Dataset Information

Both ?2,3- and ?2,6-linked sialic acids on O-linked glycoproteins act as functional receptors for porcine Sapovirus.

ABSTRACT: Sapovirus, a member of the Caliciviridae 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 Sapovirus 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 Vibrio cholerae neuraminidase (NA), suggesting a role for ?2,3-linked, ?2,6-linked or ?2,8-linked sialic acid in virus attachment. However, viral attachment and infection were only partially inhibited by treatment of cells with sialidase S (SS) or Maackia amurensis lectin (MAL), both specific for ?2,3-linked sialic acid, or Sambucus nigra lectin (SNL), specific for ?2,6-linked sialic acid. These results indicated that PSaV recognizes both ?2,3- and ?2,6-linked sialic acids for viral attachment and infection. Treatment of cells with proteases or with benzyl 4-O-?-D-galactopyranosyl-?-D-glucopyranoside (benzylGalNAc), which inhibits O-linked glycosylation, also reduced virus binding and infection, whereas inhibition of glycolipd synthesis or N-linked glycosylation had no such effect on virus binding or infection. These data suggest PSaV binds to cellular receptors that consist of ?2,3- and ?2,6-linked sialic acids on glycoproteins attached via O-linked glycosylation.

SUBMITTER: Kim DS

PROVIDER: S-EPMC4047124 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Both α2,3- and α2,6-linked sialic acids on O-linked glycoproteins act as functional receptors for porcine Sapovirus.

Kim Deok-Song DS Hosmillo Myra M Alfajaro Mia Madel MM Kim Ji-Yun JY Park Jun-Gyu JG Son Kyu-Yeol KY Ryu Eun-Hye EH Sorgeloos Frederic F Kwon Hyung-Jun HJ Park Su-Jin SJ Lee Woo Song WS Cho Duck D Kwon Joseph J Choi Jong-Soon JS Kang Mun-Il MI Kang Mun-Il MI Goodfellow Ian I Cho Kyoung-Oh KO

PLoS pathogens 20140605 6

Sapovirus, a member of the Caliciviridae 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 Sapovirus 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 bioch ...[more]

PMID: 24901849

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Dataset Information

Both ?2,3- and ?2,6-linked sialic acids on O-linked glycoproteins act as functional receptors for porcine Sapovirus.

Publications

Both α2,3- and α2,6-linked sialic acids on O-linked glycoproteins act as functional receptors for porcine Sapovirus.

Similar Datasets

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