{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T21:07:32Z","timestamp":1790716052059,"version":"4.1.0"},"reference-count":54,"publisher":"American Chemical Society (ACS)","issue":"20","license":[{"start":{"date-parts":[[2019,10,10]],"date-time":"2019-10-10T00:00:00Z","timestamp":1570665600000},"content-version":"vor","delay-in-days":371,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003329","name":"Ministerio de Econom\u00eda y Competitividad","doi-asserted-by":"publisher","award":["BFU2015-70052-R"],"award-info":[{"award-number":["BFU2015-70052-R"]}],"id":[{"id":"10.13039\/501100003329","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004587","name":"Instituto de Salud Carlos III","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/501100004587","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"Ministerio de Ciencia, Inovaci\u00f3n y Universidades","doi-asserted-by":"publisher","award":["BIO2017-89081-R"],"award-info":[{"award-number":["BIO2017-89081-R"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2018,10,16]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Many pathogens use host glycans as docking points for adhesion. Therefore, the use of compounds blocking carbohydrate-binding adhesins is a promising strategy for fighting infections. In this work, we describe a simple and rapid microarray approach for assessing the bacterial adhesion and efficiency of antiadhesive compounds targeting uropathogenic Escherichia coli UTI89, which displays mannose-specific adhesin FimH at the tip of fimbriae. The approach consisted in direct detection of live fluorescently labeled bacteria bound to mannan printed onto microarray slides. The utility of the arrays for binding\/inhibition assays was first validated by comparing array-derived results for the model mannose-binding lectin concanavalin A with data obtained by isothermal titration calorimetry. Growth phase-dependent binding of UTI89 to the arrays was observed, proving the usefulness of the setup for detecting differences in FimH expression. Importantly, bacteria labeling and binding assays entailed minimal manipulation, helping to preserve the integrity of fimbriae. The efficiency of three different dodecamannosylated fullerenes as FimH-targeted antiadhesives was next evaluated in competition assays. The results revealed a superior activity of the mannofullerenes (5- to 18-fold per mannose residue) over methyl \u03b1-d-mannopyranoside. Moreover, differences in activity were detected for mannofullerenes differing in the structure\/length of the spacer used for grafting mannose onto the fullerene core, further demonstrating the sensitivity of the assay. Overall, the approach combines straightforward and time-saving protocols for microarray preparation, bacteria labeling, and binding assays, and it can be easily tailored to other bacteria bearing carbohydrate-binding adhesins.<\/jats:p>","DOI":"10.1021\/acs.analchem.8b04235","type":"journal-article","created":{"date-parts":[[2018,10,4]],"date-time":"2018-10-04T12:04:43Z","timestamp":1538654683000},"page":"12314-12321","source":"Crossref","is-referenced-by-count":21,"title":["Direct Evaluation of Live Uropathogenic\n                    <i>Escherichia coli<\/i>\n                    Adhesion and Efficiency of Antiadhesive Compounds Using\na Simple Microarray Approach"],"prefix":"10.1021","volume":"90","author":[{"given":"Ioanna","family":"Kalograiaki","sequence":"first","affiliation":[{"name":"Instituto de Qui\u0301mica Fi\u0301sica Rocasolano, CSIC , Serrano 119 , ,","place":["Madrid, Spain, 28006"]},{"name":"CIBER de Enfermedades Respiratorias (CIBERES) , Avda Monforte de Lemos 3-5 , ,","place":["Madrid, Spain, 28029"]},{"name":"Centro de Investigaciones Biolo\u0301gicas, CSIC , Ramiro de Maeztu 9 , ,","place":["Madrid, Spain, 28040"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Abella\u0301n-Flos","sequence":"additional","affiliation":[{"name":"University of Namur (UNamur) , , Rue de Bruxelles 61 , ,","place":["Namur, Belgium, B-5000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luis A\u0301ngel","family":"Ferna\u0301ndez","sequence":"additional","affiliation":[{"name":"Centro Nacional de Biotecnologi\u0301a (CNB), CSIC , Darwin 3, Campus UAM Cantoblanco , ,","place":["Madrid, Spain, 28049"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Margarita","family":"Mene\u0301ndez","sequence":"additional","affiliation":[{"name":"Instituto de Qui\u0301mica Fi\u0301sica Rocasolano, CSIC , Serrano 119 , ,","place":["Madrid, Spain, 28006"]},{"name":"CIBER de Enfermedades Respiratorias (CIBERES) , Avda Monforte de Lemos 3-5 , ,","place":["Madrid, Spain, 28029"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ste\u0301phane P.","family":"Vincent","sequence":"additional","affiliation":[{"name":"University of Namur (UNamur) , , Rue de Bruxelles 61 , ,","place":["Namur, Belgium, B-5000"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8148-1875","authenticated-orcid":true,"given":"Dolores","family":"Soli\u0301s","sequence":"additional","affiliation":[{"name":"Instituto de Qui\u0301mica Fi\u0301sica Rocasolano, CSIC , Serrano 119 , ,","place":["Madrid, Spain, 28006"]},{"name":"CIBER de Enfermedades Respiratorias (CIBERES) , Avda Monforte de Lemos 3-5 , ,","place":["Madrid, Spain, 28029"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2018,10,4]]},"reference":[{"key":"2026090119382207100_cit1","doi-asserted-by":"publisher","first-page":"298","DOI":"10.1016\/j.tibs.2011.01.005","article-title":"From lectin\nstructure to functional glycomics: principles\nof the sugar code","volume":"36","author":"Gabius","year":"2011","journal-title":"Trends Biochem. 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Microbiol."},{"key":"2026090119382207100_cit6","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1038\/d41586-017-08323-0","article-title":"Deploy vaccines to\nfight superbugs","volume":"552","author":"Rappuoli","year":"2017","journal-title":"Nature"},{"key":"2026090119382207100_cit7","doi-asserted-by":"publisher","first-page":"7173","DOI":"10.1039\/C4RA14570D","article-title":"Bacteria microarrays\nas sensitive tools for exploring pathogen surface epitopes and recognition\nby host receptors","volume":"5","author":"Campanero-Rhodes","year":"2015","journal-title":"RSC Adv."},{"key":"2026090119382207100_cit8","doi-asserted-by":"publisher","first-page":"5950","DOI":"10.1021\/acs.analchem.6b00905","article-title":"Combined Bacteria\nMicroarray and Quartz Crystal Microbalance approach for exploring\nglycosignatures of nontypeable Haemophilus influenzae and recognition\nby host lectins","volume":"88","author":"Kalograiaki","year":"2016","journal-title":"Anal. Chem."},{"key":"2026090119382207100_cit9","first-page":"37","article-title":"Chapter Two -\nBacterial Surface Glycans: Microarray and QCM Strategies for Glycophenotyping\nand Exploration of Recognition by Host Receptors","volume-title":"Methods in Enzymology","author":"Kalograiaki","year":"2018"},{"key":"2026090119382207100_cit10","unstructured":"World Health Organisation.\n          \n          http:\/\/www.who.int\/mediacentre\/factsheets\/fs194\/en\/ (accessed\nJan, 2018)."},{"key":"2026090119382207100_cit11","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1007\/128_2008_13","article-title":"Structure, Function,\nand Assembly of Type 1 Fimbriae","volume-title":"Glycoscience\nand Microbial Adhesion","author":"Knight","year":"2009"},{"key":"2026090119382207100_cit12","doi-asserted-by":"publisher","first-page":"1566","DOI":"10.1172\/JCI30504","article-title":"CEACAM6 acts\nas a receptor for adherent-invasive E. coli, supporting\nileal mucosa colonization in Crohn disease","volume":"117","author":"Barnich","year":"2007","journal-title":"J. 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Biochem."},{"key":"2026090119382207100_cit50","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1006\/abbi.2000.2031","article-title":"Conformational\nstudies of the Man8 oligosaccharide on native ribonuclease B and on\nthe reduced and denatured protein","volume":"383","author":"Gonza\u0301lez","year":"2000","journal-title":"Arch. Biochem.\nBiophys."},{"key":"2026090119382207100_cit51","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1111\/j.1365-2958.2004.04415.x","article-title":"Receptor binding studies disclose\na novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin","volume":"55","author":"Bouckaert","year":"2005","journal-title":"Mol. Microbiol."},{"key":"2026090119382207100_cit52","doi-asserted-by":"publisher","first-page":"645","DOI":"10.1016\/j.cell.2010.03.038","article-title":"Structural basis for mechanical force\nregulation of the adhesin FimH via finger trap-like \u03b2 sheet\ntwisting","volume":"141","author":"Le Trong","year":"2010","journal-title":"Cell"},{"key":"2026090119382207100_cit53","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1021\/bc4005365","article-title":"Structure binding relationship\nof galactosylated glycoclusters toward Pseudomonas aeruginosa lectin LecA using a DNA-based carbohydrate microarray","volume":"25","author":"Gerland","year":"2014","journal-title":"Bioconjugate Chem."},{"key":"2026090119382207100_cit54","doi-asserted-by":"publisher","first-page":"5135","DOI":"10.1039\/C7OB00889A","article-title":"An oxime-based glycocluster microarray","volume":"15","author":"Hoang","year":"2017","journal-title":"Org. Biomol. 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