Enterovirus 70 Binds to Different Glycoconjugates Containing α2,3-Linked Sialic Acid on Different Cell Lines

Nokhbeh, M.R.; Hazra, Samir; Alexander, David; Khan, Ahmar; McAllister, Morgan; Suuronen, Erik J.; Griffith, May; Dimock, Kenneth

doi:10.1128/jvi.79.11.7087-7094.2005

Cited by 48 publications

(55 citation statements)

References 76 publications

(89 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The other serotypes of HEV-D (EV68 and EV70) use DAF as a receptor in HeLa cells (Karnauchow et al, 1996;Blomqvist et al, 2002). EV70 also uses sialic acid-containing receptors in a variety of other human cell lines (Alexander & Dimock, 2002;Haddad et al, 2004;Nokhbeh et al, 2005). Our results suggest that EV94 does not need DAF to infect RD cells.…”

Section: Discussionsupporting

confidence: 52%

Enterovirus 94, a proposed new serotype in human enterovirus species D

Smura

Junttila

Blomqvist

et al. 2007

Journal of General Virology

View full text Add to dashboard Cite

The genus Enterovirus (family Picornaviridae) contains five species with strains isolated from humans: Human enterovirus A (HEV-A), HEV-B, HEV-C, HEV-D and Poliovirus. In this study, a proposed new serotype of HEV-D was characterized. Four virus strains were isolated from sewage in Egypt and one strain from acute flaccid paralysis cases in the Democratic Republic of the Congo. The complete genome of one environmental isolate, the complete coding sequence of one clinical isolate and complete VP1 regions from the other isolates were sequenced. These isolates had 66.6-69.4 % nucleotide similarity and 74.7-76.6 % amino acid sequence similarity in the VP1 region with the closest enterovirus serotype, enterovirus 70 (EV70), suggesting that the isolates form a new enterovirus type, tentatively designated enterovirus 94 (EV94). Phylogenetic analyses including sequences of the 59 UTR, VP1 and 3D regions demonstrated that EV94 isolates formed a monophyletic group within the species HEV-D. No evidence of recombination was found between EV94 and the other HEV-D serotypes, EV68 and EV70. Further biological characterization showed that EV94 was acid stable and had a wide cell tropism in vitro. Attempts to prevent replication with protective antibodies to known enterovirus receptors (poliovirus receptor, vitronectin a v b 3 receptor and decay accelerating factor) were not successful. Seroprevalence studies in the Finnish population revealed a high prevalence of this virus over the past two decades. INTRODUCTIONThe genus Enterovirus (family Picornaviridae) contains a large group of human pathogens. Although the majority of enterovirus infections are subclinical, enterovirus infection can lead to a variety of acute and chronic diseases including mild upper respiratory illness, febrile rash, aseptic meningitis, encephalitis, acute haemorrhagic conjunctivitis, pleurodynia, acute flaccid paralysis (AFP), diabetes, myocarditis and neonatal sepsis-like disease (Pallansch & Roos, 2001). The primary site of enterovirus infection is the mucosal tissue of the respiratory or gastrointestinal tract. After spreading through the lymphatic system and circulation, the virus can infect secondary target tissues. The secondary replication sites largely define the clinical manifestations of a given enterovirus strain. In the intestinal mucosa, virus replication can continue for several weeks, during which time progeny virus is shed into faeces.The enterovirus genome is a single-stranded RNA molecule of approximately 7500 nt consisting of a single open reading frame flanked by non-coding 59 and 39 regions. The 59 UTR contains an internal ribosome-binding site, which is essential for translation initiation (Pelletier & Sonenberg, 1988;Molla et al., 1992;Chen & Sarnow, 1995). The 39 UTR forms highly conserved secondary and tertiary structures that are thought to be important in replication initiation (Pilipenko et al., 1992(Pilipenko et al., , 1996Mirmomeni et al., 1997). The open reading frame is translated into a single, large polypeptide, which is...

show abstract

Section: Discussionsupporting

confidence: 52%

Enterovirus 94, a proposed new serotype in human enterovirus species D

Smura

Junttila

Blomqvist

et al. 2007

Journal of General Virology

View full text Add to dashboard Cite

show abstract

“…In many studies, glycosylation has been shown to affect the viral attachment or penetration steps via the modification of cellular receptors or viral envelope glycoproteins. For instance, the O-linked glycoproteins of ␣2,3-or ␣2,6-linked sialic acids were shown to play important roles during infection by IAV and other viruses, including the coxsackievirus A24 variant and enterovirus 70 (42)(43)(44)(45). Furthermore, the envelope proteins of many viruses, such as human immunodeficiency virus type 1, HCV, Ebola virus, and herpes simplex virus 1, have been shown to be modified by O-linked glycosylation, which influences the attachment of viral virions to the cell surface (42,(46)(47)(48).…”

Section: Discussionmentioning

confidence: 99%

Influenza A Virus-Induced Expression of a GalNAc Transferase, GALNT3, via MicroRNAs Is Required for Enhanced Viral Replication

Nakamura

Horie

Daidoji

et al. 2016

J Virol

View full text Add to dashboard Cite

Influenza A virus (IAV) affects the upper and lower respiratory tracts and rapidly induces the expression of mucins, which are common O-glycosylated proteins, on the epithelial surfaces of the respiratory tract. Although mucin production is associated with the inhibition of virus transmission as well as characteristic clinical symptoms, little is known regarding how mucins are produced on the surfaces of respiratory epithelial cells and how they affect IAV replication. In this study, we found that two microRNAs (miRNAs), miR-17-3p and miR-221, which target GalNAc transferase 3 (GALNT3) mRNA, are rapidly downregulated in human alveolar basal epithelial cells during the early stage of IAV infection. We demonstrated that the expression of GALNT3 mRNA is upregulated in an IAV replication-dependent fashion and leads to mucin production in bronchial epithelial cells. A lectin microarray analysis revealed that the stable expression of GALNT3 by human alveolar basal epithelial cells induces mucin-type O-glycosylation modifications similar to those present in IAV-infected cells, suggesting that GALNT3 promotes mucin-type O-linked glycosylation in IAV-infected cells. Notably, analyses using short interfering RNAs and miRNA mimics showed that GALNT3 knockdown significantly reduces IAV replication. Furthermore, IAV replication was markedly decreased in embryonic fibroblast cells obtained from galnt3-knockout mice. Interestingly, IAV-infected galnt3-knockout mice exhibited high mortality and severe pathological alterations in the lungs compared to those of wild-type mice. Our results demonstrate not only the molecular mechanism underlying rapid mucin production during IAV infection but also the contribution of O-linked glycosylation to the replication and propagation of IAV in lung cells. IMPORTANCEViral infections that affect the upper or lower respiratory tracts, such as IAV, rapidly induce mucin production on the epithelial surfaces of respiratory cells. However, the details of how mucin-type O-linked glycosylation is initiated by IAV infection and how mucin production affects viral replication have not yet been elucidated. In this study, we show that levels of two miRNAs that target the UDP-GalNAc transferase GALNT3 are markedly decreased during the early stage of IAV infection, resulting in the upregulation of GALNT3 mRNA. We also demonstrate that the expression of GALNT3 initiates mucin production and affects IAV replication in infected cells. This is the first report demonstrating the mechanism underlying the miRNA-mediated initiation of mucin-type O-glycosylation in IAV-infected cells and its role in viral replication. Our results have broad implications for understanding IAV replication and suggest a strategy for the development of novel anti-influenza approaches.

show abstract

“…The cellular receptors for several members of the Picornaviridae family have been described, including decay-accelerating factor (DAF), intercellular adhesion molecule 1 (ICAM-1), low-density lipoprotein receptor (LDL-R), sialic acid, coxsackie and adenovirus receptor (CAR), various integrins, and heparan sulfate (25,26,34,44,49,50,53,57,61,62,75). CVA24v and EV70 replicate in both conjunctival and corneal cells in vivo and in vitro (50,76).…”

mentioning

confidence: 99%

Coxsackievirus A24 Variant Uses Sialic Acid-Containing O -Linked Glycoconjugates as Cellular Receptors on Human Ocular Cells

Mistry¹,

Inoue²,

Jamshidi³

et al. 2011

J Virol

View full text Add to dashboard Cite

Coxsackievirus A24 variant (CVA24v) is a main causative agent of acute hemorrhagic conjunctivitis (AHC), which is a highly contagious eye infection. Previously it has been suggested that CVA24v uses sialic acidcontaining glycoconjugates as attachment receptors on corneal cells, but the nature of these receptors is poorly described. Here, we set out to characterize and identify the cellular components serving as receptors for CVA24v. Binding and infection experiments using corneal cells treated with deglycosylating enzymes or metabolic inhibitors of de novo glycosylation suggested that the receptor(s) used by CVA24v are constituted by sialylated O-linked glycans that are linked to one or more cell surface proteins but not to lipids. CVA24v bound better to mouse L929 cells overexpressing human P-selectin glycoprotein ligand-1 (PSGL-1) than to mocktransfected cells, suggesting that PSGL-1 is a candidate receptor for CVA24v. Finally, binding competition experiments using a library of mono-and oligosaccharides mimicking known PSGL-1 glycans suggested that CVA24v binds to Neu5Ac␣2,3Gal disaccharides (Neu5Ac is N-acetylneuraminic acid). These results provide further insights into the early steps of the CVA24v life cycle.

show abstract

Enterovirus 70 Binds to Different Glycoconjugates Containing α2,3-Linked Sialic Acid on Different Cell Lines

Cited by 48 publications

References 76 publications

Enterovirus 94, a proposed new serotype in human enterovirus species D

Enterovirus 94, a proposed new serotype in human enterovirus species D

Influenza A Virus-Induced Expression of a GalNAc Transferase, GALNT3, via MicroRNAs Is Required for Enhanced Viral Replication

Coxsackievirus A24 Variant Uses Sialic Acid-Containing O -Linked Glycoconjugates as Cellular Receptors on Human Ocular Cells

Contact Info

Product

Resources

About