Galectin-related protein: An integral member of the network of chicken galectins

Kaltner, Herbert; Caballero, Gabriel García; Sinowatz, Fred; Schmidt, Sebastian; Manning, Joachim C.; André, Sabine; Gabius, Hans‐Joachim

doi:10.1016/j.bbagen.2016.06.002

Cited by 22 publications

(8 citation statements)

References 69 publications

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“…Previously bursal FAE and IFE cells, the latter largely consisting of mucin-secreting cells (5, 31, 35), have been distinguished from each other on the basis of lectin binding on tissue sections (11, 36, 37). CSF1R -transgene expression distinguished the bursal FAE and IFE but some FAE cells appeared to lack CSF1R -transgene expression (Supplementary Figure 1D).…”

Section: Resultsmentioning

confidence: 99%

Antigen Sampling CSF1R-Expressing Epithelial Cells Are the Functional Equivalents of Mammalian M Cells in the Avian Follicle-Associated Epithelium

et al. 2019

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The follicle-associated epithelium (FAE) is a specialized structure that samples luminal antigens and transports them into mucosa-associated lymphoid tissues (MALT). In mammals, transcytosis of antigens across the gut epithelium is performed by a subset of FAE cells known as M cells. Here we show that colony-stimulating factor 1 receptor (CSF1R) is expressed by a subset of cells in the avian bursa of Fabricius FAE. Expression was initially detected using a CSF1R-reporter transgene that also label subsets of bursal macrophages. Immunohistochemical detection using a specific monoclonal antibody confirmed abundant expression of CSF1R on the basolateral membrane of FAE cells. CSF1R-transgene expressing bursal FAE cells were enriched for expression of markers previously reported as putative M cell markers, including annexin A10 and CD44. They were further distinguished from a population of CSF1R-transgene negative epithelial cells within FAE by high apical F-actin expression and differential staining with the lectins jacalin, PHA-L and SNA. Bursal FAE cells that express the CSF1R-reporter transgene were responsible for the bulk of FAE transcytosis of labeled microparticles in the size range 0.02–0.1 μm. Unlike mammalian M cells, they did not readily take up larger bacterial sized microparticles (0.5 μm). Their role in uptake of bacteria was tested using Salmonella, which can enter via M cells in mammals. Labeled Salmonella enterica serovar Typhimurium entered bursal tissue via the FAE. Entry was partially dependent upon Type III secretion system-1. However, the majority of invading bacteria were localized to CSF1R-negative FAE cells and in resident phagocytes that express the phosphatidylserine receptor TIM4. CSF1R-expressing FAE cells in infected follicles showed evidence of cell death and shedding into the bursal lumen. In mammals, CSF1R expression in the gut is restricted to macrophages which only indirectly control M cell differentiation. The novel expression of CSF1R in birds suggests that these functional equivalents to mammalian M cells may have different ontological origins and their development and function are likely to be regulated by different growth factors.

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Section: Resultsmentioning

confidence: 99%

Antigen Sampling CSF1R-Expressing Epithelial Cells Are the Functional Equivalents of Mammalian M Cells in the Avian Follicle-Associated Epithelium

et al. 2019

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“…Arrays produced by printing glycans (50 μM; total of 416 oligosaccharides) were from Semiotik LLC (Moscow, Russia). Gal-8 (NN/NC), labeled by conjugation of biotin using the N -hydroxysuccinimide ester derivative (Sigma, Munich, Germany) under activity-preserving conditions as described [ 83 , 84 , 85 ], was tested at the concentration of 50 μg/mL in phosphate-buffered saline (PBS) containing 0.1% Tween-20 and 1% bovine serum albumin. This solution was incubated for 1 h at 37 °C in a humidified chamber.…”

Section: Methodsmentioning

confidence: 99%

Studying the Structural Significance of Galectin Design by Playing a Modular Puzzle: Homodimer Generation from Human Tandem-Repeat-Type (Heterodimeric) Galectin-8 by Domain Shuffling

et al. 2017

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Tissue lectins are emerging (patho)physiological effectors with broad significance. The capacity of adhesion/growth-regulatory galectins to form functional complexes with distinct cellular glycoconjugates is based on molecular selection of matching partners. Engineering of variants by changing the topological display of carbohydrate recognition domains (CRDs) provides tools to understand the inherent specificity of the functional pairing. We here illustrate its practical implementation in the case of human tandem-repeat-type galectin-8 (Gal-8). It is termed Gal-8 (NC) due to presence of two different CRDs at the N- and C-terminal positions. Gal-8N exhibits exceptionally high affinity for 3′-sialylated/sulfated β-galactosides. This protein is turned into a new homodimer, i.e., Gal-8 (NN), by engineering. The product maintained activity for lactose-inhibitable binding of glycans and glycoproteins. Preferential association with 3′-sialylated/sulfated (and 6-sulfated) β-galactosides was seen by glycan-array analysis when compared to the wild-type protein, which also strongly bound to ABH-type epitopes. Agglutination of erythrocytes documented functional bivalency. This result substantiates the potential for comparative functional studies between the variant and natural Gal-8 (NC)/Gal-8N.

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“…The protocols for processing tissue sections by lectin histochemistry and monitoring staining proles by light and uorescence microscopy had been optimized previously. 69,85,92,93 Routinely, systematic titrations with each labelled lectin were carried out to determine the concentrations, which generate strong signals combined with minimal background staining. The tested concentration ranges for light/uorescence microscopy were 0.25-1.5/0.5-1 mg mL À1 for DBA, 0.5-4/0.25-4 mg mL À1 for SBA, 0.5-2/1-2 mg mL À1 for HPA, 1-8 mg mL À1 for MGL (CRD) and 1-8/8-32 mg mL À1 for MGL (CRD + stalk), respectively.…”

Section: Tissue Samplesmentioning

confidence: 99%

Revealing biomedically relevant cell and lectin type-dependent structure–activity profiles for glycoclusters by using tissue sections as an assay platform

et al. 2018

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Galectin-related protein: An integral member of the network of chicken galectins

Cited by 22 publications

References 69 publications

Antigen Sampling CSF1R-Expressing Epithelial Cells Are the Functional Equivalents of Mammalian M Cells in the Avian Follicle-Associated Epithelium

Antigen Sampling CSF1R-Expressing Epithelial Cells Are the Functional Equivalents of Mammalian M Cells in the Avian Follicle-Associated Epithelium

Studying the Structural Significance of Galectin Design by Playing a Modular Puzzle: Homodimer Generation from Human Tandem-Repeat-Type (Heterodimeric) Galectin-8 by Domain Shuffling

Revealing biomedically relevant cell and lectin type-dependent structure–activity profiles for glycoclusters by using tissue sections as an assay platform

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