Effect of glycosylation and glucose trimming inhibitors on the influenza A virus glycoproteins
N-glycosylation and glucose trimming of the influenza virus hemagglutinin (HA) and neuraminidase (NA) were studied by using glycosylation inhibitor (tunicamycin; TM) and glucosidase inhibitors. TM treatment of MDCK cells infected with a reassortant virus NWS-N8 resulted in reduced transport of the v...
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| Veröffentlicht in: | Journal of veterinary medical science 2000-06, Vol.62 (6), p.575-581 |
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| creator | Saito, T. (Kobe Univ. (Japan). Faculty of Agriculture) Yamaguchi, I |
| description | N-glycosylation and glucose trimming of the influenza virus hemagglutinin (HA) and neuraminidase (NA) were studied by using glycosylation inhibitor (tunicamycin; TM) and glucosidase inhibitors. TM treatment of MDCK cells infected with a reassortant virus NWS-N8 resulted in reduced transport of the viral glycoproteins to the cell surface. The degree of the effects differed between the HA and the NA (80% reduction for the HA and 97% reduction for the NA), indicating a difference in dependency on N-glycosylation between these glycoproteins. Differential dependency on glucose trimming was clearly demonstrated when the surface transport of the glycoproteins was compared after treatment of the virus-infected cells with glucosidase inhibitors. Fluorescence-activated cell sorting (FACS) analysis revealed that the surface transport of the NA reduced to 50% after castanospermine (CST) treatment but not did that of the HA. An anti-viral effect of a glucosidase inhibitor on the NWS-N8 strain was also demonstrated. The correlation between the expression of the NA on the cell surface and virus yield suggests that CST may interfere with virus release through its effect on the NA. |
| doi_str_mv | 10.1292/jvms.62.575 |
| format | Article |
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Fluorescence-activated cell sorting (FACS) analysis revealed that the surface transport of the NA reduced to 50% after castanospermine (CST) treatment but not did that of the HA. An anti-viral effect of a glucosidase inhibitor on the NWS-N8 strain was also demonstrated. 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(Kobe Univ. (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Yamaguchi, I</creatorcontrib><title>Effect of glycosylation and glucose trimming inhibitors on the influenza A virus glycoproteins</title><title>Journal of veterinary medical science</title><addtitle>J Vet Med Sci</addtitle><description>N-glycosylation and glucose trimming of the influenza virus hemagglutinin (HA) and neuraminidase (NA) were studied by using glycosylation inhibitor (tunicamycin; TM) and glucosidase inhibitors. TM treatment of MDCK cells infected with a reassortant virus NWS-N8 resulted in reduced transport of the viral glycoproteins to the cell surface. The degree of the effects differed between the HA and the NA (80% reduction for the HA and 97% reduction for the NA), indicating a difference in dependency on N-glycosylation between these glycoproteins. Differential dependency on glucose trimming was clearly demonstrated when the surface transport of the glycoproteins was compared after treatment of the virus-infected cells with glucosidase inhibitors. Fluorescence-activated cell sorting (FACS) analysis revealed that the surface transport of the NA reduced to 50% after castanospermine (CST) treatment but not did that of the HA. An anti-viral effect of a glucosidase inhibitor on the NWS-N8 strain was also demonstrated. The correlation between the expression of the NA on the cell surface and virus yield suggests that CST may interfere with virus release through its effect on the NA.</description><subject>1-Deoxynojirimycin - chemistry</subject><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Antiviral Agents - chemistry</subject><subject>Cell Line</subject><subject>Colony Count, Microbial</subject><subject>Cyclohexenes</subject><subject>ENZYME INHIBITORS</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Flow Cytometry</subject><subject>Fluorescent Antibody Technique, Indirect</subject><subject>GLUCOSIDASES</subject><subject>Glucosidases - antagonists & inhibitors</subject><subject>Glucosidases - chemistry</subject><subject>GLYCOPROTEINS</subject><subject>Glycosylation</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</subject><subject>Indolizines - chemistry</subject><subject>Influenza A virus - chemistry</subject><subject>INFLUENZAVIRUS</subject><subject>Inositol - analogs & derivatives</subject><subject>Inositol - chemistry</subject><subject>LIVESTOCK</subject><subject>Neuraminidase - analysis</subject><subject>Neuraminidase - chemistry</subject><subject>Reassortant Viruses - chemistry</subject><subject>Tunicamycin - chemistry</subject><issn>0916-7250</issn><issn>1347-7439</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkDtPwzAUhS0EoqUwMYMysaCU60fseERVeakSDLBiuYndukriEieVyq_HVTowXeno0zm6H0LXGKaYSPKw2dVhysk0E9kJGmPKRCoYladoDBLzVJAMRugihA0AwYzLczTCIEHwnIzR99xaU3SJt8mq2hc-7CvdOd8kuilj0sfEJF3r6to1q8Q1a7d0nW9DEpFubWJiq940vzp5THau7cNQs219Z1wTLtGZ1VUwV8c7QV9P88_ZS7p4f36dPS7SIqO8Swk1gktWSsLA5ljkBiim1kLGGadguKVZoaEsLdc6N5wuBbNMcqqXhbRQ0Am6G3rj8E9vQqdqFwpTVboxvg9KYMKpABzB-wEsWh9Ca6zaxud0u1cY1EGnOuhUnKioM9K3x9p-WZvyHzv4i8DNAFjtlV61Lqi3DwKAo2vIMf0D6IN7FQ</recordid><startdate>20000601</startdate><enddate>20000601</enddate><creator>Saito, T. 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Faculty of Agriculture) ; Yamaguchi, I</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c536t-23e7694d9240f8178e0313ff0564630e6f35ca0ddf6aa8e63b74f4963abc9f0c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>1-Deoxynojirimycin - chemistry</topic><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Antiviral Agents - chemistry</topic><topic>Cell Line</topic><topic>Colony Count, Microbial</topic><topic>Cyclohexenes</topic><topic>ENZYME INHIBITORS</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Flow Cytometry</topic><topic>Fluorescent Antibody Technique, Indirect</topic><topic>GLUCOSIDASES</topic><topic>Glucosidases - antagonists & inhibitors</topic><topic>Glucosidases - chemistry</topic><topic>GLYCOPROTEINS</topic><topic>Glycosylation</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</topic><topic>Indolizines - chemistry</topic><topic>Influenza A virus - chemistry</topic><topic>INFLUENZAVIRUS</topic><topic>Inositol - analogs & derivatives</topic><topic>Inositol - chemistry</topic><topic>LIVESTOCK</topic><topic>Neuraminidase - analysis</topic><topic>Neuraminidase - chemistry</topic><topic>Reassortant Viruses - chemistry</topic><topic>Tunicamycin - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saito, T. (Kobe Univ. (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Yamaguchi, I</creatorcontrib><collection>AGRIS</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>Journal of veterinary medical science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saito, T. (Kobe Univ. (Japan). Faculty of Agriculture)</au><au>Yamaguchi, I</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effect of glycosylation and glucose trimming inhibitors on the influenza A virus glycoproteins</atitle><jtitle>Journal of veterinary medical science</jtitle><addtitle>J Vet Med Sci</addtitle><date>2000-06-01</date><risdate>2000</risdate><volume>62</volume><issue>6</issue><spage>575</spage><epage>581</epage><pages>575-581</pages><issn>0916-7250</issn><eissn>1347-7439</eissn><abstract>N-glycosylation and glucose trimming of the influenza virus hemagglutinin (HA) and neuraminidase (NA) were studied by using glycosylation inhibitor (tunicamycin; TM) and glucosidase inhibitors. TM treatment of MDCK cells infected with a reassortant virus NWS-N8 resulted in reduced transport of the viral glycoproteins to the cell surface. The degree of the effects differed between the HA and the NA (80% reduction for the HA and 97% reduction for the NA), indicating a difference in dependency on N-glycosylation between these glycoproteins. Differential dependency on glucose trimming was clearly demonstrated when the surface transport of the glycoproteins was compared after treatment of the virus-infected cells with glucosidase inhibitors. Fluorescence-activated cell sorting (FACS) analysis revealed that the surface transport of the NA reduced to 50% after castanospermine (CST) treatment but not did that of the HA. An anti-viral effect of a glucosidase inhibitor on the NWS-N8 strain was also demonstrated. The correlation between the expression of the NA on the cell surface and virus yield suggests that CST may interfere with virus release through its effect on the NA.</abstract><cop>Japan</cop><pmid>10907682</pmid><doi>10.1292/jvms.62.575</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | J-STAGE Free; MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | 1-Deoxynojirimycin - chemistry Animals Antibodies, Monoclonal Antiviral Agents - chemistry Cell Line Colony Count, Microbial Cyclohexenes ENZYME INHIBITORS Enzyme Inhibitors - chemistry Flow Cytometry Fluorescent Antibody Technique, Indirect GLUCOSIDASES Glucosidases - antagonists & inhibitors Glucosidases - chemistry GLYCOPROTEINS Glycosylation Hemagglutinin Glycoproteins, Influenza Virus - chemistry Indolizines - chemistry Influenza A virus - chemistry INFLUENZAVIRUS Inositol - analogs & derivatives Inositol - chemistry LIVESTOCK Neuraminidase - analysis Neuraminidase - chemistry Reassortant Viruses - chemistry Tunicamycin - chemistry |
| title | Effect of glycosylation and glucose trimming inhibitors on the influenza A virus glycoproteins |
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