Glycosylation of the surface glycoproteins of influenza A virus is associated with several viral properties such as receptor binding and susceptibility to neuraminidase inhibitors. In this study, we evaluated the detailed structures of N-glycans derived from the same influenza virus strain A/Memphis/1/71 (H3N2) grown in different host cells, i.e., Madin-Darby canine kidney (MDCK) cells and embryonated eggs. Although both influenza virus isolates expressed neu- tral and sulfated oligosaccharides, their detailed profiles were significantly different. In contrast, N-glycosylation profiles of the influenza virus isolate from MDCK cells were highly homologous with those of desialylated N-glycans derived from its host cells. These data demonstrate that the glycosylation of influenza viruses is governed by their host cells.
{"title":"Comparative Analyses of N-Glycosylation Profiles of Influenza A Viruses Grown in Different Host Cells","authors":"H. Yagi, Shinya Watanabe, Takashi Suzuki, Tadanobu Takahashi, Yasuo Suzuki, Koichi Kato","doi":"10.2174/1875398101205010002","DOIUrl":"https://doi.org/10.2174/1875398101205010002","url":null,"abstract":"Glycosylation of the surface glycoproteins of influenza A virus is associated with several viral properties such as receptor binding and susceptibility to neuraminidase inhibitors. In this study, we evaluated the detailed structures of N-glycans derived from the same influenza virus strain A/Memphis/1/71 (H3N2) grown in different host cells, i.e., Madin-Darby canine kidney (MDCK) cells and embryonated eggs. Although both influenza virus isolates expressed neu- tral and sulfated oligosaccharides, their detailed profiles were significantly different. In contrast, N-glycosylation profiles of the influenza virus isolate from MDCK cells were highly homologous with those of desialylated N-glycans derived from its host cells. These data demonstrate that the glycosylation of influenza viruses is governed by their host cells.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"5 1","pages":"2-12"},"PeriodicalIF":0.0,"publicationDate":"2012-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68111208","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-05-04DOI: 10.2174/1875398101205010013
Kei-ichi Watanabe, K. Hidari, Takashi Suzuki
The protein structures of most mammalian sialyltransferases have yet to be elucidated. Practical and convenient protein expression systems for soluble and active sialyltransferases will facilitate elucidation of the protein structures and catalytic mechanisms of these enzymes. The present study was performed to establish an efficient expression system for human ST6Gal I (hST6Gal I). cDNA encoding a soluble form of hST6Gal I was introduced into the bacterial expression vector pCold I carrying the cold shock promoter that is inducible by low-temperature conditions. The resultant DNA en- codes the enzyme fused in frame with a maltose-binding protein (MBP) as a purification tag. This expression plasmid was introduced into the E. coli strain pGro7/BL21 harboring the molecular chaperones GroES and GroEL. Combined use of chaperone proteins and low-temperature cultivation during IPTG induction significantly improved the functional enzyme solubility in bacteria. The MBP-tagged hST6Gal I was efficiently purified by affinity chromatography using amylose- conjugated agarose.
大多数哺乳动物唾液基转移酶的蛋白质结构尚未被阐明。实用和方便的可溶性和活性唾液基转移酶的蛋白质表达系统将有助于阐明这些酶的蛋白质结构和催化机制。本研究旨在建立人类ST6Gal I (hST6Gal I)的高效表达体系，将编码hST6Gal I可溶性形式的cDNA导入细菌表达载体pCold I中，该载体携带低温诱导的冷休克启动子。所得到的DNA编码的酶融合在框架与麦芽糖结合蛋白(MBP)作为纯化标签。将该表达质粒导入含有GroES和GroEL分子伴侣的大肠杆菌菌株pGro7/BL21中。在IPTG诱导过程中，结合使用伴侣蛋白和低温培养，显著提高了功能酶在细菌中的溶解度。用直链糖偶联琼脂糖亲和层析纯化了mbp标记的hST6Gal I。
{"title":"Cold-shock Protein Expression System Facilitates the Solubility of Human ST6Gal I in Escherichia Coli","authors":"Kei-ichi Watanabe, K. Hidari, Takashi Suzuki","doi":"10.2174/1875398101205010013","DOIUrl":"https://doi.org/10.2174/1875398101205010013","url":null,"abstract":"The protein structures of most mammalian sialyltransferases have yet to be elucidated. Practical and convenient protein expression systems for soluble and active sialyltransferases will facilitate elucidation of the protein structures and catalytic mechanisms of these enzymes. The present study was performed to establish an efficient expression system for human ST6Gal I (hST6Gal I). cDNA encoding a soluble form of hST6Gal I was introduced into the bacterial expression vector pCold I carrying the cold shock promoter that is inducible by low-temperature conditions. The resultant DNA en- codes the enzyme fused in frame with a maltose-binding protein (MBP) as a purification tag. This expression plasmid was introduced into the E. coli strain pGro7/BL21 harboring the molecular chaperones GroES and GroEL. Combined use of chaperone proteins and low-temperature cultivation during IPTG induction significantly improved the functional enzyme solubility in bacteria. The MBP-tagged hST6Gal I was efficiently purified by affinity chromatography using amylose- conjugated agarose.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"5 1","pages":"13-18"},"PeriodicalIF":0.0,"publicationDate":"2012-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68110848","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-05-04DOI: 10.2174/1875398101205010041
N. Sriwilaijaroen, Sachiko Kondo, H. Yagi, H. Hiramatsu, S. Nakakita, Keita Yamada, Hiromi Ito, J. Hirabayashi, H. Narimatsu, Koichi Kato, Yasuo Suzuki
Glycans exhibit enormous structural diversity in nature and are of particular importance for self-cell survival and are often targeted by microbes. In this study, N-glycans (374.9 pmol/mg in dry delipidated weight) were enzymatical- ly released from bovine milk whey protein concentrate, and they were isolated and analyzed by a two-dimensional HPLC mapping technique and/or by MALDI-TOF mass spectrometry. A total of 39 identified N-glycans are bi- and tri-antennary sugar chains terminated with multiple mannose residues (Man-Man; molar ratio of 39.5%), N-acetyl-lactosamine (Lac- NAc; Gal1-4GlcNAc; molar ratio of 17.9), di-N-acetylated lactosamine (LacdiNAc; GalNAc1-4GlcNAc; molar ratio of 22.8), GlcNAc (molar ratio of 7.05), Neu5Ac2-6Gal1-4GlcNAc (molar ratio of 5.3), Neu5Ac2-6GalNAc1-4GlcNAc (molar ratio of 1.25), Neu5Gc2-6Gal1-4GlcNAc (molar ratio of 2.5), and Neu5Gc2-3Gal1-4GlcNAc (molar ratio of 0.25), in which some are fucosylated on the proximal core GlcNAc1-N-Asn. Terminal Neu5Ac2-3Gal/GalNAc and Neu5Gc2-3/2-6GalNAc were not detected in the bovine whey protein concentrate. Among the 39 glycans, GalNAcβ1- 4GlcNAcβ1-2Manα1-3(GalNAcβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβ- and Manα1-2Manα1-2Manα 1-3(Manα1-2Manα1-3(Manα1-2Manα1-6)Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβ- were the most abundant types found with molar ratios of 11.3 and 10, respectively. Elucidation of glycan molecular structures will lead to an understanding of their biological roles and functions. Whey contains a variety of glycans and is inexpensive, and it is thus considered to be source of glycans for array glycan libraries to be used for investigations of specific glycan-protein interactions, enabling not only analysis of biological roles of the glycan-binding proteins but also development of molecules affecting these in- teractions. Furthermore, these natural glycans may have therapeutic value in prevention and inhibition of infection of mi- crobes that recognize them.
{"title":"Bovine Milk Whey for Preparation of Natural N-glycans: Structural and Quantitative Analysis","authors":"N. Sriwilaijaroen, Sachiko Kondo, H. Yagi, H. Hiramatsu, S. Nakakita, Keita Yamada, Hiromi Ito, J. Hirabayashi, H. Narimatsu, Koichi Kato, Yasuo Suzuki","doi":"10.2174/1875398101205010041","DOIUrl":"https://doi.org/10.2174/1875398101205010041","url":null,"abstract":"Glycans exhibit enormous structural diversity in nature and are of particular importance for self-cell survival and are often targeted by microbes. In this study, N-glycans (374.9 pmol/mg in dry delipidated weight) were enzymatical- ly released from bovine milk whey protein concentrate, and they were isolated and analyzed by a two-dimensional HPLC mapping technique and/or by MALDI-TOF mass spectrometry. A total of 39 identified N-glycans are bi- and tri-antennary sugar chains terminated with multiple mannose residues (Man-Man; molar ratio of 39.5%), N-acetyl-lactosamine (Lac- NAc; Gal1-4GlcNAc; molar ratio of 17.9), di-N-acetylated lactosamine (LacdiNAc; GalNAc1-4GlcNAc; molar ratio of 22.8), GlcNAc (molar ratio of 7.05), Neu5Ac2-6Gal1-4GlcNAc (molar ratio of 5.3), Neu5Ac2-6GalNAc1-4GlcNAc (molar ratio of 1.25), Neu5Gc2-6Gal1-4GlcNAc (molar ratio of 2.5), and Neu5Gc2-3Gal1-4GlcNAc (molar ratio of 0.25), in which some are fucosylated on the proximal core GlcNAc1-N-Asn. Terminal Neu5Ac2-3Gal/GalNAc and Neu5Gc2-3/2-6GalNAc were not detected in the bovine whey protein concentrate. Among the 39 glycans, GalNAcβ1- 4GlcNAcβ1-2Manα1-3(GalNAcβ1-4GlcNAcβ1-2Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβ- and Manα1-2Manα1-2Manα 1-3(Manα1-2Manα1-3(Manα1-2Manα1-6)Manα1-6)Manβ1-4GlcNAcβ1-4GlcNAcβ- were the most abundant types found with molar ratios of 11.3 and 10, respectively. Elucidation of glycan molecular structures will lead to an understanding of their biological roles and functions. Whey contains a variety of glycans and is inexpensive, and it is thus considered to be source of glycans for array glycan libraries to be used for investigations of specific glycan-protein interactions, enabling not only analysis of biological roles of the glycan-binding proteins but also development of molecules affecting these in- teractions. Furthermore, these natural glycans may have therapeutic value in prevention and inhibition of infection of mi- crobes that recognize them.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"5 1","pages":"41-50"},"PeriodicalIF":0.0,"publicationDate":"2012-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68110915","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-05-04DOI: 10.2174/1875398101205010019
Betsy Yang, H. Chuang, Rong-Fu Chen
Sugar-lectin interactions play an important role in viral infections. Many viruses, such as human immunodefi- ciency virus (HIV), Ebola, dengue, cytomegalovirus, and hepatitis C, possess glycans that recognize C-type lectins, espe- cially CD209 (DC-SIGN), for infection. Other viruses possess lectins on their surfaces that recognize glycan epitopes on human epithelial cells for infection. Human and avian influenza viruses recognize different glycan epitopes, sialic acid- 2,6 galactose (SA-2,6Gal) and SA-2,3Gal, respectively, as their receptors, resulting in different host ranges for these two viruses. We and others have shown that sialogalactosides and fucosyllactoses are receptors for enterovirus 71 and no- rovirus infections, respectively; human milk oligosaccharides (HMOs) could block enterovirus 71 and norovirus infec- tions. Several lines of evidence also suggest that HMOs cannot only mimic viral receptors and block viral infections, but also raise immune responses through sugar/lectin (galactosides/galactins and sialylglycans/Siglecs) interactions and im- prove gut ecology by nurturing intestinal cells and/or intestinal microbiota. This review article summarizes how and why HMOs directly or indirectly protect humans from viral infections.
{"title":"Protection from Viral Infections by Human Milk Oligosaccharides: Direct Blockade and Indirect Modulation of Intestinal Ecology and Immune Reactions","authors":"Betsy Yang, H. Chuang, Rong-Fu Chen","doi":"10.2174/1875398101205010019","DOIUrl":"https://doi.org/10.2174/1875398101205010019","url":null,"abstract":"Sugar-lectin interactions play an important role in viral infections. Many viruses, such as human immunodefi- ciency virus (HIV), Ebola, dengue, cytomegalovirus, and hepatitis C, possess glycans that recognize C-type lectins, espe- cially CD209 (DC-SIGN), for infection. Other viruses possess lectins on their surfaces that recognize glycan epitopes on human epithelial cells for infection. Human and avian influenza viruses recognize different glycan epitopes, sialic acid- 2,6 galactose (SA-2,6Gal) and SA-2,3Gal, respectively, as their receptors, resulting in different host ranges for these two viruses. We and others have shown that sialogalactosides and fucosyllactoses are receptors for enterovirus 71 and no- rovirus infections, respectively; human milk oligosaccharides (HMOs) could block enterovirus 71 and norovirus infec- tions. Several lines of evidence also suggest that HMOs cannot only mimic viral receptors and block viral infections, but also raise immune responses through sugar/lectin (galactosides/galactins and sialylglycans/Siglecs) interactions and im- prove gut ecology by nurturing intestinal cells and/or intestinal microbiota. This review article summarizes how and why HMOs directly or indirectly protect humans from viral infections.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"5 1","pages":"19-25"},"PeriodicalIF":0.0,"publicationDate":"2012-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68110857","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-05-04DOI: 10.2174/1875398101205010026
Toshihiko Sawada
The present mini-review aims first at an introduction to two thermodynamic essentials of the binding between the influenza A virus hemagglutinin (HA) and the cell surface receptor sialoside, (1) the equilibrium 1:1 binding of the HA with the sialoside, (2) the polyvalent effect of the HA binding to the polyvalent sialoside. Second, the review introduces the fragment molecular orbital (FMO) studies of the HA-sialoside (1:1) complexes. The recent FMO method with the polarizable continuum model as one of the residue-based energy analysis method has revealed the role of key amino acid residue on the selective HA subtype H3 binding to the sialosides.
{"title":"Chemical Insight Into the Influenza A Virus Hemagglutinin Binding to the Sialoside Revealed by the Fragment Molecular Orbital Method","authors":"Toshihiko Sawada","doi":"10.2174/1875398101205010026","DOIUrl":"https://doi.org/10.2174/1875398101205010026","url":null,"abstract":"The present mini-review aims first at an introduction to two thermodynamic essentials of the binding between the influenza A virus hemagglutinin (HA) and the cell surface receptor sialoside, (1) the equilibrium 1:1 binding of the HA with the sialoside, (2) the polyvalent effect of the HA binding to the polyvalent sialoside. Second, the review introduces the fragment molecular orbital (FMO) studies of the HA-sialoside (1:1) complexes. The recent FMO method with the polarizable continuum model as one of the residue-based energy analysis method has revealed the role of key amino acid residue on the selective HA subtype H3 binding to the sialosides.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"5 1","pages":"26-30"},"PeriodicalIF":0.0,"publicationDate":"2012-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68110864","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2012-05-04DOI: 10.2174/1875398101205010031
K. Matsuoka, T. Koyama, Ken Hatano
This review shows introduction of glycoclusters using carbosilanes as core scaffolds, preparations of glyco- clusters and their excellent properties as well as functions. Since a dendrimer has unique advantages such as single mo- lecular weight, regularity of structure and easy control of shape and size, dendrimers are utilized in various research areas. Results of syntheses and biological evaluations of the carbosilane dendrimers having carbohydrate moieties for influenza viruses are presented.
{"title":"Glyco-silicon Functional Materials as Anti-influenza Virus Agents","authors":"K. Matsuoka, T. Koyama, Ken Hatano","doi":"10.2174/1875398101205010031","DOIUrl":"https://doi.org/10.2174/1875398101205010031","url":null,"abstract":"This review shows introduction of glycoclusters using carbosilanes as core scaffolds, preparations of glyco- clusters and their excellent properties as well as functions. Since a dendrimer has unique advantages such as single mo- lecular weight, regularity of structure and easy control of shape and size, dendrimers are utilized in various research areas. Results of syntheses and biological evaluations of the carbosilane dendrimers having carbohydrate moieties for influenza viruses are presented.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"5 1","pages":"31-40"},"PeriodicalIF":0.0,"publicationDate":"2012-05-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68110902","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2011-05-19DOI: 10.2174/1875398101104010001
S. Fedorov, L. Shubina, A. Kuzmich, S. Polonik
Glycosylated derivatives of physiologically active natural compound juglone and related 1,4- naphthoquinones are known as antifungal, immunomodulatory, and antitumor substances. However, their antileukemic properties and struc- ture-activity relationships have been studied insufficiently. Antileukemic effects and structure-activity relationships (SAR) of the 50 1,4- naphthoquinone derivatives were examined using HL-60 human promyelocytic leukemia cells and MTS method of the study of cell viability. As was shown, the substances inhibited viability of HL-60 cells at the wide range of concentrations. SAR study revealed the structure peculiarities which lead to increase or decrease of the antileu- kemic activity of the compounds studied. In conclusion, O- or S- glycosylated derivatives of juglone and related 1,4- naphthoquinones have potential for development of the new antileukemic agents and should be further investigated.
{"title":"Antileukemic Properties and Structure-Activity Relationships of O- and SGlycosylatedDerivatives of Juglone and Related 1,4-Naphthoquinones","authors":"S. Fedorov, L. Shubina, A. Kuzmich, S. Polonik","doi":"10.2174/1875398101104010001","DOIUrl":"https://doi.org/10.2174/1875398101104010001","url":null,"abstract":"Glycosylated derivatives of physiologically active natural compound juglone and related 1,4- naphthoquinones are known as antifungal, immunomodulatory, and antitumor substances. However, their antileukemic properties and struc- ture-activity relationships have been studied insufficiently. Antileukemic effects and structure-activity relationships (SAR) of the 50 1,4- naphthoquinone derivatives were examined using HL-60 human promyelocytic leukemia cells and MTS method of the study of cell viability. As was shown, the substances inhibited viability of HL-60 cells at the wide range of concentrations. SAR study revealed the structure peculiarities which lead to increase or decrease of the antileu- kemic activity of the compounds studied. In conclusion, O- or S- glycosylated derivatives of juglone and related 1,4- naphthoquinones have potential for development of the new antileukemic agents and should be further investigated.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"4 1","pages":"1-5"},"PeriodicalIF":0.0,"publicationDate":"2011-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68111198","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2009-08-19DOI: 10.2174/1875398100902010020
M. Semenova, O. Okunev, A. Gusakov, A. Sinitsyn
Four enzyme preparations produced by fungal species belonging to different genera (Aspergillus niger, Cory- nascus sp., Penicillium verruculosum, Trichoderma reesei) were used for synthesis of disaccharides by D-glucose (60% w/v) condensation catalyzed by -glucosidase. Effects of pH and temperature on the disaccharide synthesis were studied, and glycoside linkage patterns for enzymes from different sources were determined. The highest concentration of disac- charides (114 and 118 g/l) was achieved in the case of A. niger and Corynascus sp. enzymes after 48 h of the condensa- tion reaction carried out at 70 o C and optimal pH; the P. verruculosum sample slightly conceded them in the yield of products (96 g/l), while the T. reesei preparation displayed the lowest synthetic activity (35 g/l). Gentiobiose was pre- dominantly formed in the reaction catalyzed by the first three enzyme samples, while in the case of T. reesei laminaribiose was the main condensation product.
{"title":"Disaccharide Synthesis by Enzymatic Condensation of Glucose: Glycoside Linkage Patterns for Different Fungal Species","authors":"M. Semenova, O. Okunev, A. Gusakov, A. Sinitsyn","doi":"10.2174/1875398100902010020","DOIUrl":"https://doi.org/10.2174/1875398100902010020","url":null,"abstract":"Four enzyme preparations produced by fungal species belonging to different genera (Aspergillus niger, Cory- nascus sp., Penicillium verruculosum, Trichoderma reesei) were used for synthesis of disaccharides by D-glucose (60% w/v) condensation catalyzed by -glucosidase. Effects of pH and temperature on the disaccharide synthesis were studied, and glycoside linkage patterns for enzymes from different sources were determined. The highest concentration of disac- charides (114 and 118 g/l) was achieved in the case of A. niger and Corynascus sp. enzymes after 48 h of the condensa- tion reaction carried out at 70 o C and optimal pH; the P. verruculosum sample slightly conceded them in the yield of products (96 g/l), while the T. reesei preparation displayed the lowest synthetic activity (35 g/l). Gentiobiose was pre- dominantly formed in the reaction catalyzed by the first three enzyme samples, while in the case of T. reesei laminaribiose was the main condensation product.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"2 1","pages":"20-24"},"PeriodicalIF":0.0,"publicationDate":"2009-08-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68110808","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2009-08-13DOI: 10.2174/1875398100902010028
Sukanya Thongratsakul, T. Songserm, C. Poolkhet, Sachiko Kondo, H. Yagi, H. Hiramatsu, M. Tashiro, Yasuo Suzuki
Highly pathogenic and potentially pandemic H5N1 avian influenza A viruses have become endemic and are now residing in Asia, Europe, Africa, and the Middle East. H5N1 viruses have been shown to cross the species barrier and infect both dogs and cats. Domestic cats and dogs in Thailand, which were naturally infected with H5N1, exhibited severe pulmonary edema and peumonia in lung tissue as well as in other tissue dysfunctions. In order to understand the structure and quantity of influenza A receptor sialyl sugar chains in cats and dogs, especially in lung tissue, glycosylation profiles of N-glycans were determined from lung tissues of dogs and cats susceptible to H5N1 in Thailand by using multi- dimensional HPLC mapping combined with mass spectrometry. The results demonstrated different N-linked glycans com- position ratios between dogs and cats. There were a total of 30 kinds of N-linked glycans from cat lungs, which were comprised of 11 neutral, 13 mono-, 3 di-, and 3 tri-sialyl sugar chains, and 29 kinds from dog lungs, which were com- prised of 16 neutral, 11 mono- and 2 di-sialyl sugar chains. Cat lungs exhibited both 5-N-acetylneuraminic acid and 5-N- glycolylneuraminic acid sialic acid (Sia� 2-3Gal and Sia� 2-6Gal), but dog lungs contained only 5-N-acetylneuraminic (Sia� 2-3Gal and Sia� 2-6Gal) molecular species. The composition ratios of molar percentage of Sia� 2-3Gal for domestic cat and dog lungs were 21.5 and 9.9, respectively, while the composition ratios of Sia� 2-6Gal were 47.1 and 59.2, respec- tively. These results may indicate that domestic cats are more susceptible than dogs to H5N1 influenza virus infection and also cats and dogs play an important role as "mixing vessels" for the virus re-assortment.
{"title":"Determination of N-Linked Sialyl-Sugar Chains in the Lungs of Domestic Cats and Dogs in Thailand Susceptible to the Highly Pathogenic Avian Influenza Virus (H5N1)","authors":"Sukanya Thongratsakul, T. Songserm, C. Poolkhet, Sachiko Kondo, H. Yagi, H. Hiramatsu, M. Tashiro, Yasuo Suzuki","doi":"10.2174/1875398100902010028","DOIUrl":"https://doi.org/10.2174/1875398100902010028","url":null,"abstract":"Highly pathogenic and potentially pandemic H5N1 avian influenza A viruses have become endemic and are now residing in Asia, Europe, Africa, and the Middle East. H5N1 viruses have been shown to cross the species barrier and infect both dogs and cats. Domestic cats and dogs in Thailand, which were naturally infected with H5N1, exhibited severe pulmonary edema and peumonia in lung tissue as well as in other tissue dysfunctions. In order to understand the structure and quantity of influenza A receptor sialyl sugar chains in cats and dogs, especially in lung tissue, glycosylation profiles of N-glycans were determined from lung tissues of dogs and cats susceptible to H5N1 in Thailand by using multi- dimensional HPLC mapping combined with mass spectrometry. The results demonstrated different N-linked glycans com- position ratios between dogs and cats. There were a total of 30 kinds of N-linked glycans from cat lungs, which were comprised of 11 neutral, 13 mono-, 3 di-, and 3 tri-sialyl sugar chains, and 29 kinds from dog lungs, which were com- prised of 16 neutral, 11 mono- and 2 di-sialyl sugar chains. Cat lungs exhibited both 5-N-acetylneuraminic acid and 5-N- glycolylneuraminic acid sialic acid (Sia� 2-3Gal and Sia� 2-6Gal), but dog lungs contained only 5-N-acetylneuraminic (Sia� 2-3Gal and Sia� 2-6Gal) molecular species. The composition ratios of molar percentage of Sia� 2-3Gal for domestic cat and dog lungs were 21.5 and 9.9, respectively, while the composition ratios of Sia� 2-6Gal were 47.1 and 59.2, respec- tively. These results may indicate that domestic cats are more susceptible than dogs to H5N1 influenza virus infection and also cats and dogs play an important role as \"mixing vessels\" for the virus re-assortment.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"2 1","pages":"28-36"},"PeriodicalIF":0.0,"publicationDate":"2009-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68111188","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2009-08-13DOI: 10.2174/1875398100902010025
S. Lei
A fructan named ALF was isolated from the roots of Arctium lappa L.. The structure of ALF was identified by analyses of methylation, GC-MS, and both 1 H and 13 C NMR spectroscopy. The results obtained indicated that ALF, com- prised of D-fructose and D-glucose in the molar ratio of 14:1, was an inulin-type fructan, which was confirmed by the composition of 14 fructose residues linked by � (2�1) glycosidic bond and 1 glucose residue linked by � (1�2) glycosi- dic bond at the end of linear straight sugar chain.
{"title":"A Novel Fructan Possessing DB Value from Roots of Arctium lappa L.","authors":"S. Lei","doi":"10.2174/1875398100902010025","DOIUrl":"https://doi.org/10.2174/1875398100902010025","url":null,"abstract":"A fructan named ALF was isolated from the roots of Arctium lappa L.. The structure of ALF was identified by analyses of methylation, GC-MS, and both 1 H and 13 C NMR spectroscopy. The results obtained indicated that ALF, com- prised of D-fructose and D-glucose in the molar ratio of 14:1, was an inulin-type fructan, which was confirmed by the composition of 14 fructose residues linked by � (2�1) glycosidic bond and 1 glucose residue linked by � (1�2) glycosi- dic bond at the end of linear straight sugar chain.","PeriodicalId":88944,"journal":{"name":"Open glycoscience","volume":"2 1","pages":"25-27"},"PeriodicalIF":0.0,"publicationDate":"2009-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68110815","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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