{"title":"甘露糖结合凝集素巨片吸虫DM9-1的凝集活性。","authors":"Wansika Phadungsil, Rudi Grams","doi":"10.3347/kjp.2021.59.2.173","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":49938,"journal":{"name":"Korean Journal of Parasitology","volume":"59 2","pages":"173-178"},"PeriodicalIF":1.4000,"publicationDate":"2021-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/99/9e/kjp-59-2-173.PMC8106982.pdf","citationCount":"2","resultStr":"{\"title\":\"Agglutination Activity of Fasciola gigantica DM9-1, a Mannose-Binding Lectin.\",\"authors\":\"Wansika Phadungsil, Rudi Grams\",\"doi\":\"10.3347/kjp.2021.59.2.173\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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.</p>\",\"PeriodicalId\":49938,\"journal\":{\"name\":\"Korean Journal of Parasitology\",\"volume\":\"59 2\",\"pages\":\"173-178\"},\"PeriodicalIF\":1.4000,\"publicationDate\":\"2021-04-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/99/9e/kjp-59-2-173.PMC8106982.pdf\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Korean Journal of Parasitology\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://doi.org/10.3347/kjp.2021.59.2.173\",\"RegionNum\":4,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2021/4/22 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q3\",\"JCRName\":\"PARASITOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Korean Journal of Parasitology","FirstCategoryId":"3","ListUrlMain":"https://doi.org/10.3347/kjp.2021.59.2.173","RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2021/4/22 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"PARASITOLOGY","Score":null,"Total":0}
Agglutination Activity of Fasciola gigantica DM9-1, a Mannose-Binding Lectin.
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.
期刊介绍:
The Korean Journal of Parasitology is the official journal paperless, on-line publication after Vol. 53, 2015 of The Korean Society for Parasitology and Tropical Medicine. Abbreviated title is ‘Korean J Parasitol’. It was launched in 1963. It contains original articles, case reports, brief communications, reviews or mini-reviews, book reviews, and letters to the editor on parasites of humans and animals, vectors, host-parasite relationships, zoonoses, and tropical medicine. It is published bimonthly in February, April, June, August, October, and December each year. Supplement numbers are at times published. All of the manuscripts are peer-reviewed.