Parasites, Hosts and Diseases

The Korea Society for Parasitology and Tropical Medicine (대한기생충학·열대의학회)
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Agglutination Activity of Fasciola gigantica DM9-1, a Mannose-Binding Lectin

  • Phadungsil, Wansika (Graduate Program in Biomedical Sciences, Faculty of Allied Health Sciences, Thammasat University) ;
  • Grams, Rudi (Graduate Program in Biomedical Sciences, Faculty of Allied Health Sciences, Thammasat University)
  • Received : 2020.12.29
  • Accepted : 2021.03.22
  • Published : 2021.04.30
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Abstract

The DM9 domain is a protein unit of 60-75 amino acids that has been first detected in the fruit fly Drosophila as a repeated motif of unknown function. Recent research on proteins carrying DM9 domains in the mosquito Anopheles gambiae and the oyster Crassostrea gigas indicated an association with the uptake of microbial organisms. Likewise, in the trematode Fasciola gigantica DM9-1 showed intracellular relocalization following microbial, heat and drug stress. In the present research, we show that FgDM9-1 is a lectin with a novel mannose-binding site that has been recently described for the protein CGL1 of Crassostrea gigas. This property allowed FgDM9-1 to agglutinate gram-positive and -negative bacteria with appropriate cell surface glycosylation patterns. Furthermore, FgDM9-1 caused hemagglutination across all ABO blood group phenotypes. It is speculated that the parenchymal located FgDM9-1 has a role in cellular processes that involve the transport of mannose-carrying molecules in the parenchymal cells of the parasite.

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Acknowledgement

This study was financially supported by a grant through Faculty of Allied Health Sciences, Thammasat University, contract no. 3/2561 and Thammasat University research fund, contract no. TUGR 2/46/2562.

References

  1. Phadungsil W, Smooker PM, Vichasri-Grams S, Grams R. Characterization of a Fasciola gigantica protein carrying two DM9 domains reveals cellular relocalization property. Mol Biochem Parasitol 2016; 205: 6-15. https://doi.org/10.1016/j.molbiopara.2016.02.008
  2. Chertemps T, Mitri C, Perrot S, Sautereau J, Jacques JC, Thiery I, Bourgouin C, Rosinski-Chupin I. Anopheles gambiae PRS1 modulates Plasmodium development at both midgut and salivary gland steps. PLoS One 2010; 5: e11538. https://doi.org/10.1371/journal.pone.0011538
  3. Labbunruang N, Phadungsil W, Tesana S, Smooker PM, Grams R. Similarity of a 16.5kDa tegumental protein of the human liver fluke Opisthorchis viverrini to nematode cytoplasmic motility protein. Mol Biochem Parasitol 2016; 207: 1-9. https://doi.org/10.1016/j.molbiopara.2016.04.002
  4. Grant RP, Buttery SM, Ekman GC, Roberts TM, Stewart M. Structure of MFP2 and its function in enhancing MSP polymerization in Ascaris sperm amoeboid motility. J Mol Biol 2005; 347: 583-595. https://doi.org/10.1016/j.jmb.2005.01.054
  5. Unno H, Matsuyama K, Tsuji Y, Goda S, Hiemori K, Tateno H, Hirabayashi J, Hatakeyama T. Identification, characterization, and X-ray crystallographic analysis of a novel type of mannosespecific lectin CGL1 from the pacific oyster Crassostrea gigas. Sci Rep 2016; 6: 29135. https://doi.org/10.1038/srep29135
  6. Jiang S, Wang L, Huang M, Jia Z, Weinert T, Warkentin E, Liu C, Song X, Zhang H, Witt J, Qiu L, Peng G, Song L. DM9 domain containing protein functions as a pattern recognition receptor with broad microbial recognition spectrum. Front Immunol 2017; 8: 1607. https://doi.org/10.3389/fimmu.2017.01607
  7. Sumner JB, Howell SF. Identification of Hemagglutinin of Jack Bean with Concanavalin A. J Bacteriol 1936; 32: 227-237. https://doi.org/10.1128/JB.32.2.227-237.1936
  8. Goldstein IJ, Hollerman CE, Smith EE. Protein-carbohydrate interaction. II. Inhibition studies on the interaction of concanavalin A with polysaccharides. Biochemistry 1965; 4: 876-883. https://doi.org/10.1021/bi00881a013
  9. Derewenda Z, Yariv J, Helliwell JR, Kalb AJ, Dodson EJ, Papiz MZ, Wan T, Campbell J. The structure of the saccharide-binding site of concanavalin A. EMBO J 1989; 8: 2189-2193. https://doi.org/10.1002/j.1460-2075.1989.tb08341.x
  10. Waterhouse A, Bertoni M, Bienert S, Studer G, Tauriello G, Gumienny R, Heer FT, de Beer TAP, Rempfer C, Bordoli L, Lepore R, Schwede T. SWISS-MODEL: homology modelling of protein structures and complexes. Nucleic Acids Res 2018; 46: 296-303. https://doi.org/10.1093/nar/gky427
  11. Rice P, Longden I, Bleasby A. EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet 2000; 16: 276-277. https://doi.org/10.1016/S0168-9525(00)02024-2
  12. Adamova L, Malinovska L, Wimmerova M. New sensitive detection method for lectin hemagglutination using microscopy. Microsc Res Tech 2014; 77: 841-849. https://doi.org/10.1002/jemt.22407
  13. Rosinski-Chupin I, Briolay J, Brouilly P, Perrot S, Gomez SM, Chertemps T, Roth CW, Keime C, Gandrillon O, Couble P, Brey PT. SAGE analysis of mosquito salivary gland transcriptomes during Plasmodium invasion. Cell Microbiol 2007; 9: 708-724. https://doi.org/10.1111/j.1462-5822.2006.00822.x
  14. Beitz E. TEXshade: shading and labeling of multiple sequence alignments using LATEX2 epsilon. Bioinformatics 2000; 16: 135-139. https://doi.org/10.1093/bioinformatics/16.2.135
  15. Pettersen EF, Goddard TD, Huang CC, Meng EC, Couch GS, Croll TI, Morris JH, Ferrin TE. UCSF ChimeraX: Structure visualization for researchers, educators, and developers. Protein Sci 2021; 30: 70-82. https://doi.org/10.1002/pro.3943