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Identification of β1,3-galactosyltransferases responsible for biosynthesis of insect complex-type N-glycans containing a T-antigen unit in the honeybee
Honeybees ( Apis mellifera ) produce unique complex-type N -glycans bearing a Galβ1-3GalNAc (T-antigen) unit, and honeybee-specific N -glycans are linked to royal jelly glycoproteins. In this study, we identified two novel honeybee β1,3-galactosyltransferase ( β1,3-GalT ) genes responsible for biosy...
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| Published in: | Glycoconjugate journal 2015-05, Vol.32 (3-4), p.141-151 |
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| Main Authors: | , , , , , |
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| cites | cdi_FETCH-LOGICAL-c3297-260729a8eba9aea92e34a41f527b24e4a9d25beb8780b9e6bb94a634dd5809ba3 |
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| container_issue | 3-4 |
| container_start_page | 141 |
| container_title | Glycoconjugate journal |
| container_volume | 32 |
| creator | Ichimiya, Tomomi Maeda, Megumi Sakamura, Shou Kanazawa, Masato Nishihara, Shoko Kimura, Yoshinobu |
| description | Honeybees (
Apis mellifera
) produce unique complex-type
N
-glycans bearing a Galβ1-3GalNAc (T-antigen) unit, and honeybee-specific
N
-glycans are linked to royal jelly glycoproteins. In this study, we identified two novel honeybee β1,3-galactosyltransferase (
β1,3-GalT
) genes responsible for biosynthesis of the T-antigen in insect
N
-glycans. The products of the two putative
β1,3-GalT
genes
(β1,3-GalT1
and
β1,3-GalT2
), which were expressed in
Sf21
insect cells, transferred galactose (Gal) residues to GalNAc2GlcNAc2Man3GlcNAc2-PA to form the Galβ1-3GalNAc unit, indicating that the identified genes were involved in biosynthesis of the β1-3 Gal-containing
N
-glycan. Therefore, using biochemistry and molecular biology techniques, we revealed a unique
N
-glycan biosynthesis mechanism in the cephalic region of honeybees, which has not previously been found in other animal or plant cells. |
| doi_str_mv | 10.1007/s10719-015-9585-7 |
| format | article |
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Apis mellifera
) produce unique complex-type
N
-glycans bearing a Galβ1-3GalNAc (T-antigen) unit, and honeybee-specific
N
-glycans are linked to royal jelly glycoproteins. In this study, we identified two novel honeybee β1,3-galactosyltransferase (
β1,3-GalT
) genes responsible for biosynthesis of the T-antigen in insect
N
-glycans. The products of the two putative
β1,3-GalT
genes
(β1,3-GalT1
and
β1,3-GalT2
), which were expressed in
Sf21
insect cells, transferred galactose (Gal) residues to GalNAc2GlcNAc2Man3GlcNAc2-PA to form the Galβ1-3GalNAc unit, indicating that the identified genes were involved in biosynthesis of the β1-3 Gal-containing
N
-glycan. Therefore, using biochemistry and molecular biology techniques, we revealed a unique
N
-glycan biosynthesis mechanism in the cephalic region of honeybees, which has not previously been found in other animal or plant cells.</description><identifier>ISSN: 0282-0080</identifier><identifier>EISSN: 1573-4986</identifier><identifier>DOI: 10.1007/s10719-015-9585-7</identifier><identifier>PMID: 25931033</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Amino Acid Sequence ; Animals ; Antigens, Viral, Tumor - metabolism ; Bees - enzymology ; Bees - genetics ; Biochemistry ; Biomedical and Life Sciences ; Carbohydrate Conformation ; Carbohydrate Sequence ; Cloning, Molecular ; Drosophila Proteins - chemistry ; Galactose - metabolism ; Galactosyltransferases - genetics ; Galactosyltransferases - metabolism ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Life Sciences ; Molecular Sequence Data ; Original Article ; Pathology ; Polysaccharides - biosynthesis ; Polysaccharides - chemistry ; Sequence Homology, Amino Acid</subject><ispartof>Glycoconjugate journal, 2015-05, Vol.32 (3-4), p.141-151</ispartof><rights>Springer Science+Business Media New York 2015</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3297-260729a8eba9aea92e34a41f527b24e4a9d25beb8780b9e6bb94a634dd5809ba3</citedby><cites>FETCH-LOGICAL-c3297-260729a8eba9aea92e34a41f527b24e4a9d25beb8780b9e6bb94a634dd5809ba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25931033$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ichimiya, Tomomi</creatorcontrib><creatorcontrib>Maeda, Megumi</creatorcontrib><creatorcontrib>Sakamura, Shou</creatorcontrib><creatorcontrib>Kanazawa, Masato</creatorcontrib><creatorcontrib>Nishihara, Shoko</creatorcontrib><creatorcontrib>Kimura, Yoshinobu</creatorcontrib><title>Identification of β1,3-galactosyltransferases responsible for biosynthesis of insect complex-type N-glycans containing a T-antigen unit in the honeybee</title><title>Glycoconjugate journal</title><addtitle>Glycoconj J</addtitle><addtitle>Glycoconj J</addtitle><description>Honeybees (
Apis mellifera
) produce unique complex-type
N
-glycans bearing a Galβ1-3GalNAc (T-antigen) unit, and honeybee-specific
N
-glycans are linked to royal jelly glycoproteins. In this study, we identified two novel honeybee β1,3-galactosyltransferase (
β1,3-GalT
) genes responsible for biosynthesis of the T-antigen in insect
N
-glycans. The products of the two putative
β1,3-GalT
genes
(β1,3-GalT1
and
β1,3-GalT2
), which were expressed in
Sf21
insect cells, transferred galactose (Gal) residues to GalNAc2GlcNAc2Man3GlcNAc2-PA to form the Galβ1-3GalNAc unit, indicating that the identified genes were involved in biosynthesis of the β1-3 Gal-containing
N
-glycan. Therefore, using biochemistry and molecular biology techniques, we revealed a unique
N
-glycan biosynthesis mechanism in the cephalic region of honeybees, which has not previously been found in other animal or plant cells.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antigens, Viral, Tumor - metabolism</subject><subject>Bees - enzymology</subject><subject>Bees - genetics</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Carbohydrate Conformation</subject><subject>Carbohydrate Sequence</subject><subject>Cloning, Molecular</subject><subject>Drosophila Proteins - chemistry</subject><subject>Galactose - metabolism</subject><subject>Galactosyltransferases - genetics</subject><subject>Galactosyltransferases - metabolism</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>Original Article</subject><subject>Pathology</subject><subject>Polysaccharides - biosynthesis</subject><subject>Polysaccharides - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><issn>0282-0080</issn><issn>1573-4986</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><recordid>eNp9kUtuFTEQRS0EIo_AApggDxlg8Kc_9hBFfCJFMAljy-6u7jjqZzcut0TvhHWwENaEn15gyMhS-Z5bKh1CXgr-VnDev0PBe2EYFy0zrW5Z_4gcRNsr1hjdPSYHLrVknGt-QZ4h3vPKNFI_JReyNUpwpQ7k5_UIsYQpDK6EFGma6O9f4o1is1vcUBLuS8ku4gTZISDNgGuKGPwCdEqZ-lAjsdwBBjzBISIMhQ7puC7wg5V9BfqFzcs-1JI6jsWFGOJMHb1lrm6eIdIthlJJWmvoXYqwe4Dn5MnkFoQXD-8l-fbxw-3VZ3bz9dP11fsbNihpeiY73kvjNHhnHDgjQTWuEVMrey8baJwZZevB615zb6Dz3jSuU804tpob79QleX3uXXP6vgEWeww4wLK4CGlDKzotG9lKpWpUnKNDTogZJrvmcHR5t4LbkxB7FmKrEHsSYvvKvHqo3_wRxn_EXwM1IM8BrF9xhmzv05ZjPfk_rX8AFt2aRg</recordid><startdate>20150501</startdate><enddate>20150501</enddate><creator>Ichimiya, Tomomi</creator><creator>Maeda, Megumi</creator><creator>Sakamura, Shou</creator><creator>Kanazawa, Masato</creator><creator>Nishihara, Shoko</creator><creator>Kimura, Yoshinobu</creator><general>Springer US</general><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>20150501</creationdate><title>Identification of β1,3-galactosyltransferases responsible for biosynthesis of insect complex-type N-glycans containing a T-antigen unit in the honeybee</title><author>Ichimiya, Tomomi ; Maeda, Megumi ; Sakamura, Shou ; Kanazawa, Masato ; Nishihara, Shoko ; Kimura, Yoshinobu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3297-260729a8eba9aea92e34a41f527b24e4a9d25beb8780b9e6bb94a634dd5809ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antigens, Viral, Tumor - metabolism</topic><topic>Bees - enzymology</topic><topic>Bees - genetics</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Carbohydrate Conformation</topic><topic>Carbohydrate Sequence</topic><topic>Cloning, Molecular</topic><topic>Drosophila Proteins - chemistry</topic><topic>Galactose - metabolism</topic><topic>Galactosyltransferases - genetics</topic><topic>Galactosyltransferases - metabolism</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Life Sciences</topic><topic>Molecular Sequence Data</topic><topic>Original Article</topic><topic>Pathology</topic><topic>Polysaccharides - biosynthesis</topic><topic>Polysaccharides - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ichimiya, Tomomi</creatorcontrib><creatorcontrib>Maeda, Megumi</creatorcontrib><creatorcontrib>Sakamura, Shou</creatorcontrib><creatorcontrib>Kanazawa, Masato</creatorcontrib><creatorcontrib>Nishihara, Shoko</creatorcontrib><creatorcontrib>Kimura, Yoshinobu</creatorcontrib><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>Glycoconjugate journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ichimiya, Tomomi</au><au>Maeda, Megumi</au><au>Sakamura, Shou</au><au>Kanazawa, Masato</au><au>Nishihara, Shoko</au><au>Kimura, Yoshinobu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of β1,3-galactosyltransferases responsible for biosynthesis of insect complex-type N-glycans containing a T-antigen unit in the honeybee</atitle><jtitle>Glycoconjugate journal</jtitle><stitle>Glycoconj J</stitle><addtitle>Glycoconj J</addtitle><date>2015-05-01</date><risdate>2015</risdate><volume>32</volume><issue>3-4</issue><spage>141</spage><epage>151</epage><pages>141-151</pages><issn>0282-0080</issn><eissn>1573-4986</eissn><abstract>Honeybees (
Apis mellifera
) produce unique complex-type
N
-glycans bearing a Galβ1-3GalNAc (T-antigen) unit, and honeybee-specific
N
-glycans are linked to royal jelly glycoproteins. In this study, we identified two novel honeybee β1,3-galactosyltransferase (
β1,3-GalT
) genes responsible for biosynthesis of the T-antigen in insect
N
-glycans. The products of the two putative
β1,3-GalT
genes
(β1,3-GalT1
and
β1,3-GalT2
), which were expressed in
Sf21
insect cells, transferred galactose (Gal) residues to GalNAc2GlcNAc2Man3GlcNAc2-PA to form the Galβ1-3GalNAc unit, indicating that the identified genes were involved in biosynthesis of the β1-3 Gal-containing
N
-glycan. Therefore, using biochemistry and molecular biology techniques, we revealed a unique
N
-glycan biosynthesis mechanism in the cephalic region of honeybees, which has not previously been found in other animal or plant cells.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>25931033</pmid><doi>10.1007/s10719-015-9585-7</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0282-0080 |
| ispartof | Glycoconjugate journal, 2015-05, Vol.32 (3-4), p.141-151 |
| issn | 0282-0080 1573-4986 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1682425233 |
| source | Springer Nature |
| subjects | Amino Acid Sequence Animals Antigens, Viral, Tumor - metabolism Bees - enzymology Bees - genetics Biochemistry Biomedical and Life Sciences Carbohydrate Conformation Carbohydrate Sequence Cloning, Molecular Drosophila Proteins - chemistry Galactose - metabolism Galactosyltransferases - genetics Galactosyltransferases - metabolism Insect Proteins - genetics Insect Proteins - metabolism Life Sciences Molecular Sequence Data Original Article Pathology Polysaccharides - biosynthesis Polysaccharides - chemistry Sequence Homology, Amino Acid |
| title | Identification of β1,3-galactosyltransferases responsible for biosynthesis of insect complex-type N-glycans containing a T-antigen unit in the honeybee |
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