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Bacterial adhesin

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87: 560:. MAMs contain tandem repeats of mammalian cell entry (MCE) domains which specifically bind to extracellular matrix proteins and anionic lipids on host tissues. Since they are abundant in many pathogens of clinical importance, Multivalent Adhesion Molecules are a potential target for prophylactic or therapeutic anti-infectives. The use of a MAM targeting adhesion inhibitor was shown to significantly decrease the colonization of burn wounds by multidrug resistant 79:. In the crudest sense, bacterial adhesins serve as anchors allowing bacteria to overcome these environmental shear forces, thus remaining in their desired environment. However, bacterial adhesins do not serve as a sort of universal bacterial Velcro. Rather, they act as specific surface recognition molecules, allowing the targeting of a particular bacterium to a particular surface such as root tissue in plants, 357: 171:. The bacterial adhesin consists primarily of an intramembranous structural protein which provides a scaffold upon which several extracellular adhesins may be attached. However, as in the case of the CFA1 fimbriae, the structural protein itself can sometimes act as an adhesin if a portion of the protein extends into the 297:
A number of problems create challenges for the researcher exploring the anti-adhesin immunity concept. First, a large number of different bacterial adhesins target the same human tissues. Further, an individual bacterium can produce multiple different types of adhesin, at different times, in
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links the two domains. Additionally, a carbohydrate-binding pocket has been identified at the tip of the N-terminal adhesive domain. This basic structure is conserved across type 1 fimbrial adhesins though recent studies have shown that in vitro induced mutations can lead to the addition of
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Langermann S, Möllby R, Burlein J, Palaszynski S, Auguste C, DeFusco A, Strouse R, Schenerman M, Hultgren S, Pinkner J, Winberg J, Guldevall L, Söderhäll M, Ishikawa K, Normark S, Koenig S (2000). "Vaccination with FimH adhesin protects cynomolgus monkeys from colonization and infection by
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Through the mechanisms of evolution, different species of bacteria have developed different solutions to the problem of attaching receptor specific proteins to the bacteria surface. Today many different types and subclasses of bacterial adhesins may be observed in the literature.
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FimH provides an example of conformation specific immune response which enhances impact on the protein. By studying this particular adhesion, researchers hope to develop adhesion-specific vaccines which may serve as a model for antibody-mediation of pathogen adhesion.
216:. "A large number of bacterial adhesins with individual receptor specificities have been identified." Many bacterial pathogens are able to express an array of different adhesins. Expression of these adhesins at different phases during 510:
to the urinary tract. They do so by inducing the development of long cellular extensions that wrap around the bacteria. They also confer the mannose-resistant hemaglutination phenotype, which can be inhibited by
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strains most known for causing diarrhea can be found in the intestinal tissue of pigs and humans where they express the K88 and CFA1. to attach to the intestinal lining. Additionally, UPEC causes about 90% of
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then processes the protein by removing several signal peptides ultimately leaving a 279 amino acid protein. Mature FimH is displayed on the bacterial surface as a component of the type 1 fimbrial organelle.
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adhesins FHA and pertactin are components of three of the four acellular pertussis vaccines currently licensed for use in the U.S. Additionally, anti-adhesion vaccines are being explored as a solution to
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comes from early studies which indicated that an important component of protective immunity against certain bacteria came from an ability to prevent adhesin binding. Additionally, adhesins are attractive
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play the most important role in adhesion based virulence. Numerous studies have shown that inhibiting a single adhesin in this coordinated effort can often be enough to make a pathogenic bacterium
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different places, and in response to different environmental triggers. Finally, many adhesins present as different immunologically distinct antigenic varieties, even within the same
199:. FimH is folded into two domains. The N terminal adhesive domain plays the main role in surface recognition while the C-terminal domain is responsible for organelle integration. A 271:
during the first three years of life. If the child survives this initial period of susceptibility, infection rates typically drop substantially. Field studies show that this
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Huebinger, Ryan M.; Stones, Daniel H.; de Souza Santos, Marcela; Carlson, Deborah L.; Song, Juquan; Vaz, Diana Pereira; Keen, Emma; Wolf, Steven E.; Orth, Kim (2016-12-20).
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overcomes the antibody based immune response by natural conversion from the high to the low affinity state. Through this conversion, FimH adhesion may shed the
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Bacteria are typically found attached to and living in close association with surfaces. During the bacterial lifespan, a bacterium is subjected to frequent
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surface layer serves as the specific adhesin. To effectively achieve adherence to host surfaces, many bacteria produce multiple adherence factors called
1182:"Distribution of drb genes coding for Dr binding adhesins among uropathogenic and fecal Escherichia coli isolates and identification of new subtypes" 515:. The N-terminal portion of the mature protein is thought to be responsible for chloramphenicol sensitivity. Also, they induce activation of several 879:
Choudhury D, Thompson A, Stojanoff V, et al. (August 1999). "X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic
1280:"Outer membrane adhesion factor multivalent adhesion molecule 7 initiates host cell binding during infection by gram-negative pathogens" 294:
consumption. This research has opened the door to further exploration of orally administered vaccines which exploit bacterial adhesins.
1167: 1231:"Molecular structure of the Dr adhesin: nucleotide sequence and mapping of receptor-binding domain by use of fusion constructs" 585:
virulence factors." These studies have shown that only strains capable of expressing fimbriae are pathogenic. High survival of
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Adhesins are also used in cell communication, and bind to surface communicators. Can also be used to bind to other bacteria.
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stems from observations of human acquired immunity. Children in third world countries may suffer from several episodes of
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C-terminal domain specificity resulting in a bacterial adhesion with dual bending sites and related binding phenotypes.
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or adherence to other cells or to surfaces, usually in the host they are infecting or living in. Adhesins are a type of
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Multivalent Adhesion Molecules (MAMs) are a widespread family of adhesins found in Gram negative bacteria, including
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candidates because they are often essential to infection and are surface-located, making them readily accessible to
1347:"Targeting bacterial adherence inhibits multidrug-resistant Pseudomonas aeruginosa infection following burn injury" 656: 279: 224:. This has led to the exploration of adhesin activity interruption as a method of bacterial infection treatment. 504: 253: 601:
phagocytic activity. This action facilitates the spread of the pathogen throughout the epithelial cell layer.
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is host restricted almost entirely to humans. "Extensive studies have established type 4 fimbrial adhesins of
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Despite these challenges, progress is being made in the creation of anti-adhesion vaccines. In animal models,
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The best characterized bacterial adhesin is the type 1 fimbrial FimH adhesin. This adhesin is responsible for
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Kline, Kimberly A.; Fälker, Stefan; Dahlberg, Sofia; Normark, Staffan; Henriques-Normark, Birgitta (2009).
1006:"Oral consumption of cranberry juice cocktail inhibits molecular-scale adhesion of clinical uropathogenic 328:(UTIs). The use of synthetic FimH adhesion peptides was shown to prevent urogenital mucosal infection by 1610: 453: 56: 496: 489: 1170:, State Key Laboratory for Moleclular Virology and Genetic Engineering, Beijing. Retrieved July 2011 1589: 151:
in addition to a bacterium's ability to produce toxins and resist the immune defenses of the host.
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at the tip of the fimbriae that is the actual adhesin. In gram-positive bacteria, a protein or
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Levine, M. M.; Giron, J. A.; Noriega, E. R. (1994). "Fimbrial vaccines". In Klemm, Per (ed.).
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Coutte L, Alonso S, Reveneau N, Willery E, Quatannens B, Locht C, Jacob-Dubuisson F (2003).
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Langermann S, Palaszynski S, Barnhart M, et al. (April 1997). "Prevention of mucosal
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The majority of bacterial pathogens exploit specific adhesion to host cells as their main
8: 516: 200: 1529:"Type 1 fimbrial adhesin FimH elicits an immune response that enhances cell adhesion of 1427: 1362: 1295: 939: 1557: 1528: 1446: 1411: 1387: 1346: 1322: 1279: 1034: 1005: 754: 729: 701: 676: 1499: 1470: 1255: 1230: 1206: 1181: 956: 919: 813: 503:
contain both fimbriated and afimbriated adherence structures and mediate adherence of
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sensitive adhesion. The bacterium synthesizes a precursor protein consisting of 300
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Klemm P, Schembri MA (March 2000). "Bacterial adhesins: function and structure".
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Proceedings of the National Academy of Sciences of the United States of America
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Zhang L, Foxman B, Tallman P, Cladera E, Le Bouguenec C, Marrs CF (June 1997).
853: 836: 651: 531: 125: 80: 60: 1599: 1378: 1313: 117: 1304: 730:"Targeting the bacteria-host interface: strategies in anti-adhesion therapy" 1566: 1455: 1396: 1331: 1108: 1043: 904: 862: 821: 763: 710: 76: 48: 1508: 1264: 1215: 1147: 1025: 965: 677:"Role of adhesin release for mucosal colonization by a bacterial pathogen" 593:
infections. Additionally, recent studies out of Stockholm have shown that
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Davies, J. K.; Koomey, J. M.; Seifert, H. S. (1994). "Pili (fimbriae) of
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researchers have shown that adhesion forces decrease with time following
144: 63:. Adhesion and bacterial adhesins are also a potential target either for 1056: 978: 745: 188: 140: 120:
bacteria function as adhesins, but in many cases it is a minor subunit
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are cell-surface components or appendages of bacteria that facilitate
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can hitchhike on PMNs using their adhesin pili thus hiding them from
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to bind to host cells and their receptors (here: the human proteins
1412:"Pathogenic Neisseria hitchhike on the uropod of human neutrophils" 1100: 725: 634: 527: 405: 268: 249: 242: 45: 31: 1527:
Tchesnokova V, Aprikian P, Kisiela D, et al. (October 2011).
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Krachler, Anne Marie; Ham, Hyeilin; Orth, Kim (2011-07-12).
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Swanson TN, Bilge SS, Nowicki B, Moseley SL (January 1991).
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Fimbriae : adhesion, genetics, biogenesis, and vaccines
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Fimbriae : adhesion, genetics, biogenesis, and vaccines
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The Dr family of adhesins are particularly associated with
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significantly reduced colonization by UPEC. Moreover, the
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The typical structure of a bacterial adhesin is that of a
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FimH is a bacterial adhesin that helps bacteria such as
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Tao Y, PinzĂłn-Arango PA, Howell AB, Camesano TA (2011).
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infection by FimH-adhesin-based systemic vaccination".
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Identified Virulence Factors of UPEC : Adherence
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The study of adhesins as a point of exploitation for
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is illustrated by studies with FimH, the adhesin of
1410:Söderholm N, Vielfort K, Hultenby K, Aro H (2011). 315:with anti FimH-antibodies and vaccination with the 275:is directed primarily against bacterial adhesins. 837:"Bacterial Adhesins in Host-Microbe Interactions" 1597: 795: 793: 195:In 1999, the structure of FimH was resolved via 1468: 1277: 1079: 791: 789: 787: 785: 783: 781: 779: 777: 775: 773: 286:may inhibit the action of UPEC adhesins. Using 1522: 1520: 1518: 147:. This prevalence marks them as key microbial 135:Bacterial adhesins provide species and tissue 67:or for the treatment of bacterial infections. 917: 799: 227: 770: 723: 1515: 1222: 1173: 1065:. Boca Raton: CRC Press. pp. 147–155. 983:. Boca Raton: CRC Press. pp. 255–270. 874: 872: 1115: 668: 355: 83:tissues in mammals, or even tooth enamel. 1588:at the U.S. National Library of Medicine 1556: 1498: 1445: 1435: 1403: 1386: 1321: 1303: 1254: 1205: 1033: 955: 852: 753: 700: 178: 869: 85: 1462: 997: 911: 657:Trimeric autotransporter adhesins (TAA) 629:, 95% express type 1 fimbriae. FimH in 207: 14: 1598: 1163: 1161: 1159: 1157: 1050: 972: 1469:Gaastra W, de Graaf FK (June 1982). 920:"Heterobinary adhesins based on the 337: 1154: 24: 519:cascades, including activation of 361:drae adhesin from escherichia coli 248:The effectiveness of anti-adhesin 25: 1622: 1579: 1087:uropathogenic Escherichia coli". 918:Schembri MA, Klemm P (May 1998). 567: 139:. Adhesins are expressed by both 1338: 1271: 1198:10.1128/iai.65.6.2011-2018.1997 948:10.1128/AEM.64.5.1628-1633.1998 280:Worcester Polytechnic Institute 828: 717: 539:Multivalent Adhesion Molecules 13: 1: 1247:10.1128/iai.59.1.261-268.1991 897:10.1126/science.285.5430.1061 814:10.1016/S1438-4221(00)80102-2 662: 587:polymorphonuclear neutrophils 421:Available protein structures: 282:show that the consumption of 154: 70: 1491:10.1128/mr.46.2.129-161.1982 1437:10.1371/journal.pone.0024353 1140:10.1126/science.276.5312.607 342: 7: 645: 10: 1627: 854:10.1016/j.chom.2009.05.011 604: 228:Vaccines based on adhesins 530:and pregnancy-associated 497:decay-accelerating factor 463: 443: 425: 420: 416: 404: 391: 379: 371: 366: 354: 349: 1590:Medical Subject Headings 1061:". In Klemm, Per (ed.). 928:Appl. Environ. Microbiol 619:urinary tract infections 44:is an essential step in 1305:10.1073/pnas.1102360108 841:Cell Host & Microbe 326:urinary tract infection 288:atomic force microscopy 1235:Infection and Immunity 1186:Infection and Immunity 924:FimH fimbrial protein" 802:Int. J. Med. Microbiol 562:Pseudomonas aeruginosa 558:Pseudomonas aeruginosa 179:FimH adhesin—structure 109: 1059:Neisseria gonorrhoeae 1026:10.1089/jmf.2010.0154 591:Neisseria gonorrhoeae 589:(PMNs) characterizes 483:Dr family of adhesins 305:Neisseria gonorrhoeae 197:x-ray crystallography 89: 1549:10.1128/IAI.05169-11 693:10.1084/jem.20021153 321:Bordetella pertussis 313:passive immunization 278:Recent studies from 208:As virulence factors 145:saprophytic bacteria 1428:2011PLoSO...624353S 1363:2016NatSR...639341H 1296:2011PNAS..10811614K 1290:(28): 11614–11619. 940:1998ApEnM..64.1628S 517:signal transduction 302:(as is the case in 141:pathogenic bacteria 1351:Scientific Reports 746:10.4161/viru.24606 259:(UPEC). Work with 201:tetra-peptide loop 110: 28:Bacterial adhesins 1611:Virulence factors 1586:Bacterial+Adhesin 1371:10.1038/srep39341 479: 478: 475: 474: 470:structure summary 338:Specific examples 273:acquired immunity 149:virulence factors 16:(Redirected from 1618: 1571: 1570: 1560: 1543:(10): 3895–904. 1531:Escherichia coli 1524: 1513: 1512: 1502: 1473:Escherichia coli 1466: 1460: 1459: 1449: 1439: 1407: 1401: 1400: 1390: 1342: 1336: 1335: 1325: 1307: 1275: 1269: 1268: 1258: 1226: 1220: 1219: 1209: 1177: 1171: 1165: 1152: 1151: 1134:(5312): 607–11. 1124:Escherichia coli 1119: 1113: 1112: 1083: 1077: 1076: 1054: 1048: 1047: 1037: 1008:Escherichia coli 1001: 995: 994: 976: 970: 969: 959: 922:Escherichia coli 915: 909: 908: 891:(5430): 1061–6. 881:Escherichia coli 876: 867: 866: 856: 832: 826: 825: 797: 768: 767: 757: 721: 715: 714: 704: 672: 639:Escherichia coli 613:Escherichia coli 507:Escherichia coli 418: 417: 359: 347: 346: 256:Escherichia coli 214:virulence factor 93:Escherichia coli 36:virulence factor 21: 1626: 1625: 1621: 1620: 1619: 1617: 1616: 1615: 1596: 1595: 1582: 1574: 1525: 1516: 1467: 1463: 1408: 1404: 1343: 1339: 1276: 1272: 1227: 1223: 1178: 1174: 1166: 1155: 1120: 1116: 1084: 1080: 1073: 1055: 1051: 1020:(7–8): 739–45. 1002: 998: 991: 977: 973: 916: 912: 877: 870: 833: 829: 798: 771: 722: 718: 673: 669: 665: 648: 609: 572: 540: 513:chloramphenicol 362: 345: 340: 292:cranberry juice 284:cranberry juice 230: 210: 181: 157: 73: 55:, required for 23: 22: 15: 12: 11: 5: 1624: 1614: 1613: 1608: 1594: 1593: 1581: 1580:External links 1578: 1573: 1572: 1514: 1479:Microbiol. Rev 1461: 1402: 1337: 1270: 1221: 1172: 1153: 1114: 1101:10.1086/315258 1078: 1072:978-0849348945 1071: 1049: 996: 990:978-0849348945 989: 971: 934:(5): 1628–33. 910: 868: 847:(6): 580–592. 827: 769: 724:Krachler, AM; 716: 666: 664: 661: 660: 659: 654: 652:Fungal adhesin 647: 644: 608: 603: 582:N. gonorrhoeae 576:N. gonorrhoeae 571: 569:N. gonorroheae 566: 538: 532:pyelonephritis 505:uropathogenic 477: 476: 473: 472: 467: 461: 460: 447: 441: 440: 430: 423: 422: 414: 413: 408: 402: 401: 396: 389: 388: 383: 377: 376: 373: 369: 368: 364: 363: 360: 352: 351: 344: 341: 339: 336: 254:uropathogenic 229: 226: 209: 206: 180: 177: 156: 153: 126:polysaccharide 72: 69: 9: 6: 4: 3: 2: 1623: 1612: 1609: 1607: 1604: 1603: 1601: 1591: 1587: 1584: 1583: 1577: 1568: 1564: 1559: 1554: 1550: 1546: 1542: 1538: 1537:Infect. Immun 1534: 1532: 1523: 1521: 1519: 1510: 1506: 1501: 1496: 1492: 1488: 1485:(2): 129–61. 1484: 1480: 1476: 1474: 1465: 1457: 1453: 1448: 1443: 1438: 1433: 1429: 1425: 1422:(9): e24353. 1421: 1417: 1413: 1406: 1398: 1394: 1389: 1384: 1380: 1376: 1372: 1368: 1364: 1360: 1356: 1352: 1348: 1341: 1333: 1329: 1324: 1319: 1315: 1311: 1306: 1301: 1297: 1293: 1289: 1285: 1281: 1274: 1266: 1262: 1257: 1252: 1248: 1244: 1240: 1236: 1232: 1225: 1217: 1213: 1208: 1203: 1199: 1195: 1192:(6): 2011–8. 1191: 1187: 1183: 1176: 1169: 1164: 1162: 1160: 1158: 1149: 1145: 1141: 1137: 1133: 1129: 1125: 1118: 1110: 1106: 1102: 1098: 1094: 1090: 1082: 1074: 1068: 1064: 1060: 1053: 1045: 1041: 1036: 1031: 1027: 1023: 1019: 1015: 1011: 1009: 1000: 992: 986: 982: 975: 967: 963: 958: 953: 949: 945: 941: 937: 933: 929: 925: 923: 914: 906: 902: 898: 894: 890: 886: 882: 875: 873: 864: 860: 855: 850: 846: 842: 838: 831: 823: 819: 815: 811: 807: 803: 796: 794: 792: 790: 788: 786: 784: 782: 780: 778: 776: 774: 765: 761: 756: 751: 747: 743: 740:(4): 284–94. 739: 735: 731: 727: 720: 712: 708: 703: 698: 694: 690: 687:(6): 735–42. 686: 682: 678: 671: 667: 658: 655: 653: 650: 649: 643: 640: 637:bound to it. 636: 632: 628: 624: 620: 615: 614: 607: 602: 600: 596: 592: 588: 584: 583: 578: 577: 570: 565: 563: 559: 555: 551: 547: 542: 541: 535: 533: 529: 524: 522: 518: 514: 509: 508: 502: 499:(DAF). These 498: 495:component of 494: 491: 487: 484: 471: 468: 466: 462: 459: 455: 451: 448: 446: 442: 438: 434: 431: 428: 424: 419: 415: 412: 409: 407: 403: 400: 397: 394: 390: 387: 384: 382: 378: 374: 370: 365: 358: 353: 348: 335: 333: 332: 327: 322: 318: 314: 309: 307: 306: 301: 295: 293: 289: 285: 281: 276: 274: 270: 266: 262: 258: 257: 251: 246: 244: 240: 235: 225: 223: 219: 215: 205: 202: 198: 193: 190: 186: 176: 174: 170: 166: 161: 152: 150: 146: 142: 138: 133: 131: 127: 123: 119: 118:gram-negative 115: 107: 103: 99: 95: 94: 88: 84: 82: 81:lacrimal duct 78: 68: 66: 62: 58: 54: 50: 47: 43: 39: 37: 33: 29: 19: 1606:Bacteriology 1575: 1540: 1536: 1530: 1482: 1478: 1472: 1464: 1419: 1415: 1405: 1354: 1350: 1340: 1287: 1283: 1273: 1241:(1): 261–8. 1238: 1234: 1224: 1189: 1185: 1175: 1131: 1127: 1123: 1117: 1095:(2): 774–8. 1092: 1089:J Infect Dis 1088: 1081: 1062: 1058: 1052: 1017: 1013: 1007: 999: 980: 974: 931: 927: 921: 913: 888: 884: 880: 844: 840: 830: 808:(1): 27–35. 805: 801: 737: 733: 719: 684: 680: 670: 638: 630: 625:which cause 622: 611: 610: 605: 594: 590: 580: 574: 573: 568: 561: 557: 553: 549: 545: 543: 537: 536: 525: 506: 482: 480: 329: 320: 310: 303: 296: 277: 264: 260: 255: 247: 231: 222:non-virulent 211: 194: 182: 162: 158: 134: 129: 111: 91: 77:shear-forces 74: 49:pathogenesis 41: 40: 27: 26: 621:. Of those 521:PI-3 kinase 490:blood group 367:Identifiers 267:associated 189:amino acids 65:prophylaxis 1600:Categories 1014:J Med Food 663:References 635:antibodies 599:neutrophil 488:to the Dr 433:structures 375:Adhesin_Dr 350:Adhesin_Dr 250:antibodies 243:antibodies 155:Structures 108:residues). 71:Background 57:colonizing 1379:2045-2322 1357:: 39341. 1314:1091-6490 734:Virulence 681:J Exp Med 595:Neisseria 564:in rats. 411:IPR006713 343:Dr family 334:in mice. 218:infection 185:D-mannose 53:infection 46:bacterial 42:Adherence 1567:21768279 1475:strains" 1456:21949708 1416:PLOS ONE 1397:27996032 1332:21709226 1109:10669375 1044:21480803 905:10446051 863:19527885 822:11043979 764:23799663 728:(2014). 711:12629063 646:See also 554:Yersinia 528:cystitis 501:proteins 450:RCSB PDB 406:InterPro 269:diarrhea 234:vaccines 130:adhesins 32:adhesion 18:Adhesins 1558:3187269 1509:6126799 1447:3174955 1424:Bibcode 1388:5171828 1359:Bibcode 1323:3136308 1292:Bibcode 1265:1670929 1216:9169726 1148:9110982 1128:Science 1035:3133681 966:9572927 936:Bibcode 885:Science 755:3710331 726:Orth, K 702:2193847 631:E. coli 623:E. coli 606:E. coli 546:E. coli 493:antigen 386:PF04619 331:E. coli 317:protein 265:E. coli 261:E. coli 239:vaccine 165:fimbria 137:tropism 122:protein 114:fimbria 106:mannose 1592:(MeSH) 1565:  1555:  1507:  1500:281536 1497:  1454:  1444:  1395:  1385:  1377:  1330:  1320:  1312:  1263:  1256:257736 1253:  1214:  1207:175278 1204:  1146:  1107:  1069:  1042:  1032:  987:  964:  957:106206 954:  903:  861:  820:  762:  752:  709:  699:  556:, and 550:Vibrio 465:PDBsum 439:  429:  399:CL0204 372:Symbol 59:a new 300:clone 169:pilus 112:Most 104:, or 1563:PMID 1505:PMID 1452:PMID 1393:PMID 1375:ISSN 1328:PMID 1310:ISSN 1261:PMID 1212:PMID 1144:PMID 1105:PMID 1067:ISBN 1040:PMID 985:ISBN 962:PMID 901:PMID 859:PMID 818:PMID 760:PMID 707:PMID 627:UTIs 486:bind 481:The 458:PDBj 454:PDBe 437:ECOD 427:Pfam 395:clan 393:Pfam 381:Pfam 143:and 102:TLR4 100:and 98:CD48 61:host 1553:PMC 1545:doi 1495:PMC 1487:doi 1442:PMC 1432:doi 1383:PMC 1367:doi 1318:PMC 1300:doi 1288:108 1251:PMC 1243:doi 1202:PMC 1194:doi 1136:doi 1132:276 1097:doi 1093:181 1030:PMC 1022:doi 952:PMC 944:doi 893:doi 889:285 883:". 849:doi 810:doi 806:290 750:PMC 742:doi 697:PMC 689:doi 685:197 445:PDB 308:). 173:ECM 167:or 116:of 51:or 1602:: 1561:. 1551:. 1541:79 1539:. 1535:. 1517:^ 1503:. 1493:. 1483:46 1481:. 1477:. 1450:. 1440:. 1430:. 1418:. 1414:. 1391:. 1381:. 1373:. 1365:. 1353:. 1349:. 1326:. 1316:. 1308:. 1298:. 1286:. 1282:. 1259:. 1249:. 1239:59 1237:. 1233:. 1210:. 1200:. 1190:65 1188:. 1184:. 1156:^ 1142:. 1130:. 1103:. 1091:. 1038:. 1028:. 1018:14 1016:. 1012:. 960:. 950:. 942:. 932:64 930:. 926:. 899:. 887:. 871:^ 857:. 843:. 839:. 816:. 804:. 772:^ 758:. 748:. 736:. 732:. 705:. 695:. 683:. 679:. 552:, 548:, 534:. 523:. 456:; 452:; 435:/ 245:. 175:. 132:. 38:. 1569:. 1547:: 1533:" 1511:. 1489:: 1458:. 1434:: 1426:: 1420:6 1399:. 1369:: 1361:: 1355:6 1334:. 1302:: 1294:: 1267:. 1245:: 1218:. 1196:: 1150:. 1138:: 1111:. 1099:: 1075:. 1046:. 1024:: 1010:" 993:. 968:. 946:: 938:: 907:. 895:: 865:. 851:: 845:5 824:. 812:: 766:. 744:: 738:4 713:. 691:: 20:)

Index

Adhesins
adhesion
virulence factor
bacterial
pathogenesis
infection
colonizing
host
prophylaxis
shear-forces
lacrimal duct

Escherichia coli
CD48
TLR4
mannose
fimbria
gram-negative
protein
polysaccharide
tropism
pathogenic bacteria
saprophytic bacteria
virulence factors
fimbria
pilus
ECM
D-mannose
amino acids
x-ray crystallography

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