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Beta defensin

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458:β-defensins genes are found across the vertebrates, including mammals, reptiles, birds and fish. The fact that alpha and theta defensins are absent in older vertebrates, like birds and fishes, indicates that defensins must have evolved from the same ancestral gene coding for β-defensins. Indeed, these defensins of this superfamily are related to the 'big defensins' which are found in invertebrate animals, indicating even earlier origins. 29: 345:. The peptides have higher affinity to the binding site compared to Ca2+ and Mg2+ ions. The peptides will therefore exchange place with those ions, thus affecting the stability of the membrane. The peptides have a greater size compared with the ions which cause changes in the membrane structure. Due to changes in the 204:
categories. Every mammalian species explored thus far has beta-defensins. In cows, as many as 13 beta-defensins exist in neutrophils. However, in other species, beta-defensins are more often produced by epithelial cells lining various organs (e.g. the epidermis, bronchial tree and genitourinary
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Defensins are 2 to 6 kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses, containing three pairs of intramolecular disulfide bonds. On the basis of their size and pattern of disulfide bonding, mammalian defensins are
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are lower in the coding regions compared to non-coding regions. The appearance of SNPs in the coding region will highly likely affecting the resistance against infections through changes in the protein sequences which will give rise to different biological functions.
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Hellgren O, Sheldon BC (July 2011). "Locus-specific protocol for nine different innate immune genes (antimicrobial peptides: β-defensins) across passerine bird species reveals within-species coding variation and a case of trans-species polymorphisms".
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Liu L, Zhao C, Heng HH, Ganz T (August 1997). "The human beta-defensin-1 and alpha-defensins are encoded by adjacent genes: two peptide families with differing disulfide topology share a common ancestry".
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Harder J, Siebert R, Zhang Y, Matthiesen P, Christophers E, Schlegelberger B, Schröder JM (December 1997). "Mapping of the gene encoding human beta-defensin-2 (DEFB2) to chromosome region 8p22-p23.1".
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Human, rabbit and guinea-pig beta-defensins, as well as human beta-defensin-2 (hBD2), induce the activation and degranulation of mast cells, resulting in the release of histamine and prostaglandin D2.
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The first beta-defensin discovered was Tracheal Antimicrobial Peptide, found in the bovine airway in 1991. The first human beta-defensin, HBD1, was discovered in 1995, followed by the HBD2 in 1997.
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Whittington, C. M.; Papenfuss, A. T.; Bansal, P.; Torres, A. M.; Wong, E. S.W.; Deakin, J. E.; Graves, T.; Alsop, A.; Schatzkamer, K.; Kremitzki, C.; Ponting, C. P. (2008-05-07).
412:β-defensins are classified in three classes and avian β-defensins constitute for one of the classes. This division is based on Zhang's classification and both the length, the 149: 476:
In addition to other antimicrobial defensins, there are related defensin-like proteins with have evolved other functions. These include toxins found in snakes (e.g.
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Abreu MT (February 2010). "Toll-like receptor signalling in the intestinal epithelium: how bacterial recognition shapes intestinal function".
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and non-heterophiles. Avian heterophiles can be divided into two sub-classes, depending on the number of present homologous residues in the
1279:"Tracheal antimicrobial peptide, a novel cysteine-rich peptide from mammalian tracheal mucosa: Peptide isolation and cloning of a cDNA" 516: 508: 548: 540: 536: 532: 528: 524: 520: 942:
Vora P, Youdim A, Thomas LS, Fukata M, Tesfay SY, Lukasek K, Michelsen KS, Wada A, Hirayama T, Arditi M, Abreu MT (November 2004).
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In 2001, it was thought that β-defensins were similar to the ancestral defensin from a comparison of sequences of β-defensins,
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and big defensins share an evolutionary origin, but are separate to the defensins found in insects, fungi and plants.
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in the terminal end of the strands connecting defensins monomers. Formation of pore complex will cause membrane
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White SH, Wimley WC, Selsted ME (August 1995). "Structure, function, and membrane integration of defensins".
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Sugiarto H, Yu PL (October 2004). "Avian antimicrobial peptides: the defense role of beta-defensins".
86: 1130:"The structure of human beta-defensin-1: new insights into structural properties of beta-defensins" 294: 377: 318: 221: 189: 373: 217: 136: 8: 944:"Beta-defensin-2 expression is regulated by TLR signaling in intestinal epithelial cells" 334: 290: 282: 1169:
Shafee, Thomas M. A.; Lay, Fung T.; Hulett, Mark D.; Anderson, Marilyn A. (2016-06-13).
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Ganz T (September 2003). "Defensins: antimicrobial peptides of innate immunity".
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Diamond, G.; Zasloff, M.; Eck, H.; Brasseur, M.; Maloy, W.; Bevins, C. (1991).
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implicated in the resistance of epithelial surfaces to microbial colonization.
1047: 1401: 1245: 1196: 1055: 389: 350: 342: 302: 286: 274: 1220:"Defensins and the convergent evolution of platypus and reptile venom genes" 1187: 1171:"The Defensins Consist of Two Independent, Convergent Protein Superfamilies" 1170: 1095: 1381: 1341: 1295: 1263: 1204: 1155: 1146: 1129: 1114: 1079:"Duplication and selection in the evolution of primate beta-defensin genes" 1063: 1013: 969: 920: 885: 852:"Pathogen recognition and inflammatory signaling in innate immune defenses" 831: 757: 714: 233: 1389: 1349: 1314: 667: 640:
Bensch KW, Raida M, Mägert HJ, Schulz-Knappe P, Forssmann WG (July 1995).
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to the infection site. Defensins will also improve the capacity of
330: 237: 185: 61: 216:β-defensins are coding for genes which impact the function of the 512: 438:
Avian heterophiles lack protective oxidative mechanisms, such as
349:, peptides will pass across the membrane and thus aggregate into 278: 1217: 432: 164: 639: 252:) are found in genes coding for β-defensins. The presences of 496: 329:β-defensins are cationic and can therefore interact with the 1327: 353:. Pore complex will be created as a result of breaking the 253: 249: 126: 49: 795: 1276: 491: 1168: 28: 1127: 941: 372:
Defensins not only have the ability to strengthen the
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van Dijk A, Veldhuizen EJ, Haagsman HP (July 2008).
1128:Hoover DM, Chertov O, Lubkowski J (October 2001). 601: 293:are expressed in intestinal epithelial cells or 220:. These genes are responsible for production of 1399: 1076: 642:"hBD-1: a novel beta-defensin from human plasma" 333:of invading microbes, which are negative due to 1366: 987: 985: 983: 981: 979: 845: 843: 841: 791: 789: 787: 785: 783: 781: 779: 777: 775: 691: 687: 685: 635: 633: 1121: 1070: 1025: 1023: 976: 892: 838: 772: 682: 597: 595: 450:and cationic peptides, even more important. 1321: 849: 729: 446:, making non-oxidative mechanisms, such as 1036:Developmental & Comparative Immunology 991: 630: 424:are factors affecting the classification. 1304: 1294: 1253: 1235: 1186: 1145: 1104: 1094: 1020: 959: 875: 821: 657: 592: 427:Avian β-defensins are separated in avian 935: 313:will take place and substances such as 1400: 1030:Zhu, Shunyi; Gao, Bin (January 2013). 1029: 735: 1077:Semple CA, Rolfe M, Dorin JR (2003). 898: 492:Human proteins containing this domain 309:. When the receptors are activated a 1032:"Evolutionary origin of β-defensins" 407: 13: 1359: 14: 1429: 480:), bearded lizards and platypus. 862:(2): 240–73, Table of Contents. 707:10.1111/j.1755-0998.2011.02995.x 240:, β-defensins are also found in 27: 1270: 1211: 1175:Molecular Biology and Evolution 1162: 246:Single-nucleotide polymorphisms 1: 994:Biochem. Biophys. Res. Commun 586: 581:Lingual antimicrobial peptide 260: 121:Available protein structures: 1413:Peripheral membrane proteins 814:10.1016/j.vetimm.2007.12.006 659:10.1016/0014-5793(95)00687-5 616:10.1016/0959-440X(95)80038-7 453: 7: 961:10.4049/jimmunol.173.9.5398 695:Molecular Ecology Resources 554: 324: 184:are a family of vertebrate 10: 1434: 1283:Proc. Natl. Acad. Sci. USA 1006:10.1016/j.bbrc.2004.08.162 850:Mogensen TH (April 2009). 802:Vet. Immunol. Immunopathol 483: 1048:10.1016/j.dci.2012.02.011 376:but can also enhance the 188:. The beta defensins are 163: 143: 125: 120: 116: 104: 92: 72: 60: 48: 40: 35: 26: 21: 604:Curr. Opin. Struct. Biol 295:antigen presenting cells 273:(NLR) will activate the 211: 1096:10.1186/gb-2003-4-5-r31 402:macrophage phagocytosis 1418:Antimicrobial peptides 1382:10.1006/geno.1997.4801 1342:10.1006/geno.1997.5074 1296:10.1073/pnas.88.9.3952 1147:10.1074/jbc.M103830200 378:adaptive immune system 319:antimicrobial peptides 222:antimicrobial peptides 190:antimicrobial peptides 1188:10.1093/molbev/msw106 868:10.1128/CMR.00046-08 856:Clin. Microbiol. Rev 374:innate immune system 218:innate immune system 341:(LTA) found in the 335:lipopolysaccharides 291:Toll-like receptors 283:lipopolysaccharides 267:toll-like receptors 1237:10.1101/gr.7149808 347:electric potential 321:will be released. 271:nod-like receptors 265:Receptors such as 16:Family of proteins 901:Nat. Rev. Immunol 798:"Avian defensins" 738:Nat. Rev. Immunol 408:Avian β-defensins 339:lipoteichoic acid 226:white blood cells 179: 178: 175: 174: 170:structure summary 1425: 1393: 1354: 1353: 1325: 1319: 1318: 1308: 1298: 1289:(9): 3952–3956. 1274: 1268: 1267: 1257: 1239: 1215: 1209: 1208: 1190: 1181:(9): 2345–2356. 1166: 1160: 1159: 1149: 1125: 1119: 1118: 1108: 1098: 1074: 1068: 1067: 1027: 1018: 1017: 989: 974: 973: 963: 939: 933: 932: 896: 890: 889: 879: 847: 836: 835: 825: 793: 770: 769: 733: 727: 726: 689: 680: 679: 661: 637: 628: 627: 599: 467:insect defensins 311:cascade reaction 242:epithelial cells 196:classified into 118: 117: 31: 19: 18: 1433: 1432: 1428: 1427: 1426: 1424: 1423: 1422: 1398: 1397: 1396: 1362: 1360:Further reading 1357: 1326: 1322: 1275: 1271: 1224:Genome Research 1216: 1212: 1167: 1163: 1140:(42): 39021–6. 1126: 1122: 1075: 1071: 1028: 1021: 990: 977: 954:(9): 5398–405. 940: 936: 913:10.1038/nri2707 897: 893: 848: 839: 794: 773: 750:10.1038/nri1180 734: 730: 690: 683: 638: 631: 600: 593: 589: 557: 494: 486: 456: 444:myeloperoxidase 410: 394:dendritic cells 327: 299:dendritic cells 297:(APCs) such as 263: 214: 182:Beta defensins 94:OPM superfamily 17: 12: 11: 5: 1431: 1421: 1420: 1415: 1410: 1395: 1394: 1363: 1361: 1358: 1356: 1355: 1320: 1269: 1230:(6): 986–994. 1210: 1161: 1120: 1069: 1042:(1–2): 79–84. 1019: 975: 934: 891: 837: 771: 728: 701:(4): 686–692. 681: 629: 590: 588: 585: 584: 583: 578: 577: 576: 571: 568: 556: 553: 493: 490: 485: 482: 455: 452: 422:gene structure 409: 406: 363:depolarization 355:hydrogen bonds 326: 323: 277:by binding of 262: 259: 213: 210: 177: 176: 173: 172: 167: 161: 160: 147: 141: 140: 130: 123: 122: 114: 113: 108: 102: 101: 96: 90: 89: 76: 70: 69: 64: 58: 57: 52: 46: 45: 42: 38: 37: 33: 32: 24: 23: 15: 9: 6: 4: 3: 2: 1430: 1419: 1416: 1414: 1411: 1409: 1406: 1405: 1403: 1391: 1387: 1383: 1379: 1376:(3): 316–20. 1375: 1371: 1365: 1364: 1351: 1347: 1343: 1339: 1335: 1331: 1324: 1316: 1312: 1307: 1302: 1297: 1292: 1288: 1284: 1280: 1273: 1265: 1261: 1256: 1251: 1247: 1243: 1238: 1233: 1229: 1225: 1221: 1214: 1206: 1202: 1198: 1194: 1189: 1184: 1180: 1176: 1172: 1165: 1157: 1153: 1148: 1143: 1139: 1135: 1134:J. Biol. Chem 1131: 1124: 1116: 1112: 1107: 1102: 1097: 1092: 1088: 1084: 1080: 1073: 1065: 1061: 1057: 1053: 1049: 1045: 1041: 1037: 1033: 1026: 1024: 1015: 1011: 1007: 1003: 999: 995: 988: 986: 984: 982: 980: 971: 967: 962: 957: 953: 949: 945: 938: 930: 926: 922: 918: 914: 910: 907:(2): 131–44. 906: 902: 895: 887: 883: 878: 873: 869: 865: 861: 857: 853: 846: 844: 842: 833: 829: 824: 819: 815: 811: 808:(1–2): 1–18. 807: 803: 799: 792: 790: 788: 786: 784: 782: 780: 778: 776: 767: 763: 759: 755: 751: 747: 744:(9): 710–20. 743: 739: 732: 724: 720: 716: 712: 708: 704: 700: 696: 688: 686: 677: 673: 669: 665: 660: 655: 651: 647: 643: 636: 634: 625: 621: 617: 613: 609: 605: 598: 596: 591: 582: 579: 575: 572: 569: 567: 564: 563: 562: 559: 558: 552: 550: 546: 542: 538: 534: 530: 526: 522: 518: 514: 510: 506: 502: 498: 489: 481: 479: 474: 472: 468: 464: 459: 451: 449: 445: 441: 436: 434: 430: 425: 423: 419: 415: 405: 403: 399: 395: 391: 390:T-lymphocytes 387: 383: 379: 375: 370: 368: 364: 360: 356: 352: 348: 344: 343:cell membrane 340: 336: 332: 322: 320: 316: 312: 308: 304: 303:B-lymphocytes 300: 296: 292: 288: 287:peptidoglycan 284: 280: 276: 275:immune system 272: 268: 258: 255: 251: 247: 243: 239: 235: 231: 227: 223: 219: 209: 206: 203: 199: 193: 191: 187: 183: 171: 168: 166: 162: 159: 155: 151: 148: 146: 142: 138: 134: 131: 128: 124: 119: 115: 112: 109: 107: 103: 100: 97: 95: 91: 88: 84: 80: 77: 75: 71: 68: 65: 63: 59: 56: 53: 51: 47: 44:Defensin_beta 43: 39: 34: 30: 25: 22:Beta defensin 20: 1373: 1369: 1336:(3): 472–5. 1333: 1329: 1323: 1286: 1282: 1272: 1227: 1223: 1213: 1178: 1174: 1164: 1137: 1133: 1123: 1086: 1082: 1072: 1039: 1035: 1000:(3): 721–7. 997: 993: 951: 947: 937: 904: 900: 894: 859: 855: 805: 801: 741: 737: 731: 698: 694: 652:(2): 331–5. 649: 645: 610:(4): 521–7. 607: 603: 495: 487: 475: 460: 457: 437: 429:heterophiles 426: 411: 371: 357:between the 328: 264: 234:granulocytes 215: 207: 194: 181: 180: 1083:Genome Biol 471:θ-defensins 463:α-defensins 359:amino acids 307:macrophages 230:macrophages 200:, beta and 106:OPM protein 36:Identifiers 1402:Categories 1089:(5): R31. 948:J. Immunol 587:References 574:θ-defensin 570:β-defensin 566:α-defensin 440:superoxide 398:mast cells 382:chemotaxis 367:cell lysis 337:(LPS) and 269:(TLR) and 261:Initiation 133:structures 1408:Defensins 1246:1088-9051 1197:0737-4038 1056:0145-305X 646:FEBS Lett 478:crotamine 454:Evolution 448:lysosomes 386:monocytes 315:cytokines 224:found in 186:defensins 67:IPR001855 1370:Genomics 1330:Genomics 1264:18463304 1205:27297472 1156:11486002 1115:12734011 1064:22369779 1014:15381059 970:15494486 929:21789611 921:20098461 886:19366914 832:18313763 758:12949495 723:12499158 715:21676198 676:84766207 561:Defensin 555:See also 517:DEFB108B 509:DEFB105B 505:DEFB105A 501:DEFB103A 420:and the 418:peptides 414:homology 331:membrane 325:Function 281:such as 238:NK-cells 228:such as 205:tract). 150:RCSB PDB 62:InterPro 1390:9268634 1350:9441752 1315:2023943 1255:2413166 877:2668232 823:7112556 766:3360031 668:7628632 624:8528769 549:SPAG11A 541:DEFB136 537:DEFB130 533:DEFB114 529:DEFB111 525:DEFB110 521:DEFB109 513:DEFB106 484:History 416:of the 279:ligands 55:PF00711 1388:  1348:  1313:  1303:  1262:  1252:  1244:  1203:  1195:  1154:  1113:  1106:156587 1103:  1062:  1054:  1012:  968:  927:  919:  884:  874:  830:  820:  764:  756:  721:  713:  674:  666:  622:  547:; 499:; 433:genome 351:dimers 165:PDBsum 139:  129:  87:SUPFAM 41:Symbol 1306:51571 925:S2CID 762:S2CID 719:S2CID 672:S2CID 545:DEFB4 497:DEFB1 212:Genes 202:theta 198:alpha 83:SCOPe 74:SCOP2 1386:PMID 1346:PMID 1311:PMID 1260:PMID 1242:ISSN 1201:PMID 1193:ISSN 1152:PMID 1111:PMID 1060:PMID 1052:ISSN 1010:PMID 966:PMID 917:PMID 882:PMID 828:PMID 754:PMID 711:PMID 664:PMID 620:PMID 543:; 539:; 535:; 527:; 523:; 465:and 442:and 396:and 365:and 317:and 305:and 285:and 254:SNPs 250:SNPs 236:and 158:PDBj 154:PDBe 137:ECOD 127:Pfam 111:1ut3 79:1bnb 50:Pfam 1378:doi 1338:doi 1301:PMC 1291:doi 1250:PMC 1232:doi 1183:doi 1142:doi 1138:276 1101:PMC 1091:doi 1044:doi 1002:doi 998:323 956:doi 952:173 909:doi 872:PMC 864:doi 818:PMC 810:doi 806:124 746:doi 703:doi 654:doi 650:368 612:doi 519:; 507:; 503:; 384:of 380:by 145:PDB 1404:: 1384:. 1374:43 1372:. 1344:. 1334:46 1332:. 1309:. 1299:. 1287:88 1285:. 1281:. 1258:. 1248:. 1240:. 1228:18 1226:. 1222:. 1199:. 1191:. 1179:33 1177:. 1173:. 1150:. 1136:. 1132:. 1109:. 1099:. 1085:. 1081:. 1058:. 1050:. 1040:39 1038:. 1034:. 1022:^ 1008:. 996:. 978:^ 964:. 950:. 946:. 923:. 915:. 905:10 903:. 880:. 870:. 860:22 858:. 854:. 840:^ 826:. 816:. 804:. 800:. 774:^ 760:. 752:. 740:. 717:. 709:. 699:11 697:. 684:^ 670:. 662:. 648:. 644:. 632:^ 618:. 606:. 594:^ 551:; 531:; 515:; 511:; 435:. 404:. 392:, 388:, 369:. 301:, 289:. 244:. 232:, 156:; 152:; 135:/ 99:54 85:/ 81:/ 1392:. 1380:: 1352:. 1340:: 1317:. 1293:: 1266:. 1234:: 1207:. 1185:: 1158:. 1144:: 1117:. 1093:: 1087:4 1066:. 1046:: 1016:. 1004:: 972:. 958:: 931:. 911:: 888:. 866:: 834:. 812:: 768:. 748:: 742:3 725:. 705:: 678:. 656:: 626:. 614:: 608:5 248:(

Index


Pfam
PF00711
InterPro
IPR001855
SCOP2
1bnb
SCOPe
SUPFAM
OPM superfamily
54
OPM protein
1ut3
Pfam
structures
ECOD
PDB
RCSB PDB
PDBe
PDBj
PDBsum
structure summary
defensins
antimicrobial peptides
alpha
theta
innate immune system
antimicrobial peptides
white blood cells
macrophages

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