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X-WR-CALNAME;VALUE=TEXT:UMCES Events
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DTSTART:20210314T020000
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UID:calendar.22486.field_date_time.0@www.umces.edu
DTSTAMP:20260414T185432Z
CREATED:20210311T183755Z
DESCRIPTION:April 15\, 2021 11:30am to 12:30pm    \n    \n      \n\n\n    
 \n\n              \nInstitute of Marine & Environmental Technology\n      
 \n\n\n\n\n  \n\n    \n\n              \n\n\n      \n  \n\n    \n\n        
       \n\n\nTitle: Opposite Roles of Zebrafish Galectins in In Vitro Attac
 hment and Infection by the Infectious Hematopoietic Necrosis Virus (IHNV)
 \n\n\n\nSpeaker: Kelsey Abernathy (Ph.D. Candidate\, UMB-IMET)\n\n\n\nAbst
 ract: IHNV is a rhabdovirus with a high mortality rate that has major econ
 omic impacts on the salmonid fisheries and aquaculture industry. The virus
  uses cell surface fibronectin as a receptor for attachment and infection\
 , but the exact mechanism remains unknown. Previously published work in ou
 r lab and preliminary data revealed that β-galactoside-binding lectins\, k
 nown as galectins\, interact directly with the IHNV envelope glycoprotein 
 to either promote or inhibit viral attachment and infection of fish epithe
 lial cells. The zebrafish tandem-repeat galectin 9 isoform 1 (Drgal9-L1) d
 isplays two carbohydrate recognition domains (CRD) joined by a linker pept
 ide that are similar but not identical in binding specificity. The goal of
  this study was to explore the mechanism of Drgal9-L1-mediated enhancement
  of IHNV attachment to EPC cells. We showed that Drgal9-L1 crosslinks IHNV
  to cell surface glycans in a carbohydrate-dependent and -specific manner.
  We determined that crosslinking was dependent on two functional CRDs thro
 ugh the development of a C-terminal mutant protein that did not enhance IH
 NV attachment or infection of epithelial cells (EPC cell line). Drgal9-L1 
 crosslinks IHNV to fibronectin on the cell surface\, enhancing viral attac
 hment\, in a carbohydrate-dependent and -specific manner. In addition\, Dr
 gal9-L1 binds to alternative ligands\, β1-integrin and CD147\, to increase
  IHNV attachment. Double antibody inhibition and siRNA knockdown of fibron
 ectin and β1-integrin in EPC significantly reduced Drgal9-L1 mediated atta
 chment of IHNV. We also investigated the protective role of epidermal mucu
 s glycans for preventing Drgal9-L1 mediated viral attachment to the epithe
 lium. All three galectin classes were detected in the zebrafish epidermal 
 mucus\, and Drgal9-L1 as well as Drgal1-L2 were found to bind to mucus gly
 cans in a carbohydrate-specific manner. In a plaque assay\, mucus coating 
 of the cell monolayer reduced the number of IHNV plaques on the EPC cells 
 in a concentration and volume-dependent manner and annulled the Drgal9-L1 
 enhancement of viral attachment and infectivity. Finally\, we identified a
 n alternative mechanism of Drgal1-L2 antiviral protective activity\, as bi
 nding of Drgal1-L2 to surface glycosylated receptors or mucus glycans sign
 ificantly inhibits IHNV attachment. This research has wide ranging applica
 tions for aquaculture disease management\, vaccine development\, and a gen
 eral model of galectin-modulated viral attachment. \n\n\n\nHost: Dr. Gerar
 do Vasta\n\n\n\nIf you would like to attend virtually\, please email imetd
 irectorsoffice@umces.edu
DTSTART;TZID=America/New_York:20210415T113000
DTEND;TZID=America/New_York:20210415T123000
LAST-MODIFIED:20210405T182129Z
SUMMARY:Virtual Defense: Kelsey Abernathy (Ph.D. Candidate\, UMB-IMET)
URL;TYPE=URI:https://www.umces.edu/events/virtual-defense-kelsey-abernathy-
 phd-candidate-umb-imet
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