2004
DOI: 10.1074/jbc.m404965200
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Sialic Acid Recognition by Vibrio cholerae Neuraminidase

Abstract: Vibrio cholerae neuraminidase (VCNA) plays a significant role in the pathogenesis of cholera by removing sialic acid from higher order gangliosides to unmask GM1, the receptor for cholera toxin. We previously showed that the structure of VCNA is composed of a central ␤-propeller catalytic domain flanked by two lectin-like domains; however the nature of the carbohydrates recognized by these lectin domains has remained unknown. We present here structures of the enzyme in complex with two substrates, ␣-2,3-sialyl… Show more

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Cited by 137 publications
(137 citation statements)
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“…Recombinant Vibrio cholerae sialidase was expressed in Escherichia coli at high yield (>500 U/L culture) and was purified chromatographically to very high purity (>100 U/mg protein) (21). Sialidase was highly stable as formulated for intrathecal delivery; analysis of sialidase activity recovered from implanted catheters after 12 d in vivo revealed retention of 90 ± 9% (mean ± SEM) of enzyme activity.…”
Section: Resultsmentioning
confidence: 99%
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“…Recombinant Vibrio cholerae sialidase was expressed in Escherichia coli at high yield (>500 U/L culture) and was purified chromatographically to very high purity (>100 U/mg protein) (21). Sialidase was highly stable as formulated for intrathecal delivery; analysis of sialidase activity recovered from implanted catheters after 12 d in vivo revealed retention of 90 ± 9% (mean ± SEM) of enzyme activity.…”
Section: Resultsmentioning
confidence: 99%
“…The enzyme used in these studies, V. cholerae sialidase overproduced in E. coli (21,33), has advantages as a potential biological drug. It is produced at high concentration (>500 U/L) in bacterial culture, is readily purified, and is remarkably stable, with little loss of activity even after 12 d in vivo.…”
Section: Discussionmentioning
confidence: 99%
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“…NanH is a large neuraminidase (83 kDa), a threedomain protein consisting of two lectin wings and a central active neuraminidase domain, formed by six β-sheets arranged as in the blades of a propeller (β-propeller, Crennel et al 1994, Moustafa et al 2004). In studies with crystals of the classical strain O395 neuraminidase, some amino acids were proposed to be relevant for activity (Crennel et al 1994), and all of these are conserved in the Amazonia strain.…”
Section: Discussionmentioning
confidence: 99%
“…Thirteen of these are in the second lectin wing of the neuraminidase, the most variable region of the protein for the Amazonia strain. The first lectin wing is known to bind sialic acid, but the ligand for the second wing is unknown (Moustafa et al 2004). The first wing of the Amazonia NanH presents only two substitutions, one of these a conservative substitution in one of the 15 β-strands of the domain, and the other in a loop region.…”
Section: Discussionmentioning
confidence: 99%