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Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors
The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes, N -glycan chains, as well as their polyvalent forms in N -glyco...
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Published in: | Glycoconjugate journal 2023-10, Vol.40 (5), p.587-608 |
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description | The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes,
N
-glycan chains, as well as their polyvalent forms in
N
-glycoproteins involved in the Con A-glycan interactions have not been well defined and organized. In this study, the recognition factors involved in these interactions were analyzed by our well developed method- the enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all the data obtained, it is concluded that Con A, as previously reported, has a relatively broad and wide recognition ability of the Manα1 → and Glcα1 → related glycans. It reacted not only strongly with yeast mannan and glycogens, but also bound well with a large number of mammalian
N
-glycans, including the
N
-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobulin and lactoferrin. The recognition specificity of Con A towards ligands, expressed by
M
olar
R
elative
P
otency (Molar R.P.), in a decreasing order is as follows: α1 → 3, α1 → 6 Mannopentaose (
M
5
) and Biantennary
N
-linked core pentasaccharide (
M
Di
) ≥ α1 → 3, α1 → 6 Mannotriose (
M
3
) > Manα1 → 3Man (α1 → 3Mannobiose), Manα1 → 2Man (α1 → 2Mannobiose), Manα1 → 6Man (α1 → 6Mannobiose), Manα1 → 4Man (α1 → 4Mannobiose) > GlcNAcβ1 → 2
Man
(β1 → 2 N-Acetyl glucosamine-mannose) > Manα1 → /Glcα1 → >
Man >
Glc, while Gal / GalNAc were inactive. Furthermore, the Man related code system, in this study, is proposed to express by both numbers of Man and GlcNAcβ1 → branches (
M
3
to
M
9
/
M
Mono to Penta etc.
) and
a table of three Manα1 → and Glcα1 → related biomasses of six recognition factors involved in the Con A-glycan interactions
has also been demonstrated. These themes should be one of the most valuable advances since 1980s. |
doi_str_mv | 10.1007/s10719-023-10129-4 |
format | article |
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N
-glycan chains, as well as their polyvalent forms in
N
-glycoproteins involved in the Con A-glycan interactions have not been well defined and organized. In this study, the recognition factors involved in these interactions were analyzed by our well developed method- the enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all the data obtained, it is concluded that Con A, as previously reported, has a relatively broad and wide recognition ability of the Manα1 → and Glcα1 → related glycans. It reacted not only strongly with yeast mannan and glycogens, but also bound well with a large number of mammalian
N
-glycans, including the
N
-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobulin and lactoferrin. The recognition specificity of Con A towards ligands, expressed by
M
olar
R
elative
P
otency (Molar R.P.), in a decreasing order is as follows: α1 → 3, α1 → 6 Mannopentaose (
M
5
) and Biantennary
N
-linked core pentasaccharide (
M
Di
) ≥ α1 → 3, α1 → 6 Mannotriose (
M
3
) > Manα1 → 3Man (α1 → 3Mannobiose), Manα1 → 2Man (α1 → 2Mannobiose), Manα1 → 6Man (α1 → 6Mannobiose), Manα1 → 4Man (α1 → 4Mannobiose) > GlcNAcβ1 → 2
Man
(β1 → 2 N-Acetyl glucosamine-mannose) > Manα1 → /Glcα1 → >
Man >
Glc, while Gal / GalNAc were inactive. Furthermore, the Man related code system, in this study, is proposed to express by both numbers of Man and GlcNAcβ1 → branches (
M
3
to
M
9
/
M
Mono to Penta etc.
) and
a table of three Manα1 → and Glcα1 → related biomasses of six recognition factors involved in the Con A-glycan interactions
has also been demonstrated. These themes should be one of the most valuable advances since 1980s.</description><identifier>ISSN: 0282-0080</identifier><identifier>EISSN: 1573-4986</identifier><identifier>DOI: 10.1007/s10719-023-10129-4</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Biochemistry ; Biomedical and Life Sciences ; Blood groups ; Carbohydrates ; Cysts ; Enzymes ; Glucosamine ; Glycoconjugates ; Glycoproteins ; Lactoferrin ; Lectins ; Life Sciences ; Mannan ; Mannose ; N-glycans ; Pathology ; Polysaccharides ; Thyroglobulin</subject><ispartof>Glycoconjugate journal, 2023-10, Vol.40 (5), p.587-608</ispartof><rights>The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c303t-70b6b42eb561ae8f47db390fb844485af043ebd025d6505125ae0a6fcaf9de0a3</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></links><search><creatorcontrib>Wu, Albert M.</creatorcontrib><title>Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors</title><title>Glycoconjugate journal</title><addtitle>Glycoconj J</addtitle><description>The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes,
N
-glycan chains, as well as their polyvalent forms in
N
-glycoproteins involved in the Con A-glycan interactions have not been well defined and organized. In this study, the recognition factors involved in these interactions were analyzed by our well developed method- the enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all the data obtained, it is concluded that Con A, as previously reported, has a relatively broad and wide recognition ability of the Manα1 → and Glcα1 → related glycans. It reacted not only strongly with yeast mannan and glycogens, but also bound well with a large number of mammalian
N
-glycans, including the
N
-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobulin and lactoferrin. The recognition specificity of Con A towards ligands, expressed by
M
olar
R
elative
P
otency (Molar R.P.), in a decreasing order is as follows: α1 → 3, α1 → 6 Mannopentaose (
M
5
) and Biantennary
N
-linked core pentasaccharide (
M
Di
) ≥ α1 → 3, α1 → 6 Mannotriose (
M
3
) > Manα1 → 3Man (α1 → 3Mannobiose), Manα1 → 2Man (α1 → 2Mannobiose), Manα1 → 6Man (α1 → 6Mannobiose), Manα1 → 4Man (α1 → 4Mannobiose) > GlcNAcβ1 → 2
Man
(β1 → 2 N-Acetyl glucosamine-mannose) > Manα1 → /Glcα1 → >
Man >
Glc, while Gal / GalNAc were inactive. Furthermore, the Man related code system, in this study, is proposed to express by both numbers of Man and GlcNAcβ1 → branches (
M
3
to
M
9
/
M
Mono to Penta etc.
) and
a table of three Manα1 → and Glcα1 → related biomasses of six recognition factors involved in the Con A-glycan interactions
has also been demonstrated. These themes should be one of the most valuable advances since 1980s.</description><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Blood groups</subject><subject>Carbohydrates</subject><subject>Cysts</subject><subject>Enzymes</subject><subject>Glucosamine</subject><subject>Glycoconjugates</subject><subject>Glycoproteins</subject><subject>Lactoferrin</subject><subject>Lectins</subject><subject>Life Sciences</subject><subject>Mannan</subject><subject>Mannose</subject><subject>N-glycans</subject><subject>Pathology</subject><subject>Polysaccharides</subject><subject>Thyroglobulin</subject><issn>0282-0080</issn><issn>1573-4986</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp9kc1q3TAQhUVpoLdJX6ArQTdZRM3ox7a8DJf0B0IKJVkLWZZuHWzpVpIXeYS8dSa9FwpZZKXRzHfODBxCPnP4ygG6y8Kh4z0DIRkHLnqm3pENbzrJVK_b92QDQgsGoOED-VjKA6BICb0hT7_T7AtNgdY_npaaV1fXbGe6xqmWC7qbH12qaY_MJV3ssth5spHespeBjYWGlOk2RXp17NApVp-tq1OKqEfXKVOXRo8fG8djI3uXdrgBIRoQTrmckZNg5-I_Hd9Tcv_t-m77g938-v5ze3XDnARZWQdDOyjhh6bl1uugunGQPYRBK6V0YwMo6YcRRDO2DTRcNNaDbYOzoR-xkqfk_OC7z-nv6ks1y1Scn2cbfVqLEbqVXdtr3iH65RX6kNYc8TqktMZ1ugOkxIFyOZWSfTD7PC02PxoO5iUdc0jHYDrmXzpGoUgeRAXhuPP5v_Ubqmddx5PY</recordid><startdate>20231001</startdate><enddate>20231001</enddate><creator>Wu, Albert M.</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20231001</creationdate><title>Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors</title><author>Wu, Albert M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c303t-70b6b42eb561ae8f47db390fb844485af043ebd025d6505125ae0a6fcaf9de0a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Blood groups</topic><topic>Carbohydrates</topic><topic>Cysts</topic><topic>Enzymes</topic><topic>Glucosamine</topic><topic>Glycoconjugates</topic><topic>Glycoproteins</topic><topic>Lactoferrin</topic><topic>Lectins</topic><topic>Life Sciences</topic><topic>Mannan</topic><topic>Mannose</topic><topic>N-glycans</topic><topic>Pathology</topic><topic>Polysaccharides</topic><topic>Thyroglobulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, Albert M.</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>ProQuest - Health & Medical Complete保健、医学与药学数据库</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</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>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Science Journals</collection><collection>Biological Science Database</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>Glycoconjugate journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, Albert M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors</atitle><jtitle>Glycoconjugate journal</jtitle><stitle>Glycoconj J</stitle><date>2023-10-01</date><risdate>2023</risdate><volume>40</volume><issue>5</issue><spage>587</spage><epage>608</epage><pages>587-608</pages><issn>0282-0080</issn><eissn>1573-4986</eissn><abstract>The binding property of Con A has been studied intensively and applied widely to glycoconjugates / glycobiology for over 80 years. However, its role and functional relationship of Con A with these mammalian structural units, glycotopes,
N
-glycan chains, as well as their polyvalent forms in
N
-glycoproteins involved in the Con A-glycan interactions have not been well defined and organized. In this study, the recognition factors involved in these interactions were analyzed by our well developed method- the enzyme linked lectinosorbent (ELLSA) and inhibition assay. Based on all the data obtained, it is concluded that Con A, as previously reported, has a relatively broad and wide recognition ability of the Manα1 → and Glcα1 → related glycans. It reacted not only strongly with yeast mannan and glycogens, but also bound well with a large number of mammalian
N
-glycans, including the
N
-glycans of rat sublingual gp (RSL), human Tamm-Horsfall glycoprotein (THGP), thyroglobulin and lactoferrin. The recognition specificity of Con A towards ligands, expressed by
M
olar
R
elative
P
otency (Molar R.P.), in a decreasing order is as follows: α1 → 3, α1 → 6 Mannopentaose (
M
5
) and Biantennary
N
-linked core pentasaccharide (
M
Di
) ≥ α1 → 3, α1 → 6 Mannotriose (
M
3
) > Manα1 → 3Man (α1 → 3Mannobiose), Manα1 → 2Man (α1 → 2Mannobiose), Manα1 → 6Man (α1 → 6Mannobiose), Manα1 → 4Man (α1 → 4Mannobiose) > GlcNAcβ1 → 2
Man
(β1 → 2 N-Acetyl glucosamine-mannose) > Manα1 → /Glcα1 → >
Man >
Glc, while Gal / GalNAc were inactive. Furthermore, the Man related code system, in this study, is proposed to express by both numbers of Man and GlcNAcβ1 → branches (
M
3
to
M
9
/
M
Mono to Penta etc.
) and
a table of three Manα1 → and Glcα1 → related biomasses of six recognition factors involved in the Con A-glycan interactions
has also been demonstrated. These themes should be one of the most valuable advances since 1980s.</abstract><cop>New York</cop><pub>Springer US</pub><doi>10.1007/s10719-023-10129-4</doi><tpages>22</tpages></addata></record> |
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subjects | Biochemistry Biomedical and Life Sciences Blood groups Carbohydrates Cysts Enzymes Glucosamine Glycoconjugates Glycoproteins Lactoferrin Lectins Life Sciences Mannan Mannose N-glycans Pathology Polysaccharides Thyroglobulin |
title | Roles of the structural units, glycotopes / mammalian N-glycans for Con A-glycan interactions, their codes, and their recognition factors |
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