leonardo Nimrichter, and Allan J. Guimarães. "Protective Efficacy of Lectin-Fc(IgG) Fusion Proteins In Vitro and in a Pulmonary Aspergillosis In Vivo Model." Journal of Fungi 6, no. 4 (October 27, 2020): 250. http://dx.doi.org/10.3390/jof6040250.

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Aspergillosis cases by Aspergillus fumigatus have increased, along with fungal resistance to antifungals, urging the development of new therapies. Passive immunization targeting common fungal antigens, such as chitin and β-glucans, are promising and would eliminate the need of species-level diagnosis, thereby expediting the therapeutic intervention. However, these polysaccharides are poorly immunogenic. To overcome this drawback, we developed the lectin-Fc(IgG) fusion proteins, Dectin1-Fc(IgG2a), Dectin1-Fc(IgG2b) and wheat germ agglutinin (WGA)-Fc(IgG2a), based on their affinity to β-1,3-glucan and chitooligomers, respectively. The WGA-Fc(IgG2a) previously demonstrated antifungal activity against Histoplasma capsulatum, Cryptococcus neoformans and Candida albicans. In the present work, we evaluated the antifungal properties of these lectin-Fc(s) against A. fumigatus. Lectin-Fc(IgG)(s) bound in a dose-dependent manner to germinating conidia and this binding increased upon conidia germination. Both lectin-Fc(IgG)(s) displayed in vitro antifungal effects, such as inhibition of conidia germination, a reduced length of germ tubes and a diminished biofilm formation. Lectin-Fc(IgG)(s) also enhanced complement deposition on conidia and macrophage effector functions, such as increased phagocytosis and killing of fungi. Finally, administration of the Dectin-1-Fc(IgG2b) and WGA-Fc(IgG2a) protected mice infected with A. fumigatus, with a 20% survival and a doubled life-span of the infected mice, which was correlated to a fungal burden reduction in lungs and brains of treated animals. These results confirm the potential of lectin-Fc(IgGs)(s) as a broad-spectrum antifungal therapeutic.

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Shiokawa, Moe, Sho Yamasaki, and Shinobu Saijo. "C-type lectin receptors in anti-fungal immunity." Current Opinion in Microbiology 40 (December 2017): 123–30. http://dx.doi.org/10.1016/j.mib.2017.11.004.

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Wang, Hexiang, and Tzi Bun Ng. "First report of an arabinose-specific fungal lectin." Biochemical and Biophysical Research Communications 337, no. 2 (November 2005): 621–25. http://dx.doi.org/10.1016/j.bbrc.2005.09.096.

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Vautier, Simon, Donna M. MacCallum, and Gordon D. Brown. "C-type lectin receptors and cytokines in fungal immunity." Cytokine 58, no. 1 (April 2012): 89–99. http://dx.doi.org/10.1016/j.cyto.2011.08.031.

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Krahmer, R. L., J. J. Morrell, and A. Choi. "Double-Staining to Improve Visualisation of Wood Decay Hyphae in Wood Sections." IAWA Journal 7, no. 2 (1986): 165–67. http://dx.doi.org/10.1163/22941932-90000981.

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Combining fluorescent-labeled wheat germ agglutinin (a chitin-specific lectin) with conventional histological stains offers a simple, efficient method for studying fungal hyphae in deteriorating wood. Cell walls stain dark red with safranin 0, providing excellent contrast for the green-fluorescing hyphae. Staining sections with brilliant vital red markedly enhances the visibility of fungal bore holes.

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Xiao, Hui, Zihou Deng, and Tania H. Watts. "TRAF1 negatively regulates C-type lectin receptor-induced proinflammatory response to fungal infection." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 205.10. http://dx.doi.org/10.4049/jimmunol.196.supp.205.10.

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Abstract Fungal infections pose serious health threat worldwide, causing severe mucosal and systemic candidiasis in elderly people, AIDS patients and organ recipients. Through sensing fungal cell-wall components b-glucan and mannan, C-type lectin receptors (CLRs) dectin-1 and dectin-2/3 play pivotal role in the induction of anti-fungal innate and adaptive immune responses. However, the regulatory mechanisms of CLR signaling remain to be better understood. Indeed, our previous work demonstrated that the protein tyrosine phosphatase SHP-2 acts as a positive regulator of CLR-induced signaling, and thus plays a critical role in DCs to promote anti-fungal Th17 response. In this study, we found that fungus-elicited CLR signals are also stringently controlled by negative regulation. Upon C. albicans infection, TRAF1 was highly induced in skin, lung and kidney. Elevated TRAF1 expression was also detected in macrophages and DCs stimulated by dectin-1 and dectin-2/3 ligands, respectively. Mechanistically, TRAF1 acted as a feed-back negative regulator critically controlling the induction of proinflammatory genes, such as Cxcl1 and Tnf, in response to fungal infection. Consistently, TRAF1-deficient mice exhibited increased neutrophil-infiltration, highly efficient fungal eradication and ameliorated tissue damage, culminating on improved host defense and better survival. Taken together, this study identified a new feed-back regulatory mechanism by which CLRs regulate anti-fungal proinflammatory response.

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Kim, W. K., and H. J. Reisener. "Evidence for binding between host proteins and pathogen wall components in the wheat stem rust system from affinity protein blotting technique." Canadian Journal of Botany 66, no. 9 (September 1, 1988): 1702–6. http://dx.doi.org/10.1139/b88-233.

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Polypeptides extracted from the urediosporeling walls of Puccinia graminis tritici were separated by two-dimensional isoelectric focusing – polyacrylamide gel electrophoresis and stained with Coomassie brilliant blue or silver or electrophoretically transferred onto nitrocellulose membrane and probed for glycosylation using concanavalin A – horseradish peroxidase, soybean agglutinin-biotin – avidin peroxidase labeled, and Lotus lectin-biotin – avidin peroxidase labeled. More than 40 proteins were distributed in the gel by silver staining. Forty concanavalin A binding glycopeptides were identified in the blot, but none of them had affinity to soybean agglutinin or Lotus lectin. When fungal polypeptides were electrophoretically transferred through a nitrocellulose membrane that was pretreated with wheat leaf proteins, several fungal glycoproteins bound to the plant protein, suggesting that these pathogen wall components bound selectively to host proteins.

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Xu, Xiao-Chao, Zhong-Wei Zhang, Yang-Er Chen, Ming Yuan, Shu Yuan, and Jin-ku Bao. "Antiviral and antitumor activities of the lectin extracted from Aspidistra elatior." Zeitschrift für Naturforschung C 70, no. 1-2 (January 1, 2015): 7–13. http://dx.doi.org/10.1515/znc-2014-4108.

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Abstract Lectins, a group of highly diverse proteins of non-immune origin and are ubiquitously distributed in plants, animals and fungi, have multiple significant biological functions, such as anti-fungal, anti-viral and, most notably, anti-tumor activities. A lectin was purified from the rhizomes of Aspidistra elatior Blume, named A. elatior lectin (AEL). In vitro experiments showed that the minimum inhibitory concentrations of AEL against the vesicular stomatitis virus, Coxsackie virus B4, and respiratory syncytial virus were all the same at about 4 μg/mL. However, AEL was ineffective against the Sindbis virus and reovirus-1. AEL also showed significant in vitro antiproliferative activity towards Bre-04, Lu-04, HepG2, and Pro-01 tumor cell lines by increasing the proportion of their sub-G1 phase. However, AEL failed to restrict the proliferation of the HeLa cell line. Western blotting indicated that AEL induced the upregulation of cell cycle-related proteins p53 and p21. The molecular basis and species-specific effectiveness of the anti-proliferative and anti-viral potential of AEL are discussed.

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NAGATA, Yoshiho, Masako YAMASHITA, Hiroaki HONDA, Junko AKABANE, Koichi UEHARA, Akihiro SAITO, Futoshi SUMISA, Kozo NISHIBORI, and Yasuo OODAIRA. "Characterization, Occurrence, and Molecular Cloning of a Lectin fromGrifola frondosa: Jacalin-Related Lectin of Fungal Origin." Bioscience, Biotechnology, and Biochemistry 69, no. 12 (January 2005): 2374–80. http://dx.doi.org/10.1271/bbb.69.2374.

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Potts, S. J., J. F. Thompson, and D. C. Slaughter. "The effect of fungal species on the fluorescent lectin test." Journal of Microbiological Methods 46, no. 3 (September 2001): 187–91. http://dx.doi.org/10.1016/s0167-7012(01)00267-6.

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Fakhoury, A. M., and C. P. Woloshuk. "Inhibition of Growth of Aspergillus flavus and Fungal α-Amylases by a Lectin-Like Protein from Lablab purpureus." Molecular Plant-Microbe Interactions® 14, no. 8 (August 2001): 955–61. http://dx.doi.org/10.1094/mpmi.2001.14.8.955.

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Aspergillus flavus is a fungal pathogen of maize causing an important ear rot disease when plants are exposed to drought and heat stress. Associated with the disease is the production of aflatoxins, which are a series of structurally related mycotoxins known to be carcinogenic. Previous research has suggested that the α-amylase of A. flavus promotes aflatoxin production in the endosperm of infected maize kernels. We report here the isolation and characterization of a 36-kDa α-amylase inhibitor from Lablab purpureus (AILP). AILP inhibited the α-amylases from several fungi but had little effect on those from animal and plant sources. The protein inhibited conidial germination and hyphal growth of A. flavus. The amino acid sequence indicated that AILP is similar to lectin members of a lectin-arcelin-α-amylase inhibitor family described in common bean and shown to be a component of plant resistance to insect pests. AILP also agglutinated papain-treated red blood cells from human and rabbit. These data indicate that AILP represents a novel variant in the lectin-arcelin-α-amylase inhibitor family of proteins having lectin-like and α-amylase inhibitory activity.

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Rosen, Stefan, Miroslaw Kata, Yvonne Persson, Peter H. Lipniunas, Mats Wikstrom, Cees A. M. J. J. Hondel, Johannes M. Brink, Lars Rask, Lars-Olof Heden, and Anders Tunlid. "Molecular Characterization of a Saline-Soluble Lectin from a Parasitic Fungus. Extensive Sequence Similarities Between Fungal Lectins." European Journal of Biochemistry 238, no. 3 (June 15, 1996): 822–29. http://dx.doi.org/10.1111/j.1432-1033.1996.0822w.x.

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Machon, Oriane, Steffi F. Baldini, João P. Ribeiro, Agata Steenackers, Annabelle Varrot, Tony Lefebvre, and Anne Imberty. "Recombinant fungal lectin as a new tool to investigateO-GlcNAcylation processes." Glycobiology 27, no. 2 (October 18, 2016): 123–28. http://dx.doi.org/10.1093/glycob/cww105.

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Hamshou, M., E. J. M. Van Damme, and G. Smagghe. "Entomotoxic effects of fungal lectin from Rhizoctonia solani towards Spodoptera littoralis." Fungal Biology 114, no. 1 (January 2010): 34–40. http://dx.doi.org/10.1016/j.mycres.2009.10.002.

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Choteau, L., M. Parny, N. François, B. Bertin, M. Fumery, L. Dubuquoy, K. Takahashi, et al. "Role of mannose-binding lectin in intestinal homeostasis and fungal elimination." Mucosal Immunology 9, no. 3 (October 7, 2015): 767–76. http://dx.doi.org/10.1038/mi.2015.100.

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Borrebaeck, Carl A. K., Bo Mattiasson, and Birgit Nordbring-Hertz. "A fungal lectin and its apparent receptors on a nematode surface." FEMS Microbiology Letters 27, no. 1 (April 1985): 35–39. http://dx.doi.org/10.1111/j.1574-6968.1985.tb01633.x.

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27

Benhamou, N., and G. B. Ouellette. "Ultrastructural localization of glycoconjugates in the fungus Ascocalyx abietina, the Scleroderris canker agent of conifers, using lectin-gold complexes." Journal of Histochemistry & Cytochemistry 34, no. 7 (July 1986): 855–67. http://dx.doi.org/10.1177/34.7.3519750.

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Different glycoconjugates were revealed in the fungus Ascocalyx abietina (Lagerberg.) Schlaepfer-Bernhard, by using various lectin-gold complexes. N-acetylglucosamine, N-acetylgalactosamine, and D-mannose were specifically localized in cell walls of fungal cells. N-acetylneuraminic acid (sialic acid) and L-fucose were detected in structures corresponding to lipid bodies, whereas they were totally absent in the cell wall. This is the first report on the occurrence of sialic acid in fungi and of fucose in Ascomycetes. The great advantage of using lectin-gold complexes for ultrastructural localization of sugars in phytopathogenic fungi, as well as in studies concerning host-pathogen interactions, is discussed.

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Jeffs, Lloyd B., Ilungo J. Xavier, Russell E. Matai, and George G. Khachatourians. "Relationships between fungal spore morphologies and surface properties for entomopathogenic members of the general Beauveria, Metarhizium, Paecilomyces,Tolypocladium, and Verticillium." Canadian Journal of Microbiology 45, no. 11 (November 1, 1999): 936–48. http://dx.doi.org/10.1139/w99-097.

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The surface properties of aerial conidia (AC) from 24 strains of entomopathogenic fungi were studied and compared using the salt-mediated aggregation and sedimentation (SAS) assay, electron microscopy, FITC-labelled lectins, and spore dimensions. Spores with rugose surfaces were hydrophobic, whereas hydrophilic spores had smooth surfaces. Correlation analysis found no link between spore dimensions and either hydrophobicity or surface carbohydrates. However, there was a strong positive correlation between spore hydrophobicity and surface carbohydrates. The three spore types of Beauveria bassiana were all shown to possess discrete surface hydrophobicities, which were also strongly linked to surface carbohydrate profiles. Various chemical treatments had pronounced effects on spore surface properties, with sodium dodecyl sulfate (SDS) and formic acid (FA) reducing both lectin binding and surface hydrophobicity. When FA-protein extracts were separated and analysed using SDS-PAGE, only the hydrophobic spores had low molecular weight hydrophobin-like peptides that were unglycosylated and contained disulfide bonds. The strains with hydrophilic AC had much lower levels of FA-extractable protein per spore dry weight compared to their more hydrophobic counterparts. Moreover, extracts of the more hydrophobic spores tended to have greater protein:carbohydrate ratios.Key words: fungi, spores, hydrophobicity, lectins, morphology, microbial insecticides, protein.

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Stutz, Katrin, Andres Kaech, Markus Aebi, Markus Künzler, and Michael O. Hengartner. "Disruption of the C. elegans Intestinal Brush Border by the Fungal Lectin CCL2 Phenocopies Dietary Lectin Toxicity in Mammals." PLOS ONE 10, no. 6 (June 9, 2015): e0129381. http://dx.doi.org/10.1371/journal.pone.0129381.

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Wolf, Andrea J., Randi M. Simmons, Helen S. Goodridge, and David M. Underhill. "Polymorphisms associated with human Dectin-1 result in disrupted protein folding and loss of function (135.47)." Journal of Immunology 182, no. 1_Supplement (April 1, 2009): 135.47. http://dx.doi.org/10.4049/jimmunol.182.supp.135.47.

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Abstract Recognition of fungal pathogens is primarily mediated by a combination of TLRs and Dectin-1, the C-type lectin receptor for fungal β-glucans. While fungal infections in U.S. hospitals primarily arise among immune compromised patients, there has been an increased incidence in fungal infections that has been complicated by the emergence of drug resistance among fungal pathogens. Even though Dectin-1 functions as one of the primary phagocytic receptors in macrophages for fungal pathogens, the importance of Dectin-1 for controlling fungal pathogens is still unclear and may be pathogen dependent. Therefore we set out to analyze the functional consequences of single nucleotide polymophisms (SNPs) in human Dectin-1. When we mutated the full length form of the A isoform of human Dectin-1, two SNPs in the coding region resulted in a loss of phagocytic function. While both mutant forms of the protein were detectable they no longer supported phagocytosis of yeast zymosan particles in non-phagocytic cells. Analysis of alternate amino acid substitutions demonstrated an essential structural role for amino acid 223. Consequently, individuals possessing either of these mutations are potentially at a higher risk for certain fungal pathogens.

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Ooi, Linda S. M., Fang Liu, Vincent E. C. Ooi, T. B. Ng, and M. C. Fung. "Gene expression of immunomodulatory cytokines induced by Narcissus tazetta lectin in the mouse." Biochemistry and Cell Biology 80, no. 2 (April 1, 2002): 271–77. http://dx.doi.org/10.1139/o01-240.

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The immunomodulation of Narcissus tazetta lectin (NTL) on the induction of gene expression of cytokines in the mouse was studied using specific cytokine primers, total RNA isolated from mouse splenocytes and macrophages, and reverse transcription polymerase chain reaction (RT-PCR). For comparison, a fungal antimitogenic lectin from Agaricus bisporus (ABL) was used to test and compare the acute (kinetic) induction of cytokine gene expression. NTL was able to induce the expression of IL-1β, TNF-α, and immunoreactive nitric oxide synthase (NOS) in both splenocytes and macrophages in vivo after 10-day consecutive peritoneal injections of 5 mg NTL·kg1·day1 in the mouse. Nevertheless, the expression levels of IFN-γ and TGF-β were markedly increased in macrophages, and the levels of IL-2 and IL-4 were up-regulated only in splenocytes. From the kinetic pattern of cytokine induction and gene expression, ABL appeared to induce the up-regulation of IL-1β and TNF-α in splenocytes up to 24 h, whereas NTL showed a more sustained effect on the expression of these cytokines in macrophages. While NTL manifested TGF-β expression at the onset of 12 and 24 h in macrophages and splenocytes, respectively, ABL induced TGF-β in neither splenocytes nor macrophages. After injection of NTL, stem-cell factor was clearly down-regulated in macrophages at 24 and 48 h but up-regulated in splenocytes at the end of 24 h. The immunopotentiating effect of NTL is quite similar to that of LZ-8, a fungal immunomodulatory lectin isolated from the Chinese premier medicinal mushroom Ganoderma lucidium. However, the mechanism of immunomodulation of NTL still awaits to be elucidated.Key words: immunomodulation, cytokine genes, mannose-binding lectin, Narcissus.

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McCabe, Patricia M., and Neal K. Van Alfen. "Secretion of Cryparin, a Fungal Hydrophobin." Applied and Environmental Microbiology 65, no. 12 (December 1, 1999): 5431–35. http://dx.doi.org/10.1128/aem.65.12.5431-5435.1999.

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ABSTRACT Cryparin is a cell-surface-associated hydrophobin of the filamentous ascomycete Cryphonectria parasitica. This protein contains a signal peptide that directs it to the vesicle-mediated secretory pathway. We detected a glycosylated form of cryparin in a secretory vesicle fraction, but secreted forms of this protein are not glycosylated. This glycosylation occurred in the proprotein region, which is cleaved during maturation by a Kex2-like serine protease, leaving a mature form of cryparin that could be isolated from both the cell wall and culture medium. Pulse-chase labeling experiments showed that cryparin was secreted through the cell wall, without being bound, into the culture medium. The secreted protein then binds to the cell walls ofC. parasitica, where it remains. Binding of cryparin to the cell wall occurred in submerged culture, presumably because of the lectin-like properties unique to this hydrophobin. Thus, the binding of this hydrophobin to the cell wall is different from that of other hydrophobins which are reported to require a hydrophobic-hydrophilic interface for assembly.

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Tronchin, Guy, Karine Esnault, Myriam Sanchez, Gerald Larcher, Agnes Marot-Leblond, and Jean-Philippe Bouchara. "Purification and Partial Characterization of a 32-Kilodalton Sialic Acid-Specific Lectin from Aspergillus fumigatus." Infection and Immunity 70, no. 12 (December 2002): 6891–95. http://dx.doi.org/10.1128/iai.70.12.6891-6895.2002.

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ABSTRACT Adherence of the opportunistic fungus Aspergillus fumigatus to the extracellular matrix components is considered a crucial step in the establishment of the infection. Given the high carbohydrate content of these glycoproteins and the role of carbohydrate-protein interactions in numerous adherence processes, the presence of a lectin in A. fumigatus was investigated. Different fungal extracts obtained by sonication or grinding in liquid nitrogen from resting or swollen conidia, as well as from germ tubes and mycelium, were tested by hemagglutination assays using rabbit erythrocytes. A lectin activity was recovered in all the extracts tested. However, sonication of resting conidia resulted in the highest specific activity. Purification of the lectin was achieved by gel filtration followed by ion-exchange and hydrophobic-interaction chromatographies. Analysis of the purified lectin by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed an apparent molecular mass of 32 kDa, which is similar to that of the alkaline protease already identified from different strains of A. fumigatus. However, as evidenced by the use of an alkaline protease-deficient mutant, the two activities were supported by distinct proteins. In addition, hemagglutination inhibition experiments using different saccharides and glycoproteins demonstrated the specificity of the lectin for sialic acid residues. Together these results suggest that this lectin may contribute to the attachment of conidia to the extracellular matrix components through the recognition of the numerous terminal sialic acid residues of their carbohydrate chains.

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Audfray, Aymeric, Mona Beldjoudi, Adrien Breiman, Amandine Hurbin, Irene Boos, Carlo Unverzagt, Mourad Bouras, et al. "A Recombinant Fungal Lectin for Labeling Truncated Glycans on Human Cancer Cells." PLOS ONE 10, no. 6 (June 4, 2015): e0128190. http://dx.doi.org/10.1371/journal.pone.0128190.

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Bidula, Stefan, Hany Kenawy, Youssif M. Ali, Darren Sexton, Wilhelm J. Schwaeble, and Silke Schelenz. "Role of Ficolin-A and Lectin Complement Pathway in the Innate Defense against Pathogenic Aspergillus Species." Infection and Immunity 81, no. 5 (March 11, 2013): 1730–40. http://dx.doi.org/10.1128/iai.00032-13.

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ABSTRACTAspergillusspecies are saprophytic molds causing life-threatening invasive fungal infections in the immunocompromised host. Innate immune recognition, in particular, the mechanisms of opsonization and complement activation, has been reported to be an integral part of the defense against fungi. We have shown that the complement component ficolin-A significantly binds toAspergillusconidia and hyphae in a concentration-dependent manner and was inhibited byN-acetylglucosamine andN-acetylgalactosamine. Calcium-independent binding toAspergillus fumigatusandA. terreuswas observed, but binding toA. flavusandA. nigerwas calcium dependent. Ficolin-A binding to conidia was increased under low-pH conditions, and opsonization led to enhanced binding of conidia to A549 airway epithelial cells. In investigations of the lectin pathway of complement activation, ficolin-A-opsonized conidia did not lead to lectin pathway-specific C4 deposition. In contrast, the collectin mannose binding lectin C (MBL-C) but not MBL-A led to efficient lectin pathway activation onA. fumigatusin the absence of ficolin-A. In addition, ficolin-A opsonization led to a modulation of the proinflammatory cytokine interleukin-8. We conclude that ficolin-A may play an important role in the innate defense againstAspergillusby opsonizing conidia, immobilizing this fungus through enhanced adherence to epithelial cells and modulation of inflammation. However, it appears that other immune pattern recognition molecules, i.e., those of the collectin MBL-C, are involved in theAspergillus-lectin complement pathway activation rather than ficolin-A.

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Mateos, François Villalba, Martina Rickauer, and Marie-Thérèse Esquerré-Tugayé. "Cloning and Characterization of a cDNA Encoding an Elicitor of Phytophthora parasitica var. nicotianae That Shows Cellulose-Binding and Lectin-Like Activities." Molecular Plant-Microbe Interactions® 10, no. 9 (December 1997): 1045–53. http://dx.doi.org/10.1094/mpmi.1997.10.9.1045.

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Phytophthora parasitica var. nicotianae produces a 34-kDa glycoprotein elicitor (CBEL) that is localized in the cell wall. A cDNA encoding the protein moiety of this elicitor was cloned and characterized. The deduced amino acid sequence consisted of two direct repeats of a cysteine-rich domain, joined by a Thr/Pro-rich region. Although having no general homology with published sequences, the positions of the cysteine residues in the two repeats show a conserved pattern, similar to that of the cellulose-binding domain of fungal glycanases. CBEL did not possess hydrolytic activity on a variety of glycans, but bound to fibrous cellulose and plant cell walls. In addition, it exerted a lectin-like hemagglutinating activity. Infiltration of tobacco leaves (cultivar 46–8) with this molecule elicited necrosis and defense gene expression at 150 nM. Elicitor pre-treatment of this tobacco cultivar resulted in protection against subsequent inoculation with an otherwise virulent race of P. parasitica var. nicotianae. All these biological activities were exerted within a low concentration range. This is the first report that a fungal elicitor exhibits cellulose-binding and lectin-like activities. The possible implications of such a multifunctional elicitor in plant-microbe interactions are discussed.

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Maldonado, Samuel D., Jihong Dai, Orchi Dutta, Harry J. Hurley, Sukhwinder Singh, Lisa Gittens-Williams, Evelyne Kalyoussef, Karen L. Edelblum, Amariliz Rivera, and Patricia Fitzgerald-Bocarsly. "Human Plasmacytoid Dendritic Cells Express C-Type Lectin Receptors and Attach and Respond to Aspergillus fumigatus." Journal of Immunology 209, no. 4 (August 15, 2022): 675–83. http://dx.doi.org/10.4049/jimmunol.2000632.

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Abstract Plasmacytoid dendritic cells (pDCs) have been implicated as having a role in antifungal immunity, but mechanisms of their interaction with fungi and the resulting cellular responses are not well understood. In this study, we identify the direct and indirect biological response of human pDCs to the fungal pathogen Aspergillus fumigatus and characterize the expression and regulation of antifungal receptors on the pDC surface. Results indicate pDCs do not phagocytose Aspergillus conidia, but instead bind hyphal surfaces and undergo activation and maturation via the upregulation of costimulatory and maturation markers. Measuring the expression of C-type lectin receptors dectin-1, dectin-2, dectin-3, and mannose receptor on human pDCs revealed intermediate expression of each receptor compared with monocytes. The specific dectin-1 agonist curdlan induced pDC activation and maturation in a cell-intrinsic and cell-extrinsic manner. The indirect activation of pDCs by curdlan was much stronger than direct stimulation and was mediated through cytokine production by other PBMCs. Overall, our data indicate pDCs express various C-type lectin receptors, recognize and respond to Aspergillus hyphal Ag, and serve as immune enhancers or modulators in the overarching fungal immune response.

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Massicotte, H. B., C. A. Ackerley, and R. L. Peterson. "Localization of three sugar residues in the interface of ectomycorrhizae synthesized between Alnus crispa and Alpova diplophloeus as demonstrated by lectin binding." Canadian Journal of Botany 65, no. 6 (June 1, 1987): 1127–32. http://dx.doi.org/10.1139/b87-157.

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The interface established between Alnus crispa and the basidiomycete Alpova diplophloeus involves structural modifications of host cell walls and hyphal walls in the Hartig net region of the ectomycorrhizae synthesized in pouches. Indirect labelling of cell wall carbohydrates by using colloidal gold conjugated with the lectins Ulex europaeus agglutinin, wheat-germ agglutinin, and concanavalin A was applied to these mycorrhizae and to nonmycorrhizal roots. Significantly more binding of the lectins was observed in the mycorrhizal roots than in control roots. In the Hartig net region of mycorrhizal roots, the lectins bound intensely to the host cell wall, particularly the wall ingrowths, and to adjacent fungal walls, whereas in nonmycorrhizal roots, a sparse labelling was recorded in the cell wall. Possible explanations for this pattern of lectin binding include the following: the sugar residues L-fucose, mannose, and N-acetylglucosamine may be utilized in the synthesis of the elaborate epidermal wall ingrowths and N-acetylglucosamine may be utilized in the synthesis of the labyrinthine wall branchings of the fungus; the sugar residues are bound to a proteinaceous fraction in the host and hyphal walls; the sugar residues bound by the lectins may be components of defense reaction elicitors released from the host wall and hyphal wall by wall-degrading enzymes; the sugar residues may simply be the result of enzymatic degradation of walls but not involving elicitors of defense reactions.

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Robinson, Matthew J., Fabiola Osorio, Marcela Rosas, Rui P. Freitas, Edina Schweighoffer, Olaf Groß, J. Sjef Verbeek, et al. "Dectin-2 is a Syk-coupled pattern recognition receptor crucial for Th17 responses to fungal infection." Journal of Experimental Medicine 206, no. 9 (August 24, 2009): 2037–51. http://dx.doi.org/10.1084/jem.20082818.

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Innate immune cells detect pathogens via pattern recognition receptors (PRRs), which signal for initiation of immune responses to infection. Studies with Dectin-1, a PRR for fungi, have defined a novel innate signaling pathway involving Syk kinase and the adaptor CARD9, which is critical for inducing Th17 responses to fungal infection. We show that another C-type lectin, Dectin-2, also signals via Syk and CARD9, and contributes to dendritic cell (DC) activation by fungal particles. Unlike Dectin-1, Dectin-2 couples to Syk indirectly, through association with the FcRγ chain. In a model of Candida albicans infection, blockade of Dectin-2 did not affect innate immune resistance but abrogated Candida-specific T cell production of IL-17 and, in combination with the absence of Dectin-1, decreased Th1 responses to the organism. Thus, Dectin-2 constitutes a major fungal PRR that can couple to the Syk–CARD9 innate signaling pathway to activate DCs and regulate adaptive immune responses to fungal infection.

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Amiel, Eyal, Phyu M. Thwe, Daniel Fritz, and Julia Snyder. "Syk-dependent Glycolytic Reprogramming in Dendritic Cells Regulates IL-1-beta Production to Fungal-assoicated Ligands in a TLR-independent Manner." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 64.2. http://dx.doi.org/10.4049/jimmunol.202.supp.64.2.

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Abstract Dendritic cells (DCs) activated via TLR ligation experience metabolic reprogramming, in which the cells are heavily dependent on glucose and glycolysis for the synthesis of molecular building blocks essential for maturation, cytokine production, and the ability to stimulate T cells. Although the TLR-driven metabolic reprogramming events are well documented, fungal-mediated metabolic regulation via C-type Lectin Receptors such as Dectin-1 is not clearly understood. Here, we show that activation of DCs with fungal-associated ligands induces acute glycolytic reprogramming that supports the production of IL-1b via inflammasome activation. This acute glycolytic induction to fungal-associated ligands is depending on Syk signaling in a TLR-independent manner, suggesting now that different classes of innate immune receptors functionally induce conserved metabolic responses to support immune cell activation. These studies provide new insight into the complexities of metabolic regulation of DCs immune effector function regarding cellular activation associated with protection against fungal microbes.

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Inbar, J., and I. Chet. "Biomimics of fungal cell-cell recognition by use of lectin-coated nylon fibers." Journal of Bacteriology 174, no. 3 (1992): 1055–59. http://dx.doi.org/10.1128/jb.174.3.1055-1059.1992.

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Oda, Yasuo, Tsutomu Senaha, Yuuki Matsuno, Kazuki Nakajima, Ryousuke Naka, Mitsuhiro Kinoshita, Eiko Honda, Itaru Furuta, and Kazuaki Kakehi. "A New Fungal Lectin Recognizing α(1–6)-linked Fucose in theN-Glycan." Journal of Biological Chemistry 278, no. 34 (June 4, 2003): 32439–47. http://dx.doi.org/10.1074/jbc.m305181200.

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Del Rio, Marianela, Laura de la Canal, Marcela Pinedo, and Mariana Regente. "Internalization of a sunflower mannose-binding lectin into phytopathogenic fungal cells induces cytotoxicity." Journal of Plant Physiology 221 (February 2018): 22–31. http://dx.doi.org/10.1016/j.jplph.2017.12.001.

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van Deenen, N., D. Prufer, and C. Gronover. "A latex lectin from Euphorbia trigona is a potent inhibitor of fungal growth." Biologia plantarum 55, no. 2 (June 1, 2011): 335–39. http://dx.doi.org/10.1007/s10535-011-0049-z.

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Nagre, Nagaraja N., Vishwanath B. Chachadi, Sachin M. Eligar, C. Shubhada, Radha Pujari, Padma Shastry, Bale M. Swamy, and Shashikala R. Inamdar. "Purification and Characterization of a Mitogenic Lectin fromCephalosporium, a Pathogenic Fungus Causing Mycotic Keratitis." Biochemistry Research International 2010 (2010): 1–6. http://dx.doi.org/10.1155/2010/854656.

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Ophthalmic mycoses caused by infectious fungi are being recognized as a serious concern since they lead to total blindness.Cephalosporiumis one amongst several opportunistic fungal species implicated in ophthalmic infections leading to mycotic keratitis. A mitogenic lectin has been purified from the mycelia of fungusCephalosporium, isolated from the corneal smears of a keratitis patient.Cephalosporiumlectin (CSL) is a tetramer with subunit mass of 14 kDa, agglutinates human A, B, and O erythrocytes, and exhibits high affinity for mucin compared to fetuin and asialofetuin but does not bind to simple sugars indicating its complex sugar specificity. CSL showed strong binding to normal human peripheral blood mononuclear cells (PBMCs) to elicit mitogenic activity. The sugar specificity of the lectin and its interaction with PBMCs to exhibit mitogenic effect indicate its possible role in adhesion and infection process ofCephalosporium.

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Bertini, Laura, Silvia Proietti, Maria Pia Aleandri, Francesca Mondello, Silvia Sandini, Carlo Caporale, and Carla Caruso. "Modular structure of HEL protein from Arabidopsis reveals new potential functions for PR-4 proteins." Biological Chemistry 393, no. 12 (December 1, 2012): 1533–46. http://dx.doi.org/10.1515/hsz-2012-0225.

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Abstract Plants possess an innate immune system enabling them to defend themselves against pathogen attack. The accumulation of newly synthesized pathogenesis-related proteins (PRs) is one of the most studied inducible plant defence response. In this paper, we report on the characterization of a class I PR4 vacuolar protein from Arabidopsis, named AtHEL. The protein has a modular structure consisting of an N-terminal hevein-like domain (CB-HEL) and a C-terminal domain (CD-HEL) that are posttranslationally processed. Both domains show a strong antifungal activity, but they do not have chitinolitic properties. CD-HEL was found to be endowed with RNase, but not DNase activity. Molecular modeling carried out on both domains revealed that CB-HEL possesses a chitin binding site strictly conserved between hevein-type peptides and that the cavity involved in substrate interaction of CD-HEL do not show any residue substitution with respect to the orthologous wheatwin1 from wheat. Using a fishing for partners approach, CB-HEL was found to interact with a fungal fruiting body lectin. According to literature, we can hypothesize that CB-HEL could cross the pathogen hyphal membrane and that its interaction with a fungal lectin could knock out one of the weapons that the fungus uses.

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Hardham, AR. "Lectin and Antibody Labelling of Surface Components of Spores of Phytophthora cinnamomi." Functional Plant Biology 16, no. 1 (1989): 19. http://dx.doi.org/10.1071/pp9890019.

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Molecules on the surface of zoospores and cysts of soilborne fungi such as Phytophthora cinnamomi are important mediators in the early stages of infection of host plants. Surface components of P. cinnamomi cells have been analysed ultrastructurally and at the molecular level using lectins and monoclonal antibodies, with a view to localising and characterising molecules involved in the infection process. Staining with ruthenium red and the lectin, concanavalin A, indicates the presence of a glycocalyx over the surface of the zoospores. Localised antibody binding also reveals that the zoospore surface is subdivided into at least three distinct molecular domains. During encystment, the spectrum of molecules on the cell surface changes dramatically with the secretion of material which is rich in N-acetyl-D-galactosamine and which bonds the cells to any adjacent structure. lmmunolabelling shows that this material is stored in small peripheral vesicles and is secreted 1-3 min after encystment is induced. Encystment can be triggered by the binding of a monoclonal antibody to the flagella, suggesting that specific receptors may be localised there. Surface components on the fungal cells display a variety of taxonomic specificities including those for species and genus. Monoclonal antibodies which bind to these components promise to be valuable tools for diagnostic use.

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Wang, Huafeng, Mengyi Li, Tassanee Lerksuthirat, Bruce Klein, and Marcel Wüthrich. "The C-Type Lectin Receptor MCL Mediates Vaccine-Induced Immunity against Infection with Blastomyces dermatitidis." Infection and Immunity 84, no. 3 (December 14, 2015): 635–42. http://dx.doi.org/10.1128/iai.01263-15.

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C-type lectin receptors (CLRs) are essential in shaping the immune response to fungal pathogens. Vaccine-induced resistance requires Dectin-2 to promote differentiation of antifungal Th1 and Th17 cells. Since Dectin-2 and MCL heterodimerize and both CLRs use FcRγ as the signaling adaptor, we investigated the role of MCL in vaccine immunity to the fungal pathogenBlastomyces dermatitidis. MCL−/−mice showed impaired vaccine resistance againstB. dermatitidisinfection compared to that of wild-type animals. The lack of resistance correlated with the reduced recruitment of Th17 cells to the lung upon recall following experimental challenge and impaired interleukin-17 (IL-17) production by vaccine antigen-stimulated splenocytesin vitro. Soluble MCL fusion protein recognized and bound a water-soluble ligand from the cell wall of vaccine yeast, but the addition of soluble Dectin-2 fusion protein did not augment ligand recognition by MCL. Taken together, our data indicate that MCL regulates the development of vaccine-induced Th17 cells and protective immunity against lethal experimental infection withB. dermatitidis.

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Genster, Ninette, Jack Cowland, Elisabeth Cramer, Anne Rosbjerg, Katrine Pilely, and Peter Garred. "Ficolins promote fungal clearance during the early stage of pulmonary infection with Aspergillus fumigatus." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 124.34. http://dx.doi.org/10.4049/jimmunol.196.supp.124.34.

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Abstract Aspergillus fumigatus is a fungal pathogen causing severe and usually fatal invasive infections in immunocompromised patients. The Ficolins are pattern recognition molecules of the lectin pathway of complement and in vitro studies suggest a role for ficolins in the defence against A.fumigatus. However, little is known about their significance in fungal infections in vivo. Thus, our aim of the current project was to establish a murine model of pulmonary A. fumigatus infection to study the relevance of ficolins in host protection against A.fumigatus. Wildtype and ficolin knockout mice were infected intranasally with a sublethal dose of A.fumigatus conidia and the lungs were removed at various time points post-infection to assess the fungal load and expression of pro-inflammatory cytokines. In addition, the concentration of pro-inflammatory cytokines was measured in the bronchoalveolar lavage. After 24 hours of A.fumigatus infection, the pulmonary fungal load was significantly higher in ficolin knockout mice compared to wildtype mice. In contrast, no significant difference in fungal load between ficolin knockout mice and wildtype mice was observed after 12, 48 or 72 hours of infection. Interestingly, the increased fungal load in knockout mice 24 post-infection was accompanied by a significantly impaired induction of pro-inflammatory cytokines compared to wildtype mice. These results show that ficolins promote fungal clearance and modulate the pro-inflammatory cytokine response, demonstrating the importance of ficolins during the initial phase of A. fumigatus infections in vivo.

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Nørregaard, Kirstine Sandal, Oliver Krigslund, Niels Behrendt, Lars H. Engelholm, and Henrik Jessen Jürgensen. "The collagen receptor uPARAP/Endo180 regulates collectins through unique structural elements in its FNII domain." Journal of Biological Chemistry 295, no. 27 (May 18, 2020): 9157–70. http://dx.doi.org/10.1074/jbc.ra120.013710.

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C-type lectins that contain collagen-like domains are known as collectins. These proteins are present both in the circulation and in extravascular compartments and are central players of the innate immune system, contributing to first-line defenses against viral, bacterial, and fungal pathogens. The collectins mannose-binding lectin (MBL) and surfactant protein D (SP-D) are regulated by tissue fibroblasts at extravascular sites via an endocytic mechanism governed by urokinase plasminogen activator receptor–associated protein (uPARAP or Endo180), which is also a collagen receptor. Here, we investigated the molecular mechanisms that drive the uPARAP-mediated cellular uptake of MBL and SP-D. We found that the uptake depends on residues within a protruding loop in the fibronectin type-II (FNII) domain of uPARAP that are also critical for collagen uptake. Importantly, however, we also identified FNII domain residues having an exclusive role in collectin uptake. We noted that these residues are absent in the related collagen receptor, the mannose receptor (MR or CD206), which consistently does not interact with collectins. We also show that the second C-type lectin-like domain (CTLD2) is critical for the uptake of SP-D, but not MBL, indicating an additional level of complexity in the interactions between collectins and uPARAP. Finally, we demonstrate that the same molecular mechanisms enable uPARAP to engage MBL immobilized on the surface of pathogens, thereby expanding the potential biological implications of this interaction. Our study reveals molecular details of the receptor-mediated cellular regulation of collectins and offers critical clues for future investigations into collectin biology and pathology.

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Journal articles on the topic 'Fungal Lectin'

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