Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients
Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structu...
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| Veröffentlicht in: | Nature Structural Biology 2002-12, Vol.9 (12), p.918-921 |
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| creator | Imberty, Anne Mitchell, Edward Houles, Corinne Sudakevitz, Dvora Wimmerova, Michaela Gautier, Catherine Pérez, Serge Wu, Albert M Gilboa-Garber, Nechama |
| description | Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structure. Each monomer displays a nine-stranded, antiparallel b-sandwich arrangement and contains two close calcium cations that mediate the binding of fucose in a recognition mode unique among carbohydrate-protein interactions. Experimental binding studies, together with theoretical docking of fucose-containing oligosaccharides, are consistent with the assumption that antigens of the Lewis a (Lea) series may be the preferred ligands of this lectin. Precise knowledge of the lectin-binding site should allow a better design of new antibacterial-adhesion prophylactics. |
| doi_str_mv | 10.1038/nsb865 |
| format | Article |
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The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structure. Each monomer displays a nine-stranded, antiparallel b-sandwich arrangement and contains two close calcium cations that mediate the binding of fucose in a recognition mode unique among carbohydrate-protein interactions. Experimental binding studies, together with theoretical docking of fucose-containing oligosaccharides, are consistent with the assumption that antigens of the Lewis a (Lea) series may be the preferred ligands of this lectin. Precise knowledge of the lectin-binding site should allow a better design of new antibacterial-adhesion prophylactics.</description><identifier>ISSN: 1072-8368</identifier><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 2331-365X</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsb865</identifier><identifier>PMID: 12415289</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>Adhesins, Bacterial - chemistry ; Adhesins, Bacterial - metabolism ; Adhesion ; Bacterial Adhesion ; Binding Sites ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Calcium - chemistry ; Calcium - metabolism ; Cations ; Crystallography, X-Ray ; Cystic Fibrosis - microbiology ; Fucose - chemistry ; Fucose - metabolism ; Humans ; Lectins - chemistry ; Lectins - metabolism ; letter ; Life Sciences ; Lung - microbiology ; Macromolecular Substances ; Membrane Biology ; Models, Molecular ; Oligosaccharides - chemistry ; Oligosaccharides - metabolism ; Protein Binding ; Protein Structure ; Pseudomonas aeruginosa - pathogenicity</subject><ispartof>Nature Structural Biology, 2002-12, Vol.9 (12), p.918-921</ispartof><rights>Springer Nature America, Inc. 2002</rights><rights>Copyright Nature Publishing Group Dec 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c452t-ef0370067a1b1faf2012406e5a73d87c0bda0ab2e82e4b42c4c3e685b89efb543</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsb865$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsb865$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,778,782,27907,27908,41471,42540,51302</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12415289$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Imberty, Anne</creatorcontrib><creatorcontrib>Mitchell, Edward</creatorcontrib><creatorcontrib>Houles, Corinne</creatorcontrib><creatorcontrib>Sudakevitz, Dvora</creatorcontrib><creatorcontrib>Wimmerova, Michaela</creatorcontrib><creatorcontrib>Gautier, Catherine</creatorcontrib><creatorcontrib>Pérez, Serge</creatorcontrib><creatorcontrib>Wu, Albert M</creatorcontrib><creatorcontrib>Gilboa-Garber, Nechama</creatorcontrib><title>Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients</title><title>Nature Structural Biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Biol</addtitle><description>Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structure. Each monomer displays a nine-stranded, antiparallel b-sandwich arrangement and contains two close calcium cations that mediate the binding of fucose in a recognition mode unique among carbohydrate-protein interactions. Experimental binding studies, together with theoretical docking of fucose-containing oligosaccharides, are consistent with the assumption that antigens of the Lewis a (Lea) series may be the preferred ligands of this lectin. Precise knowledge of the lectin-binding site should allow a better design of new antibacterial-adhesion prophylactics.</description><subject>Adhesins, Bacterial - chemistry</subject><subject>Adhesins, Bacterial - metabolism</subject><subject>Adhesion</subject><subject>Bacterial Adhesion</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Calcium - chemistry</subject><subject>Calcium - metabolism</subject><subject>Cations</subject><subject>Crystallography, X-Ray</subject><subject>Cystic Fibrosis - microbiology</subject><subject>Fucose - chemistry</subject><subject>Fucose - metabolism</subject><subject>Humans</subject><subject>Lectins - chemistry</subject><subject>Lectins - metabolism</subject><subject>letter</subject><subject>Life Sciences</subject><subject>Lung - microbiology</subject><subject>Macromolecular Substances</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Oligosaccharides - 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Academic</collection><jtitle>Nature Structural Biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Imberty, Anne</au><au>Mitchell, Edward</au><au>Houles, Corinne</au><au>Sudakevitz, Dvora</au><au>Wimmerova, Michaela</au><au>Gautier, Catherine</au><au>Pérez, Serge</au><au>Wu, Albert M</au><au>Gilboa-Garber, Nechama</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients</atitle><jtitle>Nature Structural Biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>2002-12-01</date><risdate>2002</risdate><volume>9</volume><issue>12</issue><spage>918</spage><epage>921</epage><pages>918-921</pages><issn>1072-8368</issn><issn>1545-9993</issn><eissn>2331-365X</eissn><eissn>1545-9985</eissn><abstract>Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structure. Each monomer displays a nine-stranded, antiparallel b-sandwich arrangement and contains two close calcium cations that mediate the binding of fucose in a recognition mode unique among carbohydrate-protein interactions. Experimental binding studies, together with theoretical docking of fucose-containing oligosaccharides, are consistent with the assumption that antigens of the Lewis a (Lea) series may be the preferred ligands of this lectin. Precise knowledge of the lectin-binding site should allow a better design of new antibacterial-adhesion prophylactics.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>12415289</pmid><doi>10.1038/nsb865</doi><tpages>4</tpages></addata></record> |
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| subjects | Adhesins, Bacterial - chemistry Adhesins, Bacterial - metabolism Adhesion Bacterial Adhesion Binding Sites Biochemistry Biological Microscopy Biomedical and Life Sciences Calcium - chemistry Calcium - metabolism Cations Crystallography, X-Ray Cystic Fibrosis - microbiology Fucose - chemistry Fucose - metabolism Humans Lectins - chemistry Lectins - metabolism letter Life Sciences Lung - microbiology Macromolecular Substances Membrane Biology Models, Molecular Oligosaccharides - chemistry Oligosaccharides - metabolism Protein Binding Protein Structure Pseudomonas aeruginosa - pathogenicity |
| title | Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients |
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