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RISS 인기검색어
- 검색키워드
- 저자 : Frederic Sorgeloos (검색결과 2 건)
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Kim, Deok-Song,Hosmillo, Myra,Alfajaro, Mia Madel,Kim, Ji-Yun,Park, Jun-Gyu,Son, Kyu-Yeol,Ryu, Eun-Hye,Sorgeloos, Frederic,Kwon, Hyung-Jun,Park, Su-Jin,Lee, Woo Song,Cho, Duck,Kwon, Joseph,Choi, Jong- Public Library of Science 2014 PLoS pathogens Vol.10 No.6
<▼1><P>Sapovirus, a member of the <I>Caliciviridae</I> family, is an important cause of acute gastroenteritis in humans and pigs. Currently, the porcine sapovirus (PSaV) Cowden strain remains the only cultivable member of the <I>Sapovirus</I> genus. While some caliciviruses are known to utilize carbohydrate receptors for entry and infection, a functional receptor for sapovirus is unknown. To characterize the functional receptor of the Cowden strain of PSaV, we undertook a comprehensive series of protein-ligand biochemical assays in mock and PSaV-infected cell culture and/or piglet intestinal tissue sections. PSaV revealed neither hemagglutination activity with red blood cells from any species nor binding activity to synthetic histo-blood group antigens, indicating that PSaV does not use histo-blood group antigens as receptors. Attachment and infection of PSaV were markedly blocked by sialic acid and <I>Vibrio cholerae</I> neuraminidase (NA), suggesting a role for α2,3-linked, α2,6-linked or α2,8-linked sialic acid in virus attachment. However, viral attachment and infection were only partially inhibited by treatment of cells with sialidase S (SS) or <I>Maackia amurensis</I> lectin (MAL), both specific for α2,3-linked sialic acid, or <I>Sambucus nigra</I> lectin (SNL), specific for α2,6-linked sialic acid. These results indicated that PSaV recognizes both α2,3- and α2,6-linked sialic acids for viral attachment and infection. Treatment of cells with proteases or with benzyl 4-O-β-D-galactopyranosyl-β-D-glucopyranoside (benzylGalNAc), which inhibits <I>O</I>-linked glycosylation, also reduced virus binding and infection, whereas inhibition of glycolipd synthesis or <I>N</I>-linked glycosylation had no such effect on virus binding or infection. These data suggest PSaV binds to cellular receptors that consist of α2,3- and α2,6-linked sialic acids on glycoproteins attached via <I>O</I>-linked glycosylation.</P></▼1><▼2><P><B>Author Summary</B></P><P>Although enteropathogenic sapoviruses and noroviruses are leading causes of acute gastroenteritis in both humans and animals, the study of viral pathogenesis and immunity of these ubiquitous pathogens has been hampered due to the lack of a fully permissive cell culture system. Porcine sapovirus Cowden strain provides a suitable system that can be used to identify the molecular mechanisms of viral pathogenesis. Previous studies have shown that carbohydrates and glycolipids play important roles in the attachment of members of the <I>Caliciviridae</I>; histo-blood group antigens (HBGAs) are used by <I>Norovirus</I> genogroups I to IV, as well as members of the <I>Lagovirus</I>, and <I>Recovirus</I> genera, whereas terminal sialic acid is recognized as a receptor for feline calicivirus and murine norovirus. To date, however, the role of carbohydrates in the life cycle of sapoviruses has remained largely unknown. We found that porcine sapovirus binds to susceptible host cells through both α2,3- and α2,6-linked terminal sialic acids which are attached to <I>O</I>-linked glycoproteins. These efforts, findings and insights will significantly contribute to a better understanding of the sapovirus life cycle.</P></▼2>
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