Glycosphingolipids as Receptors for Non-Enveloped Viruses

Taube, Stefan; Jiang, Mengxi; Wobus, Christiane E.

doi:10.3390/v2041011

Cited by 87 publications

(74 citation statements)

References 213 publications

(309 reference statements)

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“…Our data indicated that MNV, similarly to human norovirus (13,52), may have evolved multiple strategies to bind distinct glycan receptors on the cell surface. Interestingly, a strain-dependent SA-binding phenotype is also observed in rotaviruses, where animal rotaviruses bind terminal SA in a neuraminidase-sensitive manner, while the neuraminidase-insensitive human rotaviruses attach to internal SA, which are inaccessible to neuraminidase cleavage (12,17,54). Additional studies are required to determine whether the neuraminidase-insensitive CR3 strain can utilize internal SA moieties during attachment.…”

Section: Discussionmentioning

confidence: 99%

“…The majority of surface proteins are glycosylated, and most of them are N-glycosylated (18). Because glycans are abundantly expressed on gastrointestinal and respiratory epithelial cells, they are exploited as receptors by many viruses, bacteria, and toxins (e.g., see references 2,36,43,49,54,63). Glycan composition differs greatly between species, tissues, and cell types and subsequently contributes to host specificity, tropism, and pathogenicity of many different pathogens (reviewed in references 5, 43, and 54).…”

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confidence: 99%

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Murine Noroviruses Bind Glycolipid and Glycoprotein Attachment Receptors in a Strain-Dependent Manner

Taube

Perry

McGreevy

et al. 2012

J Virol

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Human norovirus infections are the most common cause of acute nonbacterial gastroenteritis in humans worldwide, and glycan binding plays an important role in the susceptibility to these infections. However, due to the lack of an efficient cell culture system or small animal model for human noroviruses, little is known about the biological role of glycan binding during infection. Murine noroviruses (MNV) are also enteric viruses that bind to cell surface glycans, but in contrast to their human counterparts, they can be grown in tissue culture and a small animal host. In this study, we determined glycan-binding specificities of the MNV strains MNV-1 and CR3 in vitro , identified molecular determinants of glycan binding, and analyzed infection in vivo . We showed that unlike MNV-1, CR3 binding to murine macrophages was resistant to neuraminidase treatment and glycosphingolipid depletion. Both strains depended on N-linked glycoproteins for binding, while only MNV-1 attachment to macrophages was sensitive to O-linked glycoprotein depletion. In vivo , CR3 showed differences in tissue tropism compared to MNV-1 by replicating in the large intestine. Mapping of a glycan-binding site in the MNV-1 capsid by reverse genetics identified a region topologically similar to the histo-blood group antigen (HBGA)-binding sites of the human norovirus strain VA387. The recombinant virus showed distinct changes in tissue tropism compared to wild-type virus. Taken together, our data demonstrate that MNV strains evolved multiple strategies to bind different glycan receptors on the surface of murine macrophages and that glycan binding contributes to tissue tropism in vivo .

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Murine Noroviruses Bind Glycolipid and Glycoprotein Attachment Receptors in a Strain-Dependent Manner

Taube

Perry

McGreevy

et al. 2012

J Virol

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“…Besides these important biological functions they are also used as receptors for many viruses, including different members of the Polyomaviridae family (simian virus 40, murine polyomavirus, BK virus, JC virus, Merkel cell polyomavirus) (14,15), paramyxoviruses (Newcastle disease virus and Sendai virus) (16), bovine adeno-associated virus (17), influenza virus (18), murine norovirus (19), and rotavirus (10,20).…”

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confidence: 99%

Gangliosides Have a Functional Role during Rotavirus Cell Entry

Martı́nez

López

Arias

et al. 2013

J Virol

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Cell entry of rotaviruses is a complex process, which involves sequential interactions with several cell surface molecules. Among the molecules implicated are gangliosides, glycosphingolipids with one or more sialic acid (SA) residues. The role of gangliosides in rotavirus cell entry was studied by silencing the expression of two key enzymes involved in their biosynthesis-the UDP-glucose:ceramide glucosyltransferase (UGCG), which transfers a glucose molecule to ceramide to produce glucosylceramide GlcCer, and the lactosyl ceramide-␣-2,3-sialyl transferase 5 (GM3-s), which adds the first SA to lactoceramide-producing ganglioside GM3. Silencing the expression of both enzymes resulted in decreased ganglioside levels (as judged by GM1a detection). Four rotavirus strains tested (human Wa, simian RRV, porcine TFR-41, and bovine UK) showed a decreased infectivity in cells with impaired ganglioside synthesis; however, their replication after bypassing the entry step was not affected, confirming the importance of gangliosides for cell entry of the viruses. Interestingly, viral binding to the cell surface was not affected in cells with inhibited ganglioside synthesis, but the infectivity of all strains tested was inhibited by preincubation of gangliosides with virus prior to infection. These data suggest that rotaviruses can attach to cell surface in the absence of gangliosides but require them for productive cell entry, confirming their functional role during rotavirus cell entry.

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“…Briefly, GIPSLs are distinguishable from traditional glycosphingolipids (GSLs) by the relation of the carbohydrate to the ceramide moiety; specifically, the carbohydrate is coupled to the lipophilic portion of the molecule via an intermittent inositol phosphate (56). While GSLs present on vertebrate cells can function as receptors for bacteria and viruses via their carbohydrate structure (57), the role of the closely related GIPSLs present on amoe- (58) indicated the presence of acidic groups on GIPSLs found in A. castellanii plasma membrane, an important consideration given that both MNV-1 and select strains of genogroup II. 4 HuNoV have been shown to bind negatively charged sialylated structures that are also present on acidic GSLs (58)(59)(60)(61).…”

Section: Fig 4 Mnv-1 Associated With a Castellanii (A) And A Polyphmentioning

confidence: 99%

Interactions between Human Norovirus Surrogates and Acanthamoeba spp

Hsueh

Gibson

2015

Appl Environ Microbiol

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Human noroviruses (HuNoVs) are the most common cause of food-borne disease outbreaks, as well as virus-related waterborne disease outbreaks in the United States. Here, we hypothesize that common free-living amoebae (FLA)-ubiquitous in the environment, known to interact with pathogens, and frequently isolated from water and fresh produce-could potentially act as reservoirs of HuNoV and facilitate the environmental transmission of HuNoVs. To investigate FLA as reservoirs for HuNoV, the interactions between two Acanthamoeba species, A. castellanii and A. polyphaga, as well as two HuNoV surrogates, murine norovirus type 1 (MNV-1) and feline calicivirus (FCV), were evaluated. The results showed that after 1 h of amoeba-virus incubation at 25°C, 490 and 337 PFU of MNV-1/ml were recovered from A. castellanii and A. polyphaga, respectively, while only few or no FCVs were detected. In addition, prolonged interaction of MNV-1 with amoebae was investigated for a period of 8 days, and MNV-1 was demonstrated to remain stable at around 200 PFU/ml from day 2 to day 8 after virus inoculation in A. castellanii. Moreover, after a complete amoeba life cycle (i.e., encystment and excystment), infectious viruses could still be detected. To determine the location of virus associated with amoebae, immunofluorescence experiments were performed and showed MNV-1 transitioning from the amoeba surface to inside the amoeba over a 24-h period. These results are significant to the understanding of how HuNoVs may interact with other microorganisms in the environment in order to aid in its persistence and survival, as well as potential transmission in water and to vulnerable food products such as fresh produce.N oroviruses belong to a highly genetically and antigenically diverse genus Norovirus of the Caliciviridae family. Noroviruses are divided into five genogroups (GI, GII, GIII, GIV, and GV) according to the genetic similarity of highly conserved areas of their genomes, such as the RNA-dependent RNA polymerase and the VP1 protein (1), with GI, GII, and GIV associated with human diseases. They are important enteric pathogens responsible for at least 50% of all gastroenteritis outbreaks worldwide (2) and, partially due to their high infectivity and low infectious dose (18 to 1,000 virus particles) (3), human noroviruses (HuNoVs) are the most common cause of food-borne disease outbreaks in the United States (4).Transmission of HuNoV occurs primarily through exposure to contaminated food or water, person-to-person contact, aerosolized particles from vomitus, and contact with contaminated fomites (e.g., door handles, toilets, tables, and elevator buttons) (5). Numerous waterborne disease outbreaks have been linked to HuNoV (6-9), and HuNoVs are often detected in surface water (10), wastewater (11), and even finished drinking water (12). With respect to food-borne disease outbreaks, the most common food commodity implicated in HuNoV outbreaks is fresh produce, specifically leafy greens (13); however, the route of transmission and point of contami...

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Glycosphingolipids as Receptors for Non-Enveloped Viruses

Cited by 87 publications

References 213 publications

Murine Noroviruses Bind Glycolipid and Glycoprotein Attachment Receptors in a Strain-Dependent Manner

Murine Noroviruses Bind Glycolipid and Glycoprotein Attachment Receptors in a Strain-Dependent Manner

Gangliosides Have a Functional Role during Rotavirus Cell Entry

Interactions between Human Norovirus Surrogates and Acanthamoeba spp

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