Characterization of a Porcine Enterocyte Receptor for Group a Rotavirus

Kuhlenschmidt, Mark S.; Rolsma, Mark D.; Kuhlenschmidt, Theresa B.; Gelberg, Howard B.

doi:10.1007/978-1-4899-1828-4_21

Cited by 6 publications

(8 citation statements)

References 10 publications

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Section: Discussionmentioning

confidence: 99%

“…Purified GM2 and GM3 have the greatest inhibitory effect in preventing binding of iodinated triple-layered OSU particles to porcine enterocytes and MA104 cells (embryonic rhesus monkey kidney cells) [74,153]. Some inhibition was seen with GM1 and GD1a, even less with GD1b and GT1b and no inhibition with GA1 and GA2 [74,153]. To correlate these findings to pathogenesis, GSLs were isolated from pooled intestines of newborn to four week-old piglets and porcine GM3 (either N-glycolylneuraminic acid [NeuGc] or N-acetylneuraminic acid [NeuAc]) was identified as the attachment receptor of OSU [74,75].…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, binding of triple-layered OSU to Lec-2 cells, which have 90% reduced sialylation of glycolipids and –proteins, is reconstituted to levels greater than that of control cells by addition of exogenous NeuGcGM3 [75]. In piglets, NeuGcGM3 rapidly declines in the first four weeks of life in the intestine while NeuAcGM3 is found in lower amounts and only gradually decreases over the first 16 weeks, suggesting NeuGcGM3 determines severity of disease [153]. Thus, while OSU can bind to multiple different gangliosides, GM3 is most likely the relevant attachment receptor in the porcine intestine.…”

Section: Discussionmentioning

confidence: 99%

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Glycosphingolipids as Receptors for Non-Enveloped Viruses

Taube

Jiang

Wobus

2010

Viruses

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Glycosphingolipids are ubiquitous molecules composed of a lipid and a carbohydrate moiety. Their main functions are as antigen/toxin receptors, in cell adhesion/recognition processes, or initiation/modulation of signal transduction pathways. Microbes take advantage of the different carbohydrate structures displayed on a specific cell surface for attachment during infection. For some viruses, such as the polyomaviruses, binding to gangliosides determines the internalization pathway into cells. For others, the interaction between microbe and carbohydrate can be a critical determinant for host susceptibility. In this review, we summarize the role of glycosphingolipids as receptors for members of the non-enveloped calici-, rota-, polyoma- and parvovirus families.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Glycosphingolipids as Receptors for Non-Enveloped Viruses

Taube

Jiang

Wobus

2010

Viruses

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“…For all in vitro experiments, Group A porcine rotavirus (OSU strain (P9(7)G5)) was propagated in MA104 cells (ATCC HTB 37) and triple and double-layered virus particles isolated by gradient purification using the following modification of standard techniques [23,24,25]. A single gradient centrifugation step was performed using a near vertical tube rotor (Beckman, NVT65) for 6.5 h, at 60,000 rpm (291,110× g) instead of dual gradient runs using an SW 55 swinging bucket rotor, at 35,000 rpm, (116,140× g), for 30 h. For in vivo studies, the above virus was passed in newborn piglets and partially purified from feces as previously described [26].…”

Section: Methodsmentioning

confidence: 99%

“…Detector settings were as follows: drift tube temperature = 60 °C, exhaust temperature = 35.9 °C, gas (N 2 ) flow rate = 0.7–0.9 SLPM and pressure = 6.8 psig; the solvent pressure was 0.2 psig. Purity of the HPLC fractions and final SLPE or LPE pool was assessed by analytical TLC [23,24,25]. …”

Section: Methodsmentioning

confidence: 99%

Inhibition of Rotavirus Infectivity by a Neoglycolipid Receptor Mimetic

et al. 2011

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Group A rotaviruses are a major cause of diarrhea in the young of many mammalian species. In rotavirus infected piglets mortality can be as high as 60%. Previous research in this laboratory has identified a porcine intestinal GM3 ganglioside receptor that is required for sialic acid-dependent rotavirus recognition of host cells. In addition, we previously demonstrated exogenously added GM3 can competitively inhibit porcine rotavirus binding and infectivity of host cells in vitro. Sialyllactose, the carbohydrate moiety of GM3, is approximately 3 orders of magnitude less effective than GM3 at inhibiting rotavirus binding to cells. Furthermore, production of therapeutic quantities of GM3 ganglioside for use as an oral carbomimetic in swine is cost prohibitive. In an effort to circumvent these problems, a sialyllactose-containing neoglycolipid was synthesized and evaluated for its ability to inhibit rotavirus binding and infectivity of host cells. Sialyllactose was coupled to dipalmitoylphosphatidylethanolamine (PE) by reductive amination and the product (SLPE) purified by HPLC. Characterization of the product showed a single primulin (lipid) and resorcinol (sialic acid) positive band by thin layer chromatography and quantification of phosphate and sialic acid yielded a 1:1 molar ratio. Mass spectroscopy confirmed a molecular weight coinciding with SLPE. Concentration-dependent binding of rotavirus to SLPE was demonstrated using a thin-layer overlay assay. Using concentrations comparable to GM3, SLPE was also shown to inhibit rotavirus binding to host cells by 80%. Furthermore, SLPE was shown to decrease rotavirus infection of host cells by over 90%. Finally, preliminary results of in vivo animal challenge studies using newborn piglets in their natural environment, demonstrated SLPE afforded complete protection from rotavirus disease. The efficacy of SLPE in inhibiting rotavirus binding and infection in vitro and in vivo, coupled with its relatively low-cost, large-scale production capabilities make SLPE a promising candidate for further exploration as a possible prophylactic or therapeutic nutriceutical for combating rotavirus disease in animals. Most importantly, the results presented here provide proof of concept that the nutriceutical approach of providing natural or synthetic dietary receptor mimetics for protection against gastrointestinal virus infectious disease in all species is plausible.

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Sialic Acid Receptors of Viruses

Matrosovich

Herrler

Klenk

2013

Topics in Current Chemistry

232

262

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Sialic acid linked to glycoproteins and gangliosides is used by many viruses as a receptor for cell entry. These viruses include important human and animal pathogens, such as influenza, parainfluenza, mumps, corona, noro, rota, and DNA tumor viruses. Attachment to sialic acid is mediated by receptor binding proteins that are constituents of viral envelopes or exposed at the surface of non-enveloped viruses. Some of these viruses are also equipped with a neuraminidase or a sialyl-O-acetyl-esterase. These receptor-destroying enzymes promote virus release from infected cells and neutralize sialic acid-containing soluble proteins interfering with cell surface binding of the virus. Variations in the receptor specificity are important determinants for host range, tissue tropism, pathogenicity, and transmissibility of these viruses.

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Characterization of a Porcine Enterocyte Receptor for Group a Rotavirus

Cited by 6 publications

References 10 publications

Glycosphingolipids as Receptors for Non-Enveloped Viruses

Glycosphingolipids as Receptors for Non-Enveloped Viruses

Inhibition of Rotavirus Infectivity by a Neoglycolipid Receptor Mimetic

Sialic Acid Receptors of Viruses

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