Human adenovirus type 5 increases host cell fucosylation and modifies Ley antigen expression. (31st March 2019)
- Record Type:
- Journal Article
- Title:
- Human adenovirus type 5 increases host cell fucosylation and modifies Ley antigen expression. (31st March 2019)
- Main Title:
- Human adenovirus type 5 increases host cell fucosylation and modifies Ley antigen expression
- Authors:
- Gutiérrez-Huante, Kathya
Salinas-Marín, Roberta
Mora-Montes, Héctor M
Gonzalez, Ramón A
Martínez-Duncker, Iván - Abstract:
- Abstract: Certain viral infections are known to modify the glycosylation profile of infected cells through the overexpression of specific host cell fucosyltransferases (FUTs). Infection with CMV (cytomegalovirus), HCV (hepatitis C virus), HSV-1 (herpes simplex virus type-1) and VZV (varicella-zoster virus) increase the expression of fucosylated epitopes, including antigens sLe x (Siaα2–3 Galβ1–4(Fucα1–3)GlcNAcβ1-R) and Le y (Fucα1–2 Galβ1–4(Fucα1–3)GlcNAcβ1-R). The reorganization of the glycocalyx induced by viral infection may favor the spread of viral progeny, and alter diverse biological functions mediated by glycans, including recognition by the adaptive immune system. In this work, we aimed to establish whether infection with human adenovirus type 5 (HAd5), a well-known viral vector and infectious agent, causes changes in the glycosylation profile of A549 cells, used as a model of lung epithelium, a natural target of HAd5. We demonstrate for the first time that HAd5 infection causes a significant increase in the cell surface de novo fucosylation, as assessed by metabolic labeling, and that such modification is dependent on the expression of viral genes. The main type of increased fucosylation was determined to be in α1–2 linkage, as assessed by UEA-I lectin binding and supported by the overexpression of FUT1 and FUT2 . Also, HAd5-infected cells showed a heterogeneous change in the expression profile of the bi-fucosylated Le y antigen, an antigen associated with enhancedAbstract: Certain viral infections are known to modify the glycosylation profile of infected cells through the overexpression of specific host cell fucosyltransferases (FUTs). Infection with CMV (cytomegalovirus), HCV (hepatitis C virus), HSV-1 (herpes simplex virus type-1) and VZV (varicella-zoster virus) increase the expression of fucosylated epitopes, including antigens sLe x (Siaα2–3 Galβ1–4(Fucα1–3)GlcNAcβ1-R) and Le y (Fucα1–2 Galβ1–4(Fucα1–3)GlcNAcβ1-R). The reorganization of the glycocalyx induced by viral infection may favor the spread of viral progeny, and alter diverse biological functions mediated by glycans, including recognition by the adaptive immune system. In this work, we aimed to establish whether infection with human adenovirus type 5 (HAd5), a well-known viral vector and infectious agent, causes changes in the glycosylation profile of A549 cells, used as a model of lung epithelium, a natural target of HAd5. We demonstrate for the first time that HAd5 infection causes a significant increase in the cell surface de novo fucosylation, as assessed by metabolic labeling, and that such modification is dependent on the expression of viral genes. The main type of increased fucosylation was determined to be in α1–2 linkage, as assessed by UEA-I lectin binding and supported by the overexpression of FUT1 and FUT2 . Also, HAd5-infected cells showed a heterogeneous change in the expression profile of the bi-fucosylated Le y antigen, an antigen associated with enhanced cell proliferation and inhibition of apoptosis. … (more)
- Is Part Of:
- Glycobiology. Volume 29:Number 6(2019)
- Journal:
- Glycobiology
- Issue:
- Volume 29:Number 6(2019)
- Issue Display:
- Volume 29, Issue 6 (2019)
- Year:
- 2019
- Volume:
- 29
- Issue:
- 6
- Issue Sort Value:
- 2019-0029-0006-0000
- Page Start:
- 469
- Page End:
- 478
- Publication Date:
- 2019-03-31
- Subjects:
- adenovirus -- fucose -- fucosyltransferase -- Ley -- virus
Glycoproteins -- Periodicals
Glycolipids -- Periodicals
Glycoconjugates -- Periodicals
572.567 - Journal URLs:
- http://glycob.oupjournals.org/ ↗
http://ukcatalogue.oup.com/ ↗ - DOI:
- 10.1093/glycob/cwz017 ↗
- Languages:
- English
- ISSNs:
- 0959-6658
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4196.303000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 11778.xml