Fungal melanin stimulates surfactant protein D–mediated opsonization of and host immune response to Aspergillus fumigatus spores

Wong, Sarah Sze Wah; Rani, Manjusha; Dodagatta-Marri, Eswari; Ibrahim-Granet, Oumaïma; Kishore, Uday; Bayry, Jagadeesh; Latgé, Jean‐Paul; Sahu, Arvind; Madan, Taruna; Aimanianda, Vishukumar

doi:10.1074/jbc.m117.815852

Cited by 39 publications

(36 citation statements)

References 62 publications

(75 reference statements)

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“…A phagocytotic assay was performed for A . fumigatus conidia using human monocyte derived macrophages (HMDM) obtained as described previously [26,27]. A .…”

Section: Methodsmentioning

confidence: 99%

Novel mouse monoclonal antibodies specifically recognizing β-(1→3)-D-glucan antigen

et al. 2019

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β-(1→3)-D-Glucan is an essential component of the fungal cell wall. Mouse monoclonal antibodies (mAbs) against synthetic nona-β-(1→3)-D-glucoside conjugated with bovine serum albumin (BSA) were generated using hybridoma technology. The affinity constants of two selected mAbs, 3G11 and 5H5, measured by a surface plasmon resonance biosensor assay using biotinylated nona-β-(1→3)-D-glucan as the ligand, were approximately 11 nM and 1.9 nM, respectively. The glycoarray, which included a series of synthetic oligosaccharide derivatives representing β-glucans with different lengths of oligo-β-(1→3)-D-glucoside chains, demonstrated that linear tri-, penta- and nonaglucoside, as well as a β-(1→6)-branched octasaccharide, were recognized by mAb 5H5. By contrast, only linear oligo-β-(1→3)-D-glucoside chains that were not shorter than pentaglucosides (but not the branched octaglucoside) were ligands for mAb 3G11. Immunolabelling indicated that 3G11 and 5H5 interact with both yeasts and filamentous fungi, including species from Aspergillus , Candida , Penicillium genera and Saccharomyces cerevisiae , but not bacteria. Both mAbs could inhibit the germination of Aspergillus fumigatus conidia during the initial hours and demonstrated synergy with the antifungal fluconazole in killing C . albicans in vitro . In addition, mAbs 3G11 and 5H5 demonstrated protective activity in in vivo experiments, suggesting that these β-glucan-specific mAbs could be useful in combinatorial antifungal therapy.

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“…A phagocytotic assay was performed for A . fumigatus conidia using human monocyte derived macrophages (HMDM) obtained as described previously [26,27]. A .…”

Section: Methodsmentioning

confidence: 99%

Novel mouse monoclonal antibodies specifically recognizing β-(1→3)-D-glucan antigen

et al. 2019

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“…The mycelial suspension was centrifuged at 200 rpm for 2 min, 50 µL of the liquid media were removed by aspiration with a micropipette and replaced with 50 µL of fresh PB to remove the excess of unreacted fluorescent probe. Intracellular ROS were quantified at 0, 1, and 2 h of reaction time by measuring the fluorescence intensity using a Synergy 2 Multi-Mode Microplate Reader (Biotek) with an excitation filter at 485 nm and an emission filter at 530 nm, at 18 ± 1 • C for P. infestans and at 25 ± 1 • C for P. cinnamomi (Wong et al, 2018). Three replicates (wells) were assessed for each treatment and the experiment was carried out twice.…”

Section: Quantification Of Intracellular Reactive Oxygen Speciesmentioning

confidence: 99%

The Rare Sugar Tagatose Differentially Inhibits the Growth of Phytophthora infestans and Phytophthora cinnamomi by Interfering With Mitochondrial Processes

et al. 2020

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“…The fungal ligands of SP-A are 2 N-linked glycosylated glycoproteins (gp45 and gp55) isolated from culture filtrate and are also used for ELISA diagnosis of allergic aspergillosis (Madan et al 1997b). Fungal melanin was recently determined to be the primary ligand for SP-D on the A. fumigatus conidia cell surface, and is able to facilitate fungal phagocytosis and modulate the anti-fungal immune response (Wong et al 2018).…”

Section: Sp-a and Sp-dmentioning

confidence: 99%

Collectins: Innate Immune Pattern Recognition Molecules

Murugaiah

Tsolaki

Kishore

2020

Advances in Experimental Medicine and Biology

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Collectins are collagen-containing C-type (calcium-dependent) lectins which are important pathogen pattern recognising innate immune molecules. Their primary structure is characterised by an N-terminal, triple-helical collagenous region made up of Gly-X-Y repeats, an a-helical coiled-coil trimerising neck region, and a Cterminal C-type lectin or carbohydrate recognition domain (CRD). Further oligomerisation of this primary structure can give rise to more complex and multimeric structures that can be seen under electron microscope. Collectins can be found in serum as well as in a range of tissues at the mucosal surfaces. Mannanbinding lectin can activate the complement system while other members of the collectin family are extremely versatile in recognising a diverse range of pathogens via their CRDs and bring about effector functions designed at the clearance of invading pathogens. These mechanisms include opsonisation, enhancement of phagocytosis, triggering superoxidative burst and nitric oxide production. Collectins can also potentiate the adaptive immune response via antigen presenting cells such as macrophages and dendritic cells through modulation of cytokines and chemokines, thus they can act as a link between innate and adaptive immunity. This chapter describes the structure-function relationships of collectins, their diverse functions, and their interaction with viruses, bacteria, fungi and parasites.

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Fungal melanin stimulates surfactant protein D–mediated opsonization of and host immune response to Aspergillus fumigatus spores

Cited by 39 publications

References 62 publications

Novel mouse monoclonal antibodies specifically recognizing β-(1→3)-D-glucan antigen

Novel mouse monoclonal antibodies specifically recognizing β-(1→3)-D-glucan antigen

The Rare Sugar Tagatose Differentially Inhibits the Growth of Phytophthora infestans and Phytophthora cinnamomi by Interfering With Mitochondrial Processes

Collectins: Innate Immune Pattern Recognition Molecules

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