3
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: found
      Is Open Access

      Wild and domestic animals variably display Neu5Ac and Neu5Gc sialic acids

      research-article

      Read this article at

      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          Sialic acids are used as a receptor by several viruses and variations in the linkage type or C-5 modifications affect the binding properties. A species barrier for multiple viruses is present due to α2,3- or α2,6-linked sialic acids. The C-5 position of the sialic acid can be modified to form N-acetylneuraminic acid (Neu5Ac) or N-glycolylneuraminic acid (Neu5Gc), which acts as a determinant for host susceptibility for pathogens such as influenza A virus, rotavirus, and transmissible gastroenteritis coronavirus. Neu5Gc is present in most mammals such as pigs and horses but is absent in humans, ferrets, and dogs. However, little is known about C-5 content in wildlife species or how many C-5 modified sialic acids are present on N-linked glycans or glycolipids. Using our previously developed tissue microarray system, we investigated how 2 different lectins specific for Neu5Gc can result in varying detection levels of Neu5Gc glycans. We used these lectins to map Neu5Gc content in wild Suidae, Cervidae, tigers, and European hedgehogs. We show that Neu5Gc content is highly variable among different species. Furthermore, the removal of N-linked glycans reduces the binding of both Neu5Gc lectins while retention of glycolipids by omitting methanol treatment of tissues increases lectin binding. These findings highlight the importance of using multiple Neu5Gc lectins as the rich variety in which Neu5Gc is displayed can hardly be detected by a single lectin.

          Related collections

          Most cited references51

          • Record: found
          • Abstract: found
          • Article: not found

          Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals.

          Interspecies transmission of influenza A viruses circulating in wild aquatic birds occasionally results in influenza outbreaks in mammals, including humans. To identify early changes in the receptor binding properties of the avian virus hemagglutinin (HA) after interspecies transmission and to determine the amino acid substitutions responsible for these alterations, we studied the HAs of the initial isolates from the human pandemics of 1957 (H2N2) and 1968 (H3N2), the European swine epizootic of 1979 (H1N1), and the seal epizootic of 1992 (H3N3), all of which were caused by the introduction of avian virus HAs into these species. The viruses were assayed for their ability to bind the synthetic sialylglycopolymers 3'SL-PAA and 6'SLN-PAA, which contained, respectively, 3'-sialyllactose (the receptor determinant preferentially recognized by avian influenza viruses) and 6'-sialyl(N-acetyllactosamine) (the receptor determinant for human viruses). Avian and seal viruses bound 6'SLN-PAA very weakly, whereas the earliest available human and swine epidemic viruses bound this polymer with a higher affinity. For the H2 and H3 strains, a single mutation, 226Q-->L, increased binding to 6'SLN-PAA, while among H1 swine viruses, the 190E-->D and 225G-->E mutations in the HA appeared important for the increased affinity of the viruses for 6'SLN-PAA. Amino acid substitutions at positions 190 and 225 with respect to the avian virus consensus sequence are also present in H1 human viruses, including those that circulated in 1918, suggesting that substitutions at these positions are important for the generation of H1 human pandemic strains. These results show that the receptor-binding specificity of the HA is altered early after the transmission of an avian virus to humans and pigs and, therefore, may be a prerequisite for the highly effective replication and spread which characterize epidemic strains.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Structural basis for human coronavirus attachment to sialic acid receptors

            Coronaviruses cause respiratory tract infections in humans and outbreaks of deadly pneumonia worldwide. Infections are initiated by the transmembrane spike (S) glycoprotein, which binds to host receptors and fuses the viral and cellular membranes. To understand the molecular basis of coronavirus attachment to oligosaccharide receptors, we determined cryo-EM structures of coronavirus OC43 S glycoprotein trimer in isolation and in complex with a 9-O-acetylated sialic acid. We demonstrate that the ligand binds with fast kinetics to a surface-exposed groove and interactions at the identified site are essential for S-mediated viral entry into host cells, but free monosaccharide did not trigger fusogenic conformational changes. The receptor-interacting site is conserved in all coronavirus S glycoproteins that engage 9-O-acetyl-sialogycans, with an architecture similar to the ligand-binding pockets of coronavirus hemagglutinin esterases and influenza virus C/D hemagglutinin-esterase-fusion glycoproteins. Our results demonstrate these viruses evolved similar strategies to engage sialoglycans at the surface of target cells.
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Role of receptor binding specificity in influenza A virus transmission and pathogenesis.

              The recent emergence of a novel avian A/H7N9 influenza virus in poultry and humans in China, as well as laboratory studies on adaptation and transmission of avian A/H5N1 influenza viruses, has shed new light on influenza virus adaptation to mammals. One of the biological traits required for animal influenza viruses to cross the species barrier that received considerable attention in animal model studies, in vitro assays, and structural analyses is receptor binding specificity. Sialylated glycans present on the apical surface of host cells can function as receptors for the influenza virus hemagglutinin (HA) protein. Avian and human influenza viruses typically have a different sialic acid (SA)-binding preference and only few amino acid changes in the HA protein can cause a switch from avian to human receptor specificity. Recent experiments using glycan arrays, virus histochemistry, animal models, and structural analyses of HA have added a wealth of knowledge on receptor binding specificity. Here, we review recent data on the interaction between influenza virus HA and SA receptors of the host, and the impact on virus host range, pathogenesis, and transmission. Remaining challenges and future research priorities are also discussed.
                Bookmark

                Author and article information

                Contributors
                Journal
                Glycobiology
                Glycobiology
                glycob
                Glycobiology
                Oxford University Press
                0959-6658
                1460-2423
                September 2022
                01 June 2022
                01 June 2022
                : 32
                : 9
                : 791-802
                Affiliations
                Division of Pathology , Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University , Yalelaan 1, 3584 CL Utrecht, The Netherlands
                Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University , Universiteitsweg 99, 3584 CG Utrecht, The Netherlands
                Division of Pathology , Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University , Yalelaan 1, 3584 CL Utrecht, The Netherlands
                Division of Pathology , Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University , Yalelaan 1, 3584 CL Utrecht, The Netherlands
                Dutch Wildlife Health Centre , Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University , Yalelaan 1, 3584 CL Utrecht, The Netherlands
                Division of Pathology , Department of Biomolecular Health Sciences, Faculty of Veterinary Medicine, Utrecht University , Yalelaan 1, 3584 CL Utrecht, The Netherlands
                Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, Utrecht University , Universiteitsweg 99, 3584 CG Utrecht, The Netherlands
                Author notes
                Corresponding author: Email: r.vries@ 123456uu.nl
                Author information
                https://orcid.org/0000-0002-1586-4464
                Article
                cwac033
                10.1093/glycob/cwac033
                9387512
                35648131
                bd64b1c3-b1de-4bc2-a473-b62327d810bc
                © The Author(s) 2022. Published by Oxford University Press.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 18 February 2022
                : 20 May 2022
                : 20 May 2022
                : 02 July 2022
                Page count
                Pages: 12
                Funding
                Funded by: European Commission, DOI 10.13039/501100000780;
                Award ID: 802780
                Funded by: Beijerinck Premium of the Royal Dutch Academy of Sciences;
                Categories
                Original Article
                AcademicSubjects/SCI01000

                Biochemistry
                host tropism,influenza a,sialic acid,tissue microarray,wildlife
                Biochemistry
                host tropism, influenza a, sialic acid, tissue microarray, wildlife

                Comments

                Comment on this article