Role of the N-linked glycans of the prM and E envelope proteins in tick-borne encephalitis virus particle secretion
The tick-borne encephalitis (TBE) virus has two membrane glycoproteins (prM and E), which each has one N-linked glycan. Constructs that express prM and E proteins of TBE virus have been shown to produce virus-like particles (VLPs), which have surface properties that are similar to those of infectiou...
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| Veröffentlicht in: | Vaccine 2005-04, Vol.23 (23), p.3043-3052 |
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| creator | Goto, Akiko Yoshii, Kentarou Obara, Mayumi Ueki, Tomotaka Mizutani, Tetsuya Kariwa, Hiroaki Takashima, Ikuo |
| description | The tick-borne encephalitis (TBE) virus has two membrane glycoproteins (prM and E), which each has one N-linked glycan. Constructs that express prM and E proteins of TBE virus have been shown to produce virus-like particles (VLPs), which have surface properties that are similar to those of infectious viruses. To reveal the function of glycosylation of the TBE virus prM and E proteins in the secretion of VLPs, we expressed glycosylation-mutated prM and E proteins and compared the secretion levels and biological properties of the VLPs. In the prM protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 60% of the wild-type level. On the other hand, in the E or prM-E protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 10% of the wild-type level. Furthermore, the mutant which was glycosylated at positions 66 and 154 in protein E, the level of secreted E protein was four-fold higher than that of the wild-type. However, in the mutant which was glycosylated at position 66 only, E protein secretion was reduced to only 10% of the wild-type level. These data suggest that the glycan associated with the N-linked glycosylation site at position 154 in protein E plays an important role in VLP secretion. |
| doi_str_mv | 10.1016/j.vaccine.2004.11.068 |
| format | Article |
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Constructs that express prM and E proteins of TBE virus have been shown to produce virus-like particles (VLPs), which have surface properties that are similar to those of infectious viruses. To reveal the function of glycosylation of the TBE virus prM and E proteins in the secretion of VLPs, we expressed glycosylation-mutated prM and E proteins and compared the secretion levels and biological properties of the VLPs. In the prM protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 60% of the wild-type level. On the other hand, in the E or prM-E protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 10% of the wild-type level. Furthermore, the mutant which was glycosylated at positions 66 and 154 in protein E, the level of secreted E protein was four-fold higher than that of the wild-type. However, in the mutant which was glycosylated at position 66 only, E protein secretion was reduced to only 10% of the wild-type level. These data suggest that the glycan associated with the N-linked glycosylation site at position 154 in protein E plays an important role in VLP secretion.</description><identifier>ISSN: 0264-410X</identifier><identifier>EISSN: 1873-2518</identifier><identifier>DOI: 10.1016/j.vaccine.2004.11.068</identifier><identifier>PMID: 15811651</identifier><identifier>CODEN: VACCDE</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Amino acids ; Applied microbiology ; Biological and medical sciences ; Biological properties ; Carbohydrates ; Colleges & universities ; Encephalitis Viruses, Tick-Borne - physiology ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Glycosylation ; Glycosylation sites ; Humans ; Microbiology ; Miscellaneous ; Mutagenesis ; Mutation ; Plasmids ; Protein Folding ; Secretion ; Tick-borne encephalitis virus ; Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects) ; Viral Envelope Proteins - chemistry ; Viral Envelope Proteins - physiology ; Viral infections ; Virion - physiology ; Virology ; Viruses</subject><ispartof>Vaccine, 2005-04, Vol.23 (23), p.3043-3052</ispartof><rights>2004 Elsevier Ltd</rights><rights>2006 INIST-CNRS</rights><rights>Copyright Elsevier Limited Apr 27, 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c518t-54f5433fe8db5980c3e2dfaa14fc411f6aee651e1780644dd49b4d32a781fa4e3</citedby><cites>FETCH-LOGICAL-c518t-54f5433fe8db5980c3e2dfaa14fc411f6aee651e1780644dd49b4d32a781fa4e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.proquest.com/docview/1559074024?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995,64385,64387,64389,72469</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17588913$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15811651$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Goto, Akiko</creatorcontrib><creatorcontrib>Yoshii, Kentarou</creatorcontrib><creatorcontrib>Obara, Mayumi</creatorcontrib><creatorcontrib>Ueki, Tomotaka</creatorcontrib><creatorcontrib>Mizutani, Tetsuya</creatorcontrib><creatorcontrib>Kariwa, Hiroaki</creatorcontrib><creatorcontrib>Takashima, Ikuo</creatorcontrib><title>Role of the N-linked glycans of the prM and E envelope proteins in tick-borne encephalitis virus particle secretion</title><title>Vaccine</title><addtitle>Vaccine</addtitle><description>The tick-borne encephalitis (TBE) virus has two membrane glycoproteins (prM and E), which each has one N-linked glycan. Constructs that express prM and E proteins of TBE virus have been shown to produce virus-like particles (VLPs), which have surface properties that are similar to those of infectious viruses. To reveal the function of glycosylation of the TBE virus prM and E proteins in the secretion of VLPs, we expressed glycosylation-mutated prM and E proteins and compared the secretion levels and biological properties of the VLPs. In the prM protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 60% of the wild-type level. On the other hand, in the E or prM-E protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 10% of the wild-type level. Furthermore, the mutant which was glycosylated at positions 66 and 154 in protein E, the level of secreted E protein was four-fold higher than that of the wild-type. However, in the mutant which was glycosylated at position 66 only, E protein secretion was reduced to only 10% of the wild-type level. These data suggest that the glycan associated with the N-linked glycosylation site at position 154 in protein E plays an important role in VLP secretion.</description><subject>Amino acids</subject><subject>Applied microbiology</subject><subject>Biological and medical sciences</subject><subject>Biological properties</subject><subject>Carbohydrates</subject><subject>Colleges & universities</subject><subject>Encephalitis Viruses, Tick-Borne - physiology</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Glycoproteins</topic><topic>Glycosylation</topic><topic>Glycosylation sites</topic><topic>Humans</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Mutagenesis</topic><topic>Mutation</topic><topic>Plasmids</topic><topic>Protein Folding</topic><topic>Secretion</topic><topic>Tick-borne encephalitis virus</topic><topic>Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects)</topic><topic>Viral Envelope Proteins - chemistry</topic><topic>Viral Envelope Proteins - physiology</topic><topic>Viral infections</topic><topic>Virion - physiology</topic><topic>Virology</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goto, Akiko</creatorcontrib><creatorcontrib>Yoshii, Kentarou</creatorcontrib><creatorcontrib>Obara, Mayumi</creatorcontrib><creatorcontrib>Ueki, Tomotaka</creatorcontrib><creatorcontrib>Mizutani, Tetsuya</creatorcontrib><creatorcontrib>Kariwa, Hiroaki</creatorcontrib><creatorcontrib>Takashima, Ikuo</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Proquest Nursing & Allied Health Source</collection><collection>Health and Safety Science Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Healthcare Administration Database (Alumni)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Healthcare Administration Database</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Vaccine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goto, Akiko</au><au>Yoshii, Kentarou</au><au>Obara, Mayumi</au><au>Ueki, Tomotaka</au><au>Mizutani, Tetsuya</au><au>Kariwa, Hiroaki</au><au>Takashima, Ikuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of the N-linked glycans of the prM and E envelope proteins in tick-borne encephalitis virus particle secretion</atitle><jtitle>Vaccine</jtitle><addtitle>Vaccine</addtitle><date>2005-04-27</date><risdate>2005</risdate><volume>23</volume><issue>23</issue><spage>3043</spage><epage>3052</epage><pages>3043-3052</pages><issn>0264-410X</issn><eissn>1873-2518</eissn><coden>VACCDE</coden><abstract>The tick-borne encephalitis (TBE) virus has two membrane glycoproteins (prM and E), which each has one N-linked glycan. Constructs that express prM and E proteins of TBE virus have been shown to produce virus-like particles (VLPs), which have surface properties that are similar to those of infectious viruses. To reveal the function of glycosylation of the TBE virus prM and E proteins in the secretion of VLPs, we expressed glycosylation-mutated prM and E proteins and compared the secretion levels and biological properties of the VLPs. In the prM protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 60% of the wild-type level. On the other hand, in the E or prM-E protein glycosylation-deficient mutant, the level of secreted E protein was reduced to 10% of the wild-type level. Furthermore, the mutant which was glycosylated at positions 66 and 154 in protein E, the level of secreted E protein was four-fold higher than that of the wild-type. However, in the mutant which was glycosylated at position 66 only, E protein secretion was reduced to only 10% of the wild-type level. These data suggest that the glycan associated with the N-linked glycosylation site at position 154 in protein E plays an important role in VLP secretion.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>15811651</pmid><doi>10.1016/j.vaccine.2004.11.068</doi><tpages>10</tpages></addata></record> |
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| subjects | Amino acids Applied microbiology Biological and medical sciences Biological properties Carbohydrates Colleges & universities Encephalitis Viruses, Tick-Borne - physiology Enzymes Fundamental and applied biological sciences. Psychology Glycoproteins Glycosylation Glycosylation sites Humans Microbiology Miscellaneous Mutagenesis Mutation Plasmids Protein Folding Secretion Tick-borne encephalitis virus Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects) Viral Envelope Proteins - chemistry Viral Envelope Proteins - physiology Viral infections Virion - physiology Virology Viruses |
| title | Role of the N-linked glycans of the prM and E envelope proteins in tick-borne encephalitis virus particle secretion |
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