Interaction of cholera toxin B subunit with T and B lymphocytes
We have prepared 125I-labeled cholera toxin B subunit (125I-labeled CT-B, a specific activity of 98Ci/mmol) and found that its binding to T and B lymphocytes from the blood of healthy donors was high-affinity (Kd 2.8 and 3.0nM, respectively). The binding of labeled protein was completely inhibited b...
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Veröffentlicht in: | International immunopharmacology 2017-09, Vol.50, p.279-282 |
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description | We have prepared 125I-labeled cholera toxin B subunit (125I-labeled CT-B, a specific activity of 98Ci/mmol) and found that its binding to T and B lymphocytes from the blood of healthy donors was high-affinity (Kd 2.8 and 3.0nM, respectively). The binding of labeled protein was completely inhibited by unlabeled thymosin-α1 (TM-α1), interferon-α2 (IFN-α2), and the synthetic peptide LKEKK that corresponds to residues 16–20 in TM-α1 and 131–135 in IFN-α2, but was not inhibited by the synthetic peptide KKEKL with inverted amino acid sequence (Ki>10μM). Thus, TM-α1, IFN-α2, and the peptide: LKEKK bind with high affinity and specificity to CT-B receptor on donor blood T and B lymphocytes. It was found that CT-B and the peptide: LKEKK at concentrations of 10–1000nM increased in a dose-dependent manner the soluble guanylate cyclase activity in T and B lymphocytes.
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•Cholera toxin B subunit binds with high affinity to human T and B lymphocytes.•TM-α1, INF-α2, peptide LKEKK completely inhibit the cholera toxin B subunit binding.•Residues 16–20 in TM-α1 and 131–135 in IFN-α2 are involved in binding to the receptor.•Binding to the receptor leads to an increase in activity of soluble guanylate cyclase. |
doi_str_mv | 10.1016/j.intimp.2017.07.011 |
format | Article |
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[Display omitted]
•Cholera toxin B subunit binds with high affinity to human T and B lymphocytes.•TM-α1, INF-α2, peptide LKEKK completely inhibit the cholera toxin B subunit binding.•Residues 16–20 in TM-α1 and 131–135 in IFN-α2 are involved in binding to the receptor.•Binding to the receptor leads to an increase in activity of soluble guanylate cyclase.</description><identifier>ISSN: 1567-5769</identifier><identifier>EISSN: 1878-1705</identifier><identifier>DOI: 10.1016/j.intimp.2017.07.011</identifier><identifier>PMID: 28719851</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Affinity ; B-Lymphocytes - immunology ; B-Lymphocytes - metabolism ; Binding ; Blood ; Blood Cells - immunology ; Blood Cells - metabolism ; Cells, Cultured ; Cholera ; Cholera toxin ; Cholera Toxin - immunology ; Cholera Toxin - metabolism ; Cholera toxin B subunit ; Enzyme Activation ; Guanylate cyclase ; Guanylate Cyclase - metabolism ; Humans ; Infections ; Interferon ; Interferon-alpha - metabolism ; Lymphocyte ; Lymphocytes ; Lymphocytes B ; Lymphocytes T ; Peptide ; Peptide Fragments - metabolism ; Protein ; Protein Binding ; Proteins ; Public health ; Receptor ; Studies ; T-Lymphocytes - immunology ; T-Lymphocytes - metabolism ; Thymosin - analogs & derivatives ; Thymosin - metabolism ; Toxins ; Waterborne diseases</subject><ispartof>International immunopharmacology, 2017-09, Vol.50, p.279-282</ispartof><rights>2017 Elsevier B.V.</rights><rights>Copyright © 2017 Elsevier B.V. All rights reserved.</rights><rights>Copyright Elsevier BV Sep 2017</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-89954eb580c404d8d4d5afe0844dfee360d8b4071e3c0d290cc3614908d16d773</citedby><cites>FETCH-LOGICAL-c390t-89954eb580c404d8d4d5afe0844dfee360d8b4071e3c0d290cc3614908d16d773</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1567576917302771$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28719851$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Navolotskaya, Elena V.</creatorcontrib><creatorcontrib>Sadovnikov, Vladimir B.</creatorcontrib><creatorcontrib>Zinchenko, Dmitry V.</creatorcontrib><creatorcontrib>Lipkin, Valery M.</creatorcontrib><creatorcontrib>Zav'yalov, Vladimir P.</creatorcontrib><title>Interaction of cholera toxin B subunit with T and B lymphocytes</title><title>International immunopharmacology</title><addtitle>Int Immunopharmacol</addtitle><description>We have prepared 125I-labeled cholera toxin B subunit (125I-labeled CT-B, a specific activity of 98Ci/mmol) and found that its binding to T and B lymphocytes from the blood of healthy donors was high-affinity (Kd 2.8 and 3.0nM, respectively). The binding of labeled protein was completely inhibited by unlabeled thymosin-α1 (TM-α1), interferon-α2 (IFN-α2), and the synthetic peptide LKEKK that corresponds to residues 16–20 in TM-α1 and 131–135 in IFN-α2, but was not inhibited by the synthetic peptide KKEKL with inverted amino acid sequence (Ki>10μM). Thus, TM-α1, IFN-α2, and the peptide: LKEKK bind with high affinity and specificity to CT-B receptor on donor blood T and B lymphocytes. It was found that CT-B and the peptide: LKEKK at concentrations of 10–1000nM increased in a dose-dependent manner the soluble guanylate cyclase activity in T and B lymphocytes.
[Display omitted]
•Cholera toxin B subunit binds with high affinity to human T and B lymphocytes.•TM-α1, INF-α2, peptide LKEKK completely inhibit the cholera toxin B subunit binding.•Residues 16–20 in TM-α1 and 131–135 in IFN-α2 are involved in binding to the receptor.•Binding to the receptor leads to an increase in activity of soluble guanylate cyclase.</description><subject>Affinity</subject><subject>B-Lymphocytes - immunology</subject><subject>B-Lymphocytes - metabolism</subject><subject>Binding</subject><subject>Blood</subject><subject>Blood Cells - immunology</subject><subject>Blood Cells - metabolism</subject><subject>Cells, Cultured</subject><subject>Cholera</subject><subject>Cholera toxin</subject><subject>Cholera Toxin - immunology</subject><subject>Cholera Toxin - metabolism</subject><subject>Cholera toxin B subunit</subject><subject>Enzyme Activation</subject><subject>Guanylate cyclase</subject><subject>Guanylate Cyclase - metabolism</subject><subject>Humans</subject><subject>Infections</subject><subject>Interferon</subject><subject>Interferon-alpha - metabolism</subject><subject>Lymphocyte</subject><subject>Lymphocytes</subject><subject>Lymphocytes B</subject><subject>Lymphocytes T</subject><subject>Peptide</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Public health</subject><subject>Receptor</subject><subject>Studies</subject><subject>T-Lymphocytes - immunology</subject><subject>T-Lymphocytes - metabolism</subject><subject>Thymosin - analogs & derivatives</subject><subject>Thymosin - metabolism</subject><subject>Toxins</subject><subject>Waterborne diseases</subject><issn>1567-5769</issn><issn>1878-1705</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1v1DAQhi1ERUvhHyAUiQuXbGc2jj8uIKgKrVSpl3K2svZE61ViL7ZD2X-PyxYOHJBGGnv0-B3rYewNwgoBxcVu5UPx8361BpQrqIX4jJ2hkqpFCf3zeu6FbHsp9Cl7mfMOKggcX7DTtZKoVY9n7ONNKJQGW3wMTRwbu41TvTcl_vSh-dzkZbMEX5oHX7bNfTMEV4fTYd5voz0Uyq_YyThMmV4_9XP27cvV_eV1e3v39eby021rOw2lVVr3nDa9AsuBO-W464eRQHHuRqJOgFMbDhKps-DWGqztBHINyqFwUnbn7P0xd5_i94VyMbPPlqZpCBSXbFCvodPIESv67h90F5cU6u8q1QMIoQRUih8pm2LOiUazT34e0sEgmEfBZmeOgs2jYAO1foe_fQpfNjO5v4_-GK3AhyNA1cYPT8lk6ylYcj6RLcZF__8NvwATJov9</recordid><startdate>201709</startdate><enddate>201709</enddate><creator>Navolotskaya, Elena V.</creator><creator>Sadovnikov, Vladimir B.</creator><creator>Zinchenko, Dmitry V.</creator><creator>Lipkin, Valery M.</creator><creator>Zav'yalov, Vladimir P.</creator><general>Elsevier B.V</general><general>Elsevier BV</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>7QO</scope><scope>7T5</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>201709</creationdate><title>Interaction of cholera toxin B subunit with T and B lymphocytes</title><author>Navolotskaya, Elena V. ; Sadovnikov, Vladimir B. ; Zinchenko, Dmitry V. ; Lipkin, Valery M. ; Zav'yalov, Vladimir P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c390t-89954eb580c404d8d4d5afe0844dfee360d8b4071e3c0d290cc3614908d16d773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Affinity</topic><topic>B-Lymphocytes - immunology</topic><topic>B-Lymphocytes - metabolism</topic><topic>Binding</topic><topic>Blood</topic><topic>Blood Cells - immunology</topic><topic>Blood Cells - metabolism</topic><topic>Cells, Cultured</topic><topic>Cholera</topic><topic>Cholera toxin</topic><topic>Cholera Toxin - immunology</topic><topic>Cholera Toxin - metabolism</topic><topic>Cholera toxin B subunit</topic><topic>Enzyme Activation</topic><topic>Guanylate cyclase</topic><topic>Guanylate Cyclase - metabolism</topic><topic>Humans</topic><topic>Infections</topic><topic>Interferon</topic><topic>Interferon-alpha - metabolism</topic><topic>Lymphocyte</topic><topic>Lymphocytes</topic><topic>Lymphocytes B</topic><topic>Lymphocytes T</topic><topic>Peptide</topic><topic>Peptide Fragments - metabolism</topic><topic>Protein</topic><topic>Protein Binding</topic><topic>Proteins</topic><topic>Public health</topic><topic>Receptor</topic><topic>Studies</topic><topic>T-Lymphocytes - immunology</topic><topic>T-Lymphocytes - metabolism</topic><topic>Thymosin - analogs & derivatives</topic><topic>Thymosin - metabolism</topic><topic>Toxins</topic><topic>Waterborne diseases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Navolotskaya, Elena V.</creatorcontrib><creatorcontrib>Sadovnikov, Vladimir B.</creatorcontrib><creatorcontrib>Zinchenko, Dmitry V.</creatorcontrib><creatorcontrib>Lipkin, Valery M.</creatorcontrib><creatorcontrib>Zav'yalov, Vladimir P.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Immunology Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>International immunopharmacology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Navolotskaya, Elena V.</au><au>Sadovnikov, Vladimir B.</au><au>Zinchenko, Dmitry V.</au><au>Lipkin, Valery M.</au><au>Zav'yalov, Vladimir P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction of cholera toxin B subunit with T and B lymphocytes</atitle><jtitle>International immunopharmacology</jtitle><addtitle>Int Immunopharmacol</addtitle><date>2017-09</date><risdate>2017</risdate><volume>50</volume><spage>279</spage><epage>282</epage><pages>279-282</pages><issn>1567-5769</issn><eissn>1878-1705</eissn><abstract>We have prepared 125I-labeled cholera toxin B subunit (125I-labeled CT-B, a specific activity of 98Ci/mmol) and found that its binding to T and B lymphocytes from the blood of healthy donors was high-affinity (Kd 2.8 and 3.0nM, respectively). The binding of labeled protein was completely inhibited by unlabeled thymosin-α1 (TM-α1), interferon-α2 (IFN-α2), and the synthetic peptide LKEKK that corresponds to residues 16–20 in TM-α1 and 131–135 in IFN-α2, but was not inhibited by the synthetic peptide KKEKL with inverted amino acid sequence (Ki>10μM). Thus, TM-α1, IFN-α2, and the peptide: LKEKK bind with high affinity and specificity to CT-B receptor on donor blood T and B lymphocytes. It was found that CT-B and the peptide: LKEKK at concentrations of 10–1000nM increased in a dose-dependent manner the soluble guanylate cyclase activity in T and B lymphocytes.
[Display omitted]
•Cholera toxin B subunit binds with high affinity to human T and B lymphocytes.•TM-α1, INF-α2, peptide LKEKK completely inhibit the cholera toxin B subunit binding.•Residues 16–20 in TM-α1 and 131–135 in IFN-α2 are involved in binding to the receptor.•Binding to the receptor leads to an increase in activity of soluble guanylate cyclase.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>28719851</pmid><doi>10.1016/j.intimp.2017.07.011</doi><tpages>4</tpages></addata></record> |
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subjects | Affinity B-Lymphocytes - immunology B-Lymphocytes - metabolism Binding Blood Blood Cells - immunology Blood Cells - metabolism Cells, Cultured Cholera Cholera toxin Cholera Toxin - immunology Cholera Toxin - metabolism Cholera toxin B subunit Enzyme Activation Guanylate cyclase Guanylate Cyclase - metabolism Humans Infections Interferon Interferon-alpha - metabolism Lymphocyte Lymphocytes Lymphocytes B Lymphocytes T Peptide Peptide Fragments - metabolism Protein Protein Binding Proteins Public health Receptor Studies T-Lymphocytes - immunology T-Lymphocytes - metabolism Thymosin - analogs & derivatives Thymosin - metabolism Toxins Waterborne diseases |
title | Interaction of cholera toxin B subunit with T and B lymphocytes |
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