About: De-O-Acetylation of mucin-derived sialic acids by recombinant NanS-p esterases of Escherichia coli O157:H7 strain EDL933

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About: De-O-Acetylation of mucin-derived sialic acids by recombinant NanS-p esterases of Escherichia coli O157:H7 strain EDL933 Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	De-O-Acetylation of mucin-derived sialic acids by recombinant NanS-p esterases of Escherichia coli O157:H7 strain EDL933
Creator	Feuerbaum, S Müthing, J Pohlentz, G Saile, N Schmidt, H
Source	Elsevier; Medline; PMC
abstract	Enterohemorrhagic Escherichia coli (EHEC) O157:H7 strain EDL933 encodes the single chromosomal 9-O-acetylesterase NanS, and several copies of prophage-encoded 9-O-acetylesterases (NanS-p). These enzymes have recently been shown to cleave 5-N-acetyl-9-O-acetyl neuraminic acid (Neu5,9Ac(2)) to yield de-O-acetylated Neu5Ac, the latter of which may serve as a carbon and/or nitrogen source. In the current study, we investigated the NanS- and NanS-p-mediated digestion of synthetic O-acetylated neuraminic acids and bovine submaxillary glands mucin (BSM)-derived O-acetylneuraminic acids by high-performance thin-layer chromatography (HPTLC) and nano electrospray ionization mass spectrometry (nanoESI MS). Initial HPTLC analyses showed the expected activity of NanS and NanS-p variants for Neu5,9Ac(2). However, all tested enzymes were unable to de-O-acetylate 5-N-acetyl-4-O-acetylneuraminic acid (Neu5,4 Ac(2)) in our test system. The nanoESI MS analysis of neuraminic acids after treatment of BSM with NanS-p gave evidence that NanS-p variants of EHEC O157:H7 strain EDL933 cleave off O-acetyl groups from mono-, di-, and tri-O-acetylated Neu5Ac and N-glycolylneuraminic acid (Neu5Gc), regardless of the carbon positions C7, C8 or C9 of the acetate esters. This enzyme activity leads to neuraminidase-accessible Neu5Ac and Neu5Gc on mucin glycans. Moreover, we could demonstrate by HPTLC analyses that recombinant Bacteroides thetaiotaomicron sialidase (BTSA-His) was able to cleave Neu5Ac and Neu5,9Ac(2) from BSM and that the combination of BTSA-His with both NanS-His and NanS-p-His derivatives enhanced the release of de-O-acetylated core Neu5Ac and Neu5Gc from mammalian mucin O-glycans. Growth experiments with EHEC wildtype strain EDL933, its nanS and nanS/nanS-p1a-p7 mutant and exogenous BTSA-His in BSM demonstrated that the presence of BTSA-His enhanced growth of EDL933 and the nanS deletion mutant but not the nanS/nanS-p1a-p7 mutant. Thus, we hypothesize that the expression of sialic acid O-acetylesterases with a broad specificity could be an advantage in competition with the gut microbiota for nutrients and facilitate EHEC colonization in the human large intestine.
has issue date	2018-10-09(xsd:dateTime)
bibo:doi	10.1016/j.ijmm.2018.10.001
bibo:pmid	30340996
has license	no-cc
sha1sum (hex)	1e0daac9575e2b1ba7e46c9ced5117b7fe639a1e
schema:url	https://doi.org/10.1016/j.ijmm.2018.10.001
resource representing a document's title	De-O-Acetylation of mucin-derived sialic acids by recombinant NanS-p esterases of Escherichia coli O157:H7 strain EDL933
has PubMed Central identifier	PMC7106450
has PubMed identifier	30340996
schema:publication	Int J Med Microbiol
resource representing a document's body	covid:1e0daac9575e2b1ba7e46c9ced5117b7fe639a1e#body_text
is schema:about of	named entity 'RECENTLY' named entity 'THESE' named entity 'CHROMOSOMAL' named entity 'NEU5AC' named entity 'SINGLE' named entity 'STRAIN' covid:arg/1e0daac9575e2b1ba7e46c9ced5117b7fe639a1e named entity 'TO CLEAVE' named entity 'ESCHERICHIA COLI O157' named entity 'DERIVED' named entity 'MUCIN' named entity 'O-ACETYLATION' named entity 'ESTERASES' named entity 'COPIES' named entity 'YIELD' named entity 'CARBON' named entity 'NANS' named entity 'NANS' named entity 'SIALIC ACIDS' named entity 'SERVE' named entity 'ENCODED' named entity 'RECOMBINANT' named entity 'ACETYLATED' named entity 'ENTEROHEMORRHAGIC ESCHERICHIA COLI' named entity 'ACETYLESTERASE' named entity 'O157' named entity 'STRAIN' named entity 'ENZYMES' named entity 'N-ACETYL' named entity 'ACETYL' named entity 'NEURAMINIC ACID' named entity 'NITROGEN SOURCE' named entity 'HAVE' named entity 'PROPHAGE' named entity 'chromosomal' named entity 'Enterohemorrhagic' named entity 'O157:H7' named entity 'acetyl' named entity 'nitrogen' named entity 'acetylesterase' named entity 'supernatants' named entity '37°C' named entity 'locus of enterocyte effacement' named entity 'mucus' named entity 'commensal bacteria' named entity 'substrates' named entity 'EHEC' named entity 'Neu5Gc' named entity 'Neu5Gc' named entity 'EHEC' named entity 'Neu5Ac' named entity 'UV light' named entity 'Neu5Ac' named entity 'acetyl group' named entity 'deacetylate' named entity 'acetylated' named entity 'hemorrhagic colitis' named entity 'esterases' named entity 'mammals' named entity 'mouse hepatitis virus' named entity 'mucus layer' named entity 'primers' named entity 'OAc' named entity 'negative control' named entity 'infection' named entity 'genetic background' named entity 'Neu5Gc' named entity 'HPTLC' named entity 'sialic acids' named entity 'recombinant' named entity 'sialidases' named entity 'sialic acids' named entity 'EHEC' named entity 'acetylated' named entity 'sialic acids' named entity 'carbon' named entity 'N-acetylneuraminic acid'

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