Helicobacter pylori Interacts with the Human Single-Domain Trefoil Protein TFF1
Why Helicobacter pylori colonizes only gastric tissue is unknown. It is found on gastric mucus-secreting cells and in the overlying gastric mucus but not deep in gastric glands. This localization mirrors the expression of trefoil factor 1, TFF1. We hypothesized that H. pylori interacting with TFF1 c...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2004-05, Vol.101 (19), p.7409-7414 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Clyne, Marguerite Dillon, Paul Daly, Stephen O'Kennedy, Richard Felicity E. B. May Westley, Bruce R. Drumm, Brendan Falkow, Stanley |
| description | Why Helicobacter pylori colonizes only gastric tissue is unknown. It is found on gastric mucus-secreting cells and in the overlying gastric mucus but not deep in gastric glands. This localization mirrors the expression of trefoil factor 1, TFF1. We hypothesized that H. pylori interacting with TFF1 could explain the tropism of this bacteria for gastric tissue. Recombinant human TFF1 expressed in Escherichia coli was purified by affinity chromatography, ion-exchange chromatography, and gel filtration. Binding of H. pylori was assessed by using flow cytometry and the BIAcore system, which allows real-time monitoring of molecular interactions. In flow cytometry, H. pylori bound to the TFF1 dimer, but Campylobacter jejuni strains and the laboratory strain of E. coli, HB101, did not bind. When the BIAcore system was used, H. pylori bound strongly to TFF1-coated dextran chips compared with uncoated chips. Binding was inhibited by a TFF1 monoclonal antibody and by soluble TFF1. H. pylori bound to porcine gastric mucin only if it was pretreated with TFF1. In conclusion, H. pylori interacts avidly with the dimeric form of TFF1, and this interaction enables binding to gastric mucin, suggesting that TFF1 may act as a receptor for the organism in vivo. This interaction may underline the previously unexplained tropism of this organism for gastric tissue and its colocalization with the gastric mucin MUC5AC. |
| doi_str_mv | 10.1073/pnas.0308489101 |
| format | Article |
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B. May ; Westley, Bruce R. ; Drumm, Brendan ; Falkow, Stanley</creator><creatorcontrib>Clyne, Marguerite ; Dillon, Paul ; Daly, Stephen ; O'Kennedy, Richard ; Felicity E. B. May ; Westley, Bruce R. ; Drumm, Brendan ; Falkow, Stanley</creatorcontrib><description>Why Helicobacter pylori colonizes only gastric tissue is unknown. It is found on gastric mucus-secreting cells and in the overlying gastric mucus but not deep in gastric glands. This localization mirrors the expression of trefoil factor 1, TFF1. We hypothesized that H. pylori interacting with TFF1 could explain the tropism of this bacteria for gastric tissue. Recombinant human TFF1 expressed in Escherichia coli was purified by affinity chromatography, ion-exchange chromatography, and gel filtration. Binding of H. pylori was assessed by using flow cytometry and the BIAcore system, which allows real-time monitoring of molecular interactions. In flow cytometry, H. pylori bound to the TFF1 dimer, but Campylobacter jejuni strains and the laboratory strain of E. coli, HB101, did not bind. When the BIAcore system was used, H. pylori bound strongly to TFF1-coated dextran chips compared with uncoated chips. Binding was inhibited by a TFF1 monoclonal antibody and by soluble TFF1. H. pylori bound to porcine gastric mucin only if it was pretreated with TFF1. In conclusion, H. pylori interacts avidly with the dimeric form of TFF1, and this interaction enables binding to gastric mucin, suggesting that TFF1 may act as a receptor for the organism in vivo. This interaction may underline the previously unexplained tropism of this organism for gastric tissue and its colocalization with the gastric mucin MUC5AC.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0308489101</identifier><identifier>PMID: 15123808</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Bacteria ; Biological Sciences ; Campylobacter jejuni ; Chromatography ; Dimerization ; Dimers ; Escherichia coli ; Gastric mucin ; Gastric Mucosa - microbiology ; Helicobacter pylori ; Helicobacter pylori - physiology ; Humans ; Infections ; Latex ; Lewis Blood Group Antigens ; Microbiology ; Mucins ; Mucus ; Proteins ; Proteins - chemistry ; Proteins - metabolism ; Receptors ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Sensors ; Stomach ; Surface Plasmon Resonance ; Trefoil Factor-1 ; Tumor Suppressor Proteins</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2004-05, Vol.101 (19), p.7409-7414</ispartof><rights>Copyright 1993/2004 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences May 11, 2004</rights><rights>Copyright © 2004, The National Academy of Sciences 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c524t-743dd3d6bfc3b29a4700ef960d5d66bd8047b98e437de86baeb199264109afc63</citedby><cites>FETCH-LOGICAL-c524t-743dd3d6bfc3b29a4700ef960d5d66bd8047b98e437de86baeb199264109afc63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/101/19.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3371879$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3371879$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15123808$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Clyne, Marguerite</creatorcontrib><creatorcontrib>Dillon, Paul</creatorcontrib><creatorcontrib>Daly, Stephen</creatorcontrib><creatorcontrib>O'Kennedy, Richard</creatorcontrib><creatorcontrib>Felicity E. B. May</creatorcontrib><creatorcontrib>Westley, Bruce R.</creatorcontrib><creatorcontrib>Drumm, Brendan</creatorcontrib><creatorcontrib>Falkow, Stanley</creatorcontrib><title>Helicobacter pylori Interacts with the Human Single-Domain Trefoil Protein TFF1</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Why Helicobacter pylori colonizes only gastric tissue is unknown. It is found on gastric mucus-secreting cells and in the overlying gastric mucus but not deep in gastric glands. This localization mirrors the expression of trefoil factor 1, TFF1. We hypothesized that H. pylori interacting with TFF1 could explain the tropism of this bacteria for gastric tissue. Recombinant human TFF1 expressed in Escherichia coli was purified by affinity chromatography, ion-exchange chromatography, and gel filtration. Binding of H. pylori was assessed by using flow cytometry and the BIAcore system, which allows real-time monitoring of molecular interactions. In flow cytometry, H. pylori bound to the TFF1 dimer, but Campylobacter jejuni strains and the laboratory strain of E. coli, HB101, did not bind. When the BIAcore system was used, H. pylori bound strongly to TFF1-coated dextran chips compared with uncoated chips. Binding was inhibited by a TFF1 monoclonal antibody and by soluble TFF1. H. pylori bound to porcine gastric mucin only if it was pretreated with TFF1. In conclusion, H. pylori interacts avidly with the dimeric form of TFF1, and this interaction enables binding to gastric mucin, suggesting that TFF1 may act as a receptor for the organism in vivo. This interaction may underline the previously unexplained tropism of this organism for gastric tissue and its colocalization with the gastric mucin MUC5AC.</description><subject>Bacteria</subject><subject>Biological Sciences</subject><subject>Campylobacter jejuni</subject><subject>Chromatography</subject><subject>Dimerization</subject><subject>Dimers</subject><subject>Escherichia coli</subject><subject>Gastric mucin</subject><subject>Gastric Mucosa - microbiology</subject><subject>Helicobacter pylori</subject><subject>Helicobacter pylori - physiology</subject><subject>Humans</subject><subject>Infections</subject><subject>Latex</subject><subject>Lewis Blood Group Antigens</subject><subject>Microbiology</subject><subject>Mucins</subject><subject>Mucus</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Receptors</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sensors</subject><subject>Stomach</subject><subject>Surface Plasmon Resonance</subject><subject>Trefoil Factor-1</subject><subject>Tumor Suppressor Proteins</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EokvhzAVBxKHqJe34I7F94IBKt1upUpEoZ8tJnK5XTrzYDtD_Hke76gIHOI1m_Hsjv3kIvcZwhoHT8-2o4xlQEExIDPgJWmCQuKyZhKdoAUB4KRhhR-hFjBsAkJWA5-gIV5hQAWKBblfG2dY3uk0mFNsH54Mtrsfc5Eksfti0LtLaFKtp0GPxxY73zpSf_KDtWNwF03vris_BJzP3yyV-iZ712kXzal-P0dfl5d3Fqry5vbq--HhTthVhqeSMdh3t6qZvaUOkZhzA9LKGrurquukEMN5IYRjlnRF1o02DpSQ1y_Z039b0GH3Y7d1OzWC61owpaKe2wQ46PCivrfrzZbRrde-_KwZSUpL1J3t98N8mE5MabGyNc3o0foqKY0lACv5fEHNBCCYz-P4vcOOnMOYjKAKYyKqSIkPnO6gNPsZ8v8cfY1BzompOVB0SzYq3vxs98PsIM3C6B2blYR1WWCqe7ap-ci6Znymj7_6NZuLNjtjE5MMjQinHgkv6C6tWviA</recordid><startdate>20040511</startdate><enddate>20040511</enddate><creator>Clyne, Marguerite</creator><creator>Dillon, Paul</creator><creator>Daly, Stephen</creator><creator>O'Kennedy, Richard</creator><creator>Felicity E. 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B. May</au><au>Westley, Bruce R.</au><au>Drumm, Brendan</au><au>Falkow, Stanley</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Helicobacter pylori Interacts with the Human Single-Domain Trefoil Protein TFF1</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2004-05-11</date><risdate>2004</risdate><volume>101</volume><issue>19</issue><spage>7409</spage><epage>7414</epage><pages>7409-7414</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Why Helicobacter pylori colonizes only gastric tissue is unknown. It is found on gastric mucus-secreting cells and in the overlying gastric mucus but not deep in gastric glands. This localization mirrors the expression of trefoil factor 1, TFF1. We hypothesized that H. pylori interacting with TFF1 could explain the tropism of this bacteria for gastric tissue. Recombinant human TFF1 expressed in Escherichia coli was purified by affinity chromatography, ion-exchange chromatography, and gel filtration. Binding of H. pylori was assessed by using flow cytometry and the BIAcore system, which allows real-time monitoring of molecular interactions. In flow cytometry, H. pylori bound to the TFF1 dimer, but Campylobacter jejuni strains and the laboratory strain of E. coli, HB101, did not bind. When the BIAcore system was used, H. pylori bound strongly to TFF1-coated dextran chips compared with uncoated chips. Binding was inhibited by a TFF1 monoclonal antibody and by soluble TFF1. H. pylori bound to porcine gastric mucin only if it was pretreated with TFF1. In conclusion, H. pylori interacts avidly with the dimeric form of TFF1, and this interaction enables binding to gastric mucin, suggesting that TFF1 may act as a receptor for the organism in vivo. This interaction may underline the previously unexplained tropism of this organism for gastric tissue and its colocalization with the gastric mucin MUC5AC.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>15123808</pmid><doi>10.1073/pnas.0308489101</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bacteria Biological Sciences Campylobacter jejuni Chromatography Dimerization Dimers Escherichia coli Gastric mucin Gastric Mucosa - microbiology Helicobacter pylori Helicobacter pylori - physiology Humans Infections Latex Lewis Blood Group Antigens Microbiology Mucins Mucus Proteins Proteins - chemistry Proteins - metabolism Receptors Recombinant Proteins - chemistry Recombinant Proteins - metabolism Sensors Stomach Surface Plasmon Resonance Trefoil Factor-1 Tumor Suppressor Proteins |
| title | Helicobacter pylori Interacts with the Human Single-Domain Trefoil Protein TFF1 |
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