SA11 rotavirus is specifically inhibited by an acetylated sialic acid

Rodney E. Willoughby; Robert H. Yolken

doi:10.1093/infdis/161.1.116

SA11 rotavirus is specifically inhibited by an acetylated sialic acid

Rodney E. Willoughby, Robert H. Yolken

School of Medicine

Research output: Contribution to journal › Article › peer-review

37 Scopus citations

Abstract

Bovine salivary mucin (BSM) inhibits rotavirus replication in vitro and in vivo. The inhibitory effect of BSM in vitro is abolished by Arthrobacter ureafaciens neuraminidase but not by Clostridia perfringens neuraminidase; it is abolished by mild base deacetylation but not by influenza C acetylesterase. The data suggest that SA11 rotavirus binds to a specific sialic acid structure on BSM different from the sialic acids recognized by other viruses.

Original language	English (US)
Pages (from-to)	116-119
Number of pages	4
Journal	Journal of Infectious Diseases
Volume	161
Issue number	1
DOIs	https://doi.org/10.1093/infdis/161.1.116
State	Published - Jan 1990

ASJC Scopus subject areas

General Medicine

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10.1093/infdis/161.1.116

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abstract = "Bovine salivary mucin (BSM) inhibits rotavirus replication in vitro and in vivo. The inhibitory effect of BSM in vitro is abolished by Arthrobacter ureafaciens neuraminidase but not by Clostridia perfringens neuraminidase; it is abolished by mild base deacetylation but not by influenza C acetylesterase. The data suggest that SA11 rotavirus binds to a specific sialic acid structure on BSM different from the sialic acids recognized by other viruses.",

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AB - Bovine salivary mucin (BSM) inhibits rotavirus replication in vitro and in vivo. The inhibitory effect of BSM in vitro is abolished by Arthrobacter ureafaciens neuraminidase but not by Clostridia perfringens neuraminidase; it is abolished by mild base deacetylation but not by influenza C acetylesterase. The data suggest that SA11 rotavirus binds to a specific sialic acid structure on BSM different from the sialic acids recognized by other viruses.

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SA11 rotavirus is specifically inhibited by an acetylated sialic acid

Abstract

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