Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose
The presence of galactofuranose in the oligosaccharides from mucins of Trypanosoma cruzi does not impair their acceptor properties. The oligosaccharides inhibit sialylation of N-acetyllactosamine with IC 50 values between 0.6 and 4 mM. A representative reaction is shown: The mucin-like glycoproteins...
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| Veröffentlicht in: | Bioorganic & medicinal chemistry 2007-04, Vol.15 (7), p.2611-2616 |
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| creator | Agustí, Rosalía Giorgi, M. Eugenia Mendoza, Verónica M. Gallo-Rodriguez, Carola de Lederkremer, Rosa M. |
| description | The presence of galactofuranose in the oligosaccharides from mucins of
Trypanosoma cruzi does not impair their acceptor properties. The oligosaccharides inhibit sialylation of
N-acetyllactosamine with IC
50 values between 0.6 and 4
mM. A representative reaction is shown:
The mucin-like glycoproteins of
Trypanosoma cruzi have novel O-linked oligosaccharides that are acceptors of sialic acid in the
trans-sialidase (TcTS) reaction. The transference of sialic acid from host glycoconjugates to the mucins is involved in infection and pathogenesis. The O-linked chains may contain galactofuranose in addition to the acceptor galactopyranose units. Thus far, the galactofuranose form was found in the mucins of strains belonging to the less infective lineage. The acceptor properties of the chemically synthesized oligosaccharides were now studied in order to correlate their structure with the ability to act as substrates. Recombinant TcTS and sialyllactose as donor were used. The reactions were followed by HPAEC-PAD. The
K
m values were calculated for the free sugars, the sugar alditols and the benzyl glycosides. All the compounds showed to be good acceptors of sialic acid. Thus, the introduction of galactofuranose in the mucins of the strains of lineage 1 would not be responsible for the diminished virulence of the strains. The oligosaccharides and derivatives inhibited the transfer of sialic acid to the substrate
N-acetyllactosamine with IC
50 values between 0.6 and 4
mM. |
| doi_str_mv | 10.1016/j.bmc.2007.01.045 |
| format | Article |
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Trypanosoma cruzi does not impair their acceptor properties. The oligosaccharides inhibit sialylation of
N-acetyllactosamine with IC
50 values between 0.6 and 4
mM. A representative reaction is shown:
The mucin-like glycoproteins of
Trypanosoma cruzi have novel O-linked oligosaccharides that are acceptors of sialic acid in the
trans-sialidase (TcTS) reaction. The transference of sialic acid from host glycoconjugates to the mucins is involved in infection and pathogenesis. The O-linked chains may contain galactofuranose in addition to the acceptor galactopyranose units. Thus far, the galactofuranose form was found in the mucins of strains belonging to the less infective lineage. The acceptor properties of the chemically synthesized oligosaccharides were now studied in order to correlate their structure with the ability to act as substrates. Recombinant TcTS and sialyllactose as donor were used. The reactions were followed by HPAEC-PAD. The
K
m values were calculated for the free sugars, the sugar alditols and the benzyl glycosides. All the compounds showed to be good acceptors of sialic acid. Thus, the introduction of galactofuranose in the mucins of the strains of lineage 1 would not be responsible for the diminished virulence of the strains. The oligosaccharides and derivatives inhibited the transfer of sialic acid to the substrate
N-acetyllactosamine with IC
50 values between 0.6 and 4
mM.</description><identifier>ISSN: 0968-0896</identifier><identifier>EISSN: 1464-3391</identifier><identifier>DOI: 10.1016/j.bmc.2007.01.045</identifier><identifier>PMID: 17292612</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Amino Sugars - chemistry ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Carbohydrate Sequence ; Escherichia coli - metabolism ; Fundamental and applied biological sciences. Psychology ; Galactofuranose ; Galactose - chemistry ; Galactose - isolation & purification ; Glycoproteins ; HPAEC-PAD ; Kinetics ; Molecular Sequence Data ; Mucins ; Mucins - chemistry ; Neuraminidase - antagonists & inhibitors ; Neuraminidase - metabolism ; Oligosaccharides - chemical synthesis ; Oligosaccharides - pharmacology ; Proteins ; Recombinant Proteins - chemistry ; Sialic Acids - metabolism ; trans-Sialidase ; Trypanosoma cruzi ; Trypanosoma cruzi - chemistry</subject><ispartof>Bioorganic & medicinal chemistry, 2007-04, Vol.15 (7), p.2611-2616</ispartof><rights>2007 Elsevier Ltd</rights><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-6b3def63ac854d70b21c918bfcb0cbe30e4b169f4189a765f78b8a62bbb69bf63</citedby><cites>FETCH-LOGICAL-c381t-6b3def63ac854d70b21c918bfcb0cbe30e4b169f4189a765f78b8a62bbb69bf63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0968089607000739$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18615857$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17292612$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Agustí, Rosalía</creatorcontrib><creatorcontrib>Giorgi, M. Eugenia</creatorcontrib><creatorcontrib>Mendoza, Verónica M.</creatorcontrib><creatorcontrib>Gallo-Rodriguez, Carola</creatorcontrib><creatorcontrib>de Lederkremer, Rosa M.</creatorcontrib><title>Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose</title><title>Bioorganic & medicinal chemistry</title><addtitle>Bioorg Med Chem</addtitle><description>The presence of galactofuranose in the oligosaccharides from mucins of
Trypanosoma cruzi does not impair their acceptor properties. The oligosaccharides inhibit sialylation of
N-acetyllactosamine with IC
50 values between 0.6 and 4
mM. A representative reaction is shown:
The mucin-like glycoproteins of
Trypanosoma cruzi have novel O-linked oligosaccharides that are acceptors of sialic acid in the
trans-sialidase (TcTS) reaction. The transference of sialic acid from host glycoconjugates to the mucins is involved in infection and pathogenesis. The O-linked chains may contain galactofuranose in addition to the acceptor galactopyranose units. Thus far, the galactofuranose form was found in the mucins of strains belonging to the less infective lineage. The acceptor properties of the chemically synthesized oligosaccharides were now studied in order to correlate their structure with the ability to act as substrates. Recombinant TcTS and sialyllactose as donor were used. The reactions were followed by HPAEC-PAD. The
K
m values were calculated for the free sugars, the sugar alditols and the benzyl glycosides. All the compounds showed to be good acceptors of sialic acid. Thus, the introduction of galactofuranose in the mucins of the strains of lineage 1 would not be responsible for the diminished virulence of the strains. The oligosaccharides and derivatives inhibited the transfer of sialic acid to the substrate
N-acetyllactosamine with IC
50 values between 0.6 and 4
mM.</description><subject>Amino Sugars - chemistry</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carbohydrate Sequence</subject><subject>Escherichia coli - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Galactofuranose</subject><subject>Galactose - chemistry</subject><subject>Galactose - isolation & purification</subject><subject>Glycoproteins</subject><subject>HPAEC-PAD</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Mucins</subject><subject>Mucins - chemistry</subject><subject>Neuraminidase - antagonists & inhibitors</subject><subject>Neuraminidase - metabolism</subject><subject>Oligosaccharides - chemical synthesis</subject><subject>Oligosaccharides - pharmacology</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Sialic Acids - metabolism</subject><subject>trans-Sialidase</subject><subject>Trypanosoma cruzi</subject><subject>Trypanosoma cruzi - chemistry</subject><issn>0968-0896</issn><issn>1464-3391</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU2O1DAQhSMEYpqBA7BB3sAuwc6P44gVagEz0khshrVVdpzuaiV2sJ2RwvW4GG4l0uxYlfT81XNVvSx7z2jBKOOfL4WadFFS2haUFbRuXmQHVvM6r6qOvcwOtOMip6LjN9mbEC6U0rLu2OvshrVlV3JWHrK_RzfN4CHikyGpmEDcQALCuI5JdJaolXij3aTQgo0kerAhvwLYQzAEbE_QnlFhdJ7M3s3GR9xtVhvPJqImbsSTC6D1GTz26XXwbiKPfp3BuuAmINovf5BMi8Zkr52NgBbtiZxgBB3dsPgruf23a_O6aW-zVwOMwbzb62326_u3x-Nd_vDzx_3x60OuK8FizlXVm4FXoEVT9y1VJdMdE2rQimplKmpqxXg31Ex00PJmaIUSwEulFO9UarzNPm2-acvfiwlRThi0GUewxi1BtjTdVPAugWwDtXcheDPI2eMEfpWMymty8iJTcvKanKRMpuRSz4fdfFGT6Z879qgS8HEHIGgYh7S7xvDMCc4a0bSJ-7JxJp3iCY2XQaOx2vSYcoyyd_ifMf4BdSy-dA</recordid><startdate>20070401</startdate><enddate>20070401</enddate><creator>Agustí, Rosalía</creator><creator>Giorgi, M. Eugenia</creator><creator>Mendoza, Verónica M.</creator><creator>Gallo-Rodriguez, Carola</creator><creator>de Lederkremer, Rosa M.</creator><general>Elsevier Ltd</general><general>Elsevier Science</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20070401</creationdate><title>Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose</title><author>Agustí, Rosalía ; Giorgi, M. Eugenia ; Mendoza, Verónica M. ; Gallo-Rodriguez, Carola ; de Lederkremer, Rosa M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-6b3def63ac854d70b21c918bfcb0cbe30e4b169f4189a765f78b8a62bbb69bf63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Sugars - chemistry</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carbohydrate Sequence</topic><topic>Escherichia coli - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Galactofuranose</topic><topic>Galactose - chemistry</topic><topic>Galactose - isolation & purification</topic><topic>Glycoproteins</topic><topic>HPAEC-PAD</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Mucins</topic><topic>Mucins - chemistry</topic><topic>Neuraminidase - antagonists & inhibitors</topic><topic>Neuraminidase - metabolism</topic><topic>Oligosaccharides - chemical synthesis</topic><topic>Oligosaccharides - pharmacology</topic><topic>Proteins</topic><topic>Recombinant Proteins - chemistry</topic><topic>Sialic Acids - metabolism</topic><topic>trans-Sialidase</topic><topic>Trypanosoma cruzi</topic><topic>Trypanosoma cruzi - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Agustí, Rosalía</creatorcontrib><creatorcontrib>Giorgi, M. Eugenia</creatorcontrib><creatorcontrib>Mendoza, Verónica M.</creatorcontrib><creatorcontrib>Gallo-Rodriguez, Carola</creatorcontrib><creatorcontrib>de Lederkremer, Rosa M.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioorganic & medicinal chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Agustí, Rosalía</au><au>Giorgi, M. Eugenia</au><au>Mendoza, Verónica M.</au><au>Gallo-Rodriguez, Carola</au><au>de Lederkremer, Rosa M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose</atitle><jtitle>Bioorganic & medicinal chemistry</jtitle><addtitle>Bioorg Med Chem</addtitle><date>2007-04-01</date><risdate>2007</risdate><volume>15</volume><issue>7</issue><spage>2611</spage><epage>2616</epage><pages>2611-2616</pages><issn>0968-0896</issn><eissn>1464-3391</eissn><abstract>The presence of galactofuranose in the oligosaccharides from mucins of
Trypanosoma cruzi does not impair their acceptor properties. The oligosaccharides inhibit sialylation of
N-acetyllactosamine with IC
50 values between 0.6 and 4
mM. A representative reaction is shown:
The mucin-like glycoproteins of
Trypanosoma cruzi have novel O-linked oligosaccharides that are acceptors of sialic acid in the
trans-sialidase (TcTS) reaction. The transference of sialic acid from host glycoconjugates to the mucins is involved in infection and pathogenesis. The O-linked chains may contain galactofuranose in addition to the acceptor galactopyranose units. Thus far, the galactofuranose form was found in the mucins of strains belonging to the less infective lineage. The acceptor properties of the chemically synthesized oligosaccharides were now studied in order to correlate their structure with the ability to act as substrates. Recombinant TcTS and sialyllactose as donor were used. The reactions were followed by HPAEC-PAD. The
K
m values were calculated for the free sugars, the sugar alditols and the benzyl glycosides. All the compounds showed to be good acceptors of sialic acid. Thus, the introduction of galactofuranose in the mucins of the strains of lineage 1 would not be responsible for the diminished virulence of the strains. The oligosaccharides and derivatives inhibited the transfer of sialic acid to the substrate
N-acetyllactosamine with IC
50 values between 0.6 and 4
mM.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>17292612</pmid><doi>10.1016/j.bmc.2007.01.045</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0968-0896 |
| ispartof | Bioorganic & medicinal chemistry, 2007-04, Vol.15 (7), p.2611-2616 |
| issn | 0968-0896 1464-3391 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Sugars - chemistry Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Carbohydrate Sequence Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Galactofuranose Galactose - chemistry Galactose - isolation & purification Glycoproteins HPAEC-PAD Kinetics Molecular Sequence Data Mucins Mucins - chemistry Neuraminidase - antagonists & inhibitors Neuraminidase - metabolism Oligosaccharides - chemical synthesis Oligosaccharides - pharmacology Proteins Recombinant Proteins - chemistry Sialic Acids - metabolism trans-Sialidase Trypanosoma cruzi Trypanosoma cruzi - chemistry |
| title | Comparative rates of sialylation by recombinant trans-sialidase and inhibitor properties of synthetic oligosaccharides from Trypanosoma cruzi mucins-containing galactofuranose and galactopyranose |
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