Shaan virus (ShaV), a novel species of the genus , family , was isolated from an insectivore bat (Miniopterus schreibersii) in Korea in 2016. ShaV particles contain a hemagglutinin-neuraminidase (HN) glycoprotein in their envelope that allows the virus to target cells. Typically, diverse paramyxoviruses with HN glycoprotein are reported to interact predominantly with sialic acids, but there are no studies of receptors for ShaV. In this study, the identification of potential receptors for ShaV was demonstrated using sialidase treatments, glycan microarray, magnetic bead-based virus binding assay, and neuraminidase inhibitor treatments. Pretreatment of MARC-145 cells with sialidase, which cleaves α2,3-linked sialic acids, showed higher inhibition of viral infection than α2,6-linked-specific sialidase. These data were supported by the binding of ShaV to predominantly α2,3-linked sialylated glycans in the screening of sialyl linkage patterns through glycan microarray. To further confirm the direct interaction between ShaV and α2,3-linked sialic acids, ShaV was incubated with α2,3- or α2,6-linked sialylated glycans conjugated to magnetic beads, and binding signals were detected only for α2,3-linked sialylated glycans. In addition, the potential of sialic acids as a receptor was demonstrated by the viral replication inhibitory effect of the neuraminidase inhibitor 2,3-dehydro-2-deoxy--acetylneuraminicacid (DANA) in the mature virion release steps. Collectively, these results support that α2,3-linked sialic acids are the potential receptor for ShaV infection in MARC-145 cells. Bats host major mammalian paramyxoviruses, and novel paramyxoviruses are increasingly being reported around the world. Shaan virus (ShaV), from the genus , family , has a potential attachment glycoprotein, HN. Here, we identify that ShaV binds to sialic acid and demonstrate that α2,3-linked sialic acids are the potential receptor for ShaV infection. The presented data regarding ShaV receptor specificity will enable studies into the viral tropism for the host and contribute to the development of new antiviral strategies targeting viral receptors.
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http://dx.doi.org/10.1128/spectrum.01256-22 | DOI Listing |
Vet Sci
November 2024
Animal Infectious Disease Laboratory, College of Veterinary Medicine, Yangzhou University, Yangzhou 225012, China.
Pigeon Newcastle disease (ND) is the most common viral infectious disease in the pigeon industry, caused by pigeon paramyxovirus type 1 (PPMV-1), a variant of chicken-origin Newcastle disease virus (NDV). Previous studies have identified significant amino acid differences between PPMV-1 and chicken-origin NDV at positions 347 and 349 in the hemagglutinin-neuraminidase (HN) protein, with PPMV-1 predominantly exhibiting glycine (G) at position 347 and glutamic acid (E) at position 349, while most chicken-origin NDVs show E at position 347 and aspartic acid (D) at position 349. However, the impact of these amino acid substitutions remains unclear.
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December 2024
Institute of Virology, University of Veterinary Medicine Hannover, Hannover, Germany.
Rotaviruses, non-enveloped viruses with a double-stranded RNA genome, are the leading etiological pathogen of acute gastroenteritis in young children and animals. The P[11] genotype of rotaviruses exhibits a tropism for neonates. In the present study, a binding assay using synthetic oligosaccharides demonstrated that the VP8* protein of P[11] porcine rotavirus (PRV) strain 4555 binds to lacto-N-neotetraose (LNnT) with the sequence Galβ1,4-GlcNAcβ1,3-Galβ1,4-Glc, one of the core parts of histo-blood group antigen (HBGA) and milk glycans.
View Article and Find Full Text PDFFront Oncol
December 2024
Department of Chemistry, Biochemistry and Physics, South Dakota State University, Brookings, SD, United States.
Cancers utilize a simple glycan, Sialic Acid, to engage in metastatic processes via the Sialic acid (Sia) -Selectin pathway. Selectins recognize and bind to sialylated substrates, resulting in adhesion, migration, and extravasation, however, how deviations from the canonical form of Sia regulate binding to Selectin receptors (E, L, and P) on hemopoietic cells resulting in these metastatic processes, remained a gap in knowledge. De-O-acetylated Sias has been recently shown to be an integral substrate to the binding of sialic acid binding proteins.
View Article and Find Full Text PDFBackground: Allergen-specific immunotherapy (AIT) is so far the only disease-modifying therapy for allergy, resulting in a long-lasting tolerance. However, the existing safety concerns and the need for more efficacious alternatives that shorten the duration of treatment have stimulated research into the development of novel alternatives. Some of these novel alternatives involve modifying allergens with molecules that target innate immunomodulatory receptors to suppress the immune activity of immune cells.
View Article and Find Full Text PDFRes Pract Thromb Haemost
November 2024
Joint Department of Biomedical Engineering of University of North Carolina, Chapel Hill and North Carolina State University, Raleigh, North Carolina, USA.
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