2596:
2608:
431:
40:
498:
with short saturated acyl chains, especially if they have a conical form, whereas cylindrical lipids (e.g., sphingomyelin) hinder its activity. The lytic process, most commonly seen in leucocytes, is caused by pore formation induced by an oligomerized octamer that organizes in a ring structure. Once
1325:
Dalla Serra M, Coraiola M, Viero G, Comai M, Potrich C, Ferreras M, Baba-Moussa L, Colin DA, Menestrina G, Bhakdi S, Prévost G (2005). "Staphylococcus aureus bicomponent gamma-hemolysins, HlgA, HlgB, and HlgC, can form mixed pores containing all components".
446:, this toxin binds with the outer membrane, with subsequent oligomerization of the toxin monomers to form water-filled channels. These are responsible for osmotic phenomena, cell depolarization and loss of vital molecules (v.gr. ATP), leading to cell death.
401:
This pore consists of seven alpha-hemolysin subunits, which represent the major cytotoxic agent that is freed by this kind of bacterium. These subunits attach to the target cells in the manner described before, and extend the lipid bilayer, forming the
879:
As hemolysins are produced by pathogenic organisms, the main treatment is the intake of antibiotics specific to the pathogen that have caused the infection. Moreover, some hemolysins may be neutralized by the action of anti-hemolysin
619:, earlier than expected in a normal situation. As the bone marrow cannot make erythrocytes fast enough to meet the body’s needs, oxygen does not arrive to body tissues properly. As a consequence, some symptoms may appear, such as
1250:
Krasil’nikov O.V.; Ternovsky, VI.; Tashmukhamedov, BA. Properties of conductivity channels induced in phospholipid bilayer membanes by alpha-staphylotoxin. //Biofizika (Moscow), — 1981.—V. 26, — N.2, —P.
845:
of hemolysins (such as streptolysin S) is a system repressed in the presence of iron. This ensures that hemolysin is produced only when needed. The regulation of the production of hemolysin in
589:. Lysis of these cells releases heme into the surroundings, allowing the bacteria to take up the free iron. But hemolysin is related to bacteria not only in this way but also in some others.
557:
there is a hydrophobic belt approximately 30 Å in width that provides a surface complementary to the nonpolar portion of the lipid bilayer. The interfaces are composed of both salt-links and
2011:
Karmakar P, Chakrabarti MK (July 2012). "Thermostable direct hemolysin diminishes tyrosine phosphorylation of epidermal growth factor receptor through protein kinase C dependent mechanism".
2080:
484:γ-Hemolysins are pore-forming toxins in the same family as α-Hemolysin. They are unique in that they come in two components, and hence are referred to as bi-component toxins (
406:. These pores in the cellular membrane will eventually end up causing cell death, since it allows the exchange of monovalent ions that would cause the DNA fragmentation.
177:
195:. Although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by
142:
2514:
2574:
1361:
Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE (December 1996). "Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore".
549:
has a mushroom-like shape and measures up to 100 Å in diameter and 100 Å in height. A membrane-spanning, solvent-accessible channel runs along the sevenfold
2073:
634:
Depending on the type of hemolysin and the microorganism that produces it, manifestation of symptoms and diseases may differ from one case to the other:
2310:
2305:
2058:
1903:
Burnside K, Lembo A, de Los Reyes M, Iliuk A, Binhtran NT, Connelly JE, Lin WJ, Schmidt BZ, Richardson AR, Fang FC, Tao WA, Rajagopal L (2010).
2066:
230:
199:
do not cause significant destruction of red blood cells during infection. However, hemolysins are often capable of lysing red blood cells
1674:"Staphylococcus aureus α-hemolysin mediates virulence in a murine model of severe pneumonia through activation of the NLRP3 inflammasome"
2277:
1497:"Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components"
1860:
Griffiths BB, McClain O (1988). "The role of iron in the growth and hemolysin (Streptolysin S) production in
Streptococcus pyogenes".
899:
must be removed because it filters blood and removes dead or damaged cells from the bloodstream, worsening the lack of erythrocytes.
1066:
516:
679:(a facultative intracellular bacterium that thrives within host cells, mainly macrophages and monocytes) causes the degradation of
2633:
468:. Upon investigating sheep erythrocytes, its toxic mechanism was discovered to be the hydrolysis of a specific membrane lipid,
1600:
2282:
773:
162:
1672:
Kebaier C, Chamberland RR, Allen IC, Gao X, Broglie PM, Hall JD, Jania C, Doerschuk CM, Tilley SL, Duncan JA (March 2012).
218:
Many bacteria produce hemolysins that can be detected in the laboratory. It is now believed that many clinically relevant
1151:
Bhakdi S, Mackman N, Menestrina G, Gray L, Hugo F, Seeger W, Holland IB (June 1988). "The hemolysin of
Escherichia coli".
842:
2586:
1905:"Regulation of hemolysin expression and virulence of Staphylococcus aureus by a serine/threonine kinase and phosphatase"
1000:"Di-rhamnolipid from Pseudomonas aeruginosa displays differential effects on human keratinocyte and fibroblast cultures"
585:, free iron is typically maintained at low concentrations within the body. Red blood cells are rich in iron-containing
241:
Not only are the erythrocytes affected by hemolysins, but there are also some effects among other blood cells, such as
1723:"Apigenin alleviates the symptoms of Staphylococcus aureus pneumonia by inhibiting the production of alpha-hemolysin"
687:
Both aerolysin and alpha-hemolysin are synthesized by extracellular bacteria, which infect specific tissue surfaces.
764:, the pore-forming toxin α-hemolysin (Hla), is the secreted factor responsible for the activation of an alternative
2265:
745:
aimed at developing new farmacs to cure easily or prevent this kind of pneumonia. At the moment, apiegnin and beta-
362:
secretes alpha-hemolysin monomers that bind to the outer membrane of susceptible cells. Upon binding, the monomers
2628:
264:
Visualization of hemolysis (UK: haemolysis) of red blood cells in agar plates facilitates the categorization of
2638:
2052:
1495:
Yamashita K, Kawai Y, Tanaka Y, Hirano N, Kaneko J, Tomita N, Ohta M, Kamio Y, Yao M, Tanaka I (October 2011).
969:
562:
791:
with doses of alpha-hemolysin at which nearly 80% of the cells survived decreased the ability of the cells to
604:
during infections) are combined with other virulence factors may threaten a human's life to a greater extent.
150:
2546:
957:
924:
499:
the prepore is formed, a more stable one ensues, named β-barrel. In this final part, the octamer binds with
316:
676:
566:
383:
2270:
2097:
979:
761:
708:
692:
658:
534:
512:
339:
277:
1964:"Anti-alpha-hemolysin monoclonal antibodies mediate protection against Staphylococcus aureus pneumonia"
472:, which accounts for 50% of the cell’s membrane. This degradation was followed by a noticeable rise of
146:
311:
Hemolysin is normally secreted by the bacteria in a water-soluble way. These monomers diffuse to the
2297:
2253:
2147:
1916:
1508:
1439:
1370:
1207:
305:
600:, many cases of hemolysis do not suppose a health hazard. But the fact that hemolysins (produced by
2287:
974:
577:
Hemolysins are thought to be responsible for many events in host cells. For example, iron may be a
550:
500:
289:
258:
1721:
Dong J, Qiu J, Wang J, Li H, Dai X, Zhang Y, Wang X, Tan W, Niu X, Deng X, Zhao S (October 2012).
1262:
1885:
1394:
1176:
1084:
933:
473:
395:
387:
222:
also produce hemolysins. Hemolysins can be identified by their ability to lyse red blood cells
414:
Some hemolysins damage the erythrocyte membrane by cleaving the phospholipids in the membrane.
2028:
1993:
1944:
1877:
1842:
1793:
1744:
1703:
1622:
1581:
1536:
1485:
1467:
1412:
1386:
1343:
1307:
1233:
1168:
1133:
1072:
1062:
1029:
620:
539:
476:
due to the release of organic phosphorus from sphingomyelin and ultimately caused cell lysis.
379:
137:
46:
2493:
2488:
2433:
2423:
2418:
2408:
2403:
2398:
2378:
1112:"α-Hemolysin pore formation into a supported phospholipid bilayer using cell-free expression"
895:
supplements may be given or, in case of emergencies, a blood transfusion. In rare cases, the
358:. It produces a ring-shaped complex called a staphylococcal alpha-hemolysin pore. In nature,
2519:
2348:
2328:
2235:
2230:
2225:
2220:
2215:
2210:
2200:
2190:
2185:
2175:
2170:
2093:
2020:
1983:
1975:
1934:
1924:
1869:
1832:
1824:
1813:"Effect of Escherichia coli alpha-hemolysin on human peripheral leukocyte function in vitro"
1783:
1775:
1734:
1693:
1685:
1612:
1571:
1526:
1516:
1457:
1447:
1378:
1335:
1297:
1289:
1261:
McGillivray DJ, Heinrich F, Valincius G, Ignatjev I, Vanderah DJ, Lösche M, Kasianowicz JJ.
1223:
1215:
1160:
1123:
1054:
1019:
1011:
949:
945:
741:
is a common disease in some areas, which is the reason for the many studies in the field of
723:
665:
608:
2205:
2180:
1651:
711:
leading to tissue damage or even tissue destruction. There is a clear example of this: the
129:
2612:
2132:
2127:
1096:
953:
937:
826:
690:
Hemolysins have proved to be a damaging factor for vital organs, through the activity of
578:
528:
461:
229:
188:
1920:
1512:
1443:
1374:
1278:"Staphylococcal beta-hemolysin. II. Phospholipase C activity of purified beta-hemolysin"
1211:
553:
and ranges from 14 Å to 46 Å in diameter. On the exterior of the 14-strand antiparallel
2600:
1988:
1963:
1939:
1904:
1788:
1763:
1698:
1673:
1531:
1496:
1462:
1423:
1228:
1195:
1024:
999:
650:
593:
558:
495:
403:
280:. Other hemolysins lyse erythrocytes by hydrolyzing the phospholipids in the bilayer.
2048:
1837:
1812:
1617:
1302:
1277:
1058:
2622:
639:
469:
265:
207:
192:
1889:
1398:
581:
in the growth of various pathogenic bacteria. Since free iron may generate damaging
78:
2105:
1630:
1293:
1263:"Membrane Association of α-Hemolysin: Proteins Functionally Reconstituted in tBLMs"
1180:
1015:
807:
746:
730:
612:
582:
391:
312:
293:
125:
1828:
1764:"Staphylococcus aureus promotes autophagy by decreasing intracellular cAMP levels"
1382:
91:
2024:
1929:
1128:
1111:
918:
683:
membranes, but they are not a potential danger for the cell’s plasmatic membrane.
490:
103:
2458:
2320:
868:
792:
701:
628:
616:
597:
554:
523:
363:
254:
2595:
1428:
cytolysin heptamer reveals common features among disparate pore-forming toxins"
719:. In this case, it has been proven that alpha-hemolysin takes part in inducing
2541:
2524:
2122:
1219:
888:
884:, preventing a longer and more dangerous effect of hemolysis within the body.
881:
811:
803:
799:
788:
754:
742:
734:
704:
669:
367:
297:
242:
2551:
1873:
1739:
1722:
1689:
1521:
1452:
861:
830:
769:
765:
712:
680:
351:
301:
250:
196:
2032:
1997:
1948:
1797:
1748:
1707:
1626:
1576:
1555:
1540:
1471:
1347:
1237:
1137:
1076:
1033:
592:
As mentioned before, hemolysin is a potential virulence factor produced by
398:
leading to the cell wall rupture (lysis) can cause death of the host cell.
366:
to form a water-filled transmembrane channel that facilitates uncontrolled
1881:
1846:
1585:
1390:
1311:
1172:
17:
2509:
2114:
1979:
929:
913:
853:
795:
720:
646:
601:
485:
456:
347:
320:
98:
960:
receptor (EGFR), the rational target of anti-colorectal cancer therapy.
2483:
2478:
2438:
2428:
2413:
2393:
2388:
2383:
2373:
2089:
1779:
1164:
941:
819:
777:
642:
565:, and these contacts provide a molecular stability for the heptamer in
326:
Hemolysins can be secreted by many different kinds of bacteria such as
1489:
1416:
1339:
596:, which can put a human's health at risk. Despite causing some severe
50:
2368:
2363:
2358:
2353:
2343:
2338:
2333:
2245:
2101:
896:
864:
857:
654:
355:
157:
1053:. Advances in Applied Microbiology. Vol. 55. pp. 191–213.
1048:
430:
772:
is inhibited by artificially elevating the intracellular levels of
2534:
2529:
2443:
2195:
2165:
2160:
781:
727:
429:
371:
228:
219:
184:
1110:
Chalmeau J, Monina N, Shin J, Vieu C, Noireaux V (January 2011).
668:
infects the intestinal tract, but it might also cause sepsis and
2561:
2556:
2473:
2463:
2453:
2448:
2258:
2155:
2137:
892:
833:. Hemolysins may also mediate bacterial escape from host cells.
624:
586:
375:
119:
85:
73:
2062:
39:
2468:
1194:
Thompson JR, Cronin B, Bayley H, Wallace MI (December 2011).
829:, allow bacteria to evade the immune system by escaping from
319:. After this is done, they oligomerize, creating ring-shaped
1050:
Possible role of fungal hemolysins in sick building syndrome
515:
in the soluble and pore-forming conformations. For example,
494:). Compared to beta-hemolysin, it has a higher affinity for
342:
as a specific example of pore-forming hemolysin production.
338:
among other pathogens. We can take a look at the bacterium
276:
One way hemolysin lyses erythrocytes is by forming pores in
206:
While most hemolysins are protein compounds, some are lipid
1654:. United States National Institutes of Health. 2011-04-01
776:. This process is also mediated by the exchange factors
733:, which is responsible for inflammatory processes and of
631:, an enlarged heart or even heart failure, among others.
944:
influx from an extracellular environment accompanied by
760:
Further findings show that the main virulence factor of
757:
of anti alpha-hemlysin are thought to give protection.
511:
The structure of several hemolysins has been solved by
1196:"Rapid assembly of a multimeric membrane protein pore"
2584:
887:
When blood cells are being destroyed too fast, extra
438:: macromolecular structure of the transmembrane pore.
998:
Stipcevic T, Piljac T, Isseroff RR (November 2005).
2502:
2319:
2296:
2244:
2146:
2113:
1560:: an archetype of β-barrel, channel-forming toxins"
645:produces extra-intestinal infections and can cause
156:
136:
118:
113:
97:
84:
72:
64:
59:
32:
27:
Molecule destroying the membrane of red blood cells
787:Another interesting point is that pretreatment of
44:Staphylococcus aureus alpha toxin from S. aureus (
849:(expression of hemolysin) is now possible due to
532:cytolysin also forms a heptameric pore, however
2515:LDL-receptor-related protein-associated protein
700:is a dangerous pathogen that may lead cells to
2074:
1276:Maheswaran SK, Lindorfer RK (November 1967).
661:can cause severe diseases, such as pneumonia.
611:, condition that involves the destruction of
382:. Rapid discharge of vital molecules such as
350:that causes many infectious diseases such as
8:
292:(PFT), which are able to cause the lysis of
1962:Ragle BE, Bubeck Wardenburg J (July 2009).
818:, would greatly enhance the survival of an
2081:
2067:
2059:
1811:Cavalieri SJ, Snyder IS (September 1982).
110:
38:
2311:Pulmonary surfactant-associated protein C
2306:Pulmonary surfactant-associated protein B
2051:at the U.S. National Library of Medicine
1987:
1938:
1928:
1836:
1787:
1738:
1697:
1616:
1575:
1530:
1520:
1461:
1451:
1301:
1227:
1127:
1023:
1652:"What Is Hemolytic Anemia? - NHLBI, NIH"
2591:
990:
1762:Mestre MB, Colombo MI (October 2012).
1092:
1082:
29:
2575:other cell membrane protein disorders
928:is now being studied in the field of
768:. It has been demonstrated that this
607:The main consequence of hemolysis is
315:and are attached to them by specific
7:
912:Thermostable Direct Hemolysin (TDH;
2278:Myelin oligodendrocyte glycoprotein
183:are lipids and proteins that cause
814:by alpha-hemolysin, if they occur
25:
615:and their later removal from the
569:solutions even up to 65 °C.
545:The heptamer of α-hemolysin from
538:γ-hemolysin forms a pore that is
2606:
2594:
707:usually recognized by a massive
2547:Phospholipid transfer proteins
2283:Myelin-associated glycoprotein
1601:"Iron and bacterial virulence"
1294:10.1128/JB.94.5.1313-1319.1967
1016:10.1016/j.jdermsci.2005.08.005
253:to monocytes, lymphocytes and
1:
1829:10.1128/IAI.37.3.966-974.1982
1618:10.1016/S0255-0857(21)02343-4
1383:10.1126/science.274.5294.1859
1265:. Carnegie Mellon University.
1059:10.1016/S0065-2164(04)55007-4
1047:Vesper SJ, Vesper MJ (2004).
843:regulation of gene expression
837:Regulation of gene expression
798:and particles and to undergo
526:in biological membranes. The
114:Available protein structures:
2025:10.1016/j.bbagen.2012.04.011
1930:10.1371/journal.pone.0011071
1501:Proc. Natl. Acad. Sci. U.S.A
1432:Proc. Natl. Acad. Sci. U.S.A
1129:10.1016/j.bbamem.2010.07.027
948:phosphorylation. Activated
2655:
2266:Myelin proteolipid protein
1424:"Crystal structure of the
1422:De S, Olson R (May 2011).
802:. Premature activation of
304:by producing pores on the
33:Leukocidin/Hemolysin toxin
2570:
1599:Sritharan M (July 2006).
1220:10.1016/j.bpj.2011.09.054
825:Some hemolysins, such as
749:are thought to alleviate
602:pathogenic microorganisms
249:hemolysin is potentially
109:
37:
2053:Medical Subject Headings
970:Hemolysis (microbiology)
563:hydrophobic interactions
522:forms a homo-heptameric
1874:10.1002/jobm.3620280703
1740:10.1111/1574-6968.12040
1522:10.1073/pnas.1110402108
1453:10.1073/pnas.1017442108
958:epidermal growth factor
925:Vibrio parahaemolyticus
753:pneumonia, whereas the
657:. Alpha-hemolysin from
380:small organic molecules
2634:Transmembrane proteins
2013:Biochim. Biophys. Acta
1605:Indian J Med Microbiol
1577:10.1006/jsbi.1998.3959
1116:Biochim. Biophys. Acta
737:. Pneumonia caused by
677:Listeria monocytogenes
439:
434:Alpha(α)-hemolysin of
336:Vibrio parahemolyticus
238:
2098:Cell surface receptor
1690:10.1093/infdis/jir846
1558:Staphylococcus aureus
980:Staphylococcus aureus
709:inflammatory response
693:Staphylococcus aureus
659:Staphylococcus aureus
638:Alpha-hemolysin from
573:Role during infection
547:Staphylococcus aureus
535:Staphylococcus aureus
519:Staphylococcus aureus
513:X-ray crystallography
444:Staphylococcus aureus
436:Staphylococcus aureus
433:
419:Staphylococcus aureus
386:, dissipation of the
360:Staphylococcus aureus
344:Staphylococcus aureus
340:Staphylococcus aureus
328:Staphylococcus aureus
278:phospholipid bilayers
245:(white blood cells).
232:
2298:Pulmonary surfactant
2254:Myelin basic protein
2148:Membrane-spanning 4A
1980:10.1128/IAI.00115-09
1727:FEMS Microbiol. Lett
856:that are related to
306:cytoplasmic membrane
288:Many hemolysins are
2288:Myelin protein zero
1921:2010PLoSO...511071B
1513:2011PNAS..10817314Y
1444:2011PNAS..108.7385D
1375:1996Sci...274.1859S
1212:2011BpJ...101.2679T
975:Pore-forming toxins
940:cells. TDH induces
770:autophagic response
675:Listeriolysin from
501:phosphatidylcholine
394:, and irreversible
290:pore-forming toxins
1862:J. Basic Microbiol
1780:10.4161/auto.22161
1556:"α-Hemolysin from
1165:10.1007/BF00144740
934:cell proliferation
806:and inhibition of
766:autophagic pathway
726:by the use of the
474:phosphoryl-choline
464:toxin secreted by
454:β-hemolysin (hlb;
440:
388:membrane potential
257:, leading them to
239:
191:by disrupting the
2582:
2581:
2094:membrane proteins
1554:Gouaux E (1998).
1369:(5294): 1859–66.
1340:10.1021/ci050175y
1153:Eur. J. Epidemiol
172:
171:
168:
167:
163:structure summary
16:(Redirected from
2646:
2629:Bacterial toxins
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2598:
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1701:
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1638:
1629:. Archived from
1620:
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1589:
1579:
1551:
1545:
1544:
1534:
1524:
1492:
1482:
1476:
1475:
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1455:
1419:
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1403:
1402:
1358:
1352:
1351:
1328:J Chem Inf Model
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1107:
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1100:
1094:
1090:
1088:
1080:
1044:
1038:
1037:
1027:
1004:J. Dermatol. Sci
995:
950:protein kinase C
946:protein kinase C
724:pulmonary injury
666:Aeromonas sobria
609:hemolytic anemia
459:
396:osmotic swelling
332:Escherichia coli
247:Escherichia coli
111:
53:
42:
30:
21:
2654:
2653:
2649:
2648:
2647:
2645:
2644:
2643:
2639:Protein domains
2619:
2618:
2617:
2607:
2605:
2593:
2585:
2583:
2578:
2566:
2520:Neurofibromin 2
2503:Other/ungrouped
2498:
2315:
2292:
2240:
2142:
2109:
2087:
2045:
2040:
2010:
2009:
2005:
1961:
1960:
1956:
1902:
1901:
1897:
1859:
1858:
1854:
1810:
1809:
1805:
1761:
1760:
1756:
1720:
1719:
1715:
1671:
1670:
1666:
1657:
1655:
1650:
1649:
1645:
1636:
1634:
1598:
1597:
1593:
1564:J. Struct. Biol
1553:
1552:
1548:
1507:(42): 17314–9.
1494:
1484:
1483:
1479:
1438:(18): 7385–90.
1426:Vibrio cholerae
1421:
1411:
1410:
1406:
1360:
1359:
1355:
1324:
1323:
1319:
1275:
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1249:
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1206:(11): 2679–83.
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1109:
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1104:
1091:
1081:
1069:
1046:
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997:
996:
992:
988:
966:
954:tyrosine kinase
938:colon carcinoma
932:. It regulates
910:
905:
877:
839:
827:listeriolysin O
664:Aerolysin from
579:limiting factor
575:
529:Vibrio cholerae
517:α-hemolysin of
509:
496:phosphocholines
482:
462:Phospholipase C
455:
452:
428:
423:
412:
404:pore structures
286:
274:
237:seen on a plate
216:
189:red blood cells
55:
45:
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2043:External links
2041:
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2019:(7): 1073–80.
2003:
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1754:
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594:microorganisms
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1974:(7): 2712–8.
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1968:Infect. Immun
1965:
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1817:Infect. Immun
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1683:
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1633:on 2018-09-30
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952:inhibits the
951:
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652:
648:
644:
641:
640:uropathogenic
637:
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635:
632:
630:
626:
622:
618:
614:
610:
605:
603:
599:
595:
590:
588:
584:
583:free radicals
580:
572:
570:
568:
564:
561:, as well as
560:
556:
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548:
543:
541:
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531:
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521:
520:
514:
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487:
479:
477:
475:
471:
470:sphingomyelin
467:
463:
458:
449:
447:
445:
437:
432:
425:
420:
417:
415:
409:
407:
405:
399:
397:
393:
392:ion gradients
389:
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365:
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329:
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299:
295:
291:
283:
281:
279:
271:
269:
267:
266:Streptococcus
262:
260:
256:
252:
248:
244:
236:
235:Streptococcus
233:Hemolysis by
231:
227:
225:
221:
213:
211:
209:
204:
202:
198:
194:
193:cell membrane
190:
186:
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71:
67:
63:
58:
52:
48:
41:
36:
31:
19:
2572:
2106:cytoskeleton
2096:(other than
2016:
2012:
2006:
1971:
1967:
1957:
1912:
1908:
1898:
1865:
1861:
1855:
1820:
1816:
1806:
1771:
1767:
1757:
1730:
1726:
1716:
1681:
1677:
1667:
1656:. Retrieved
1646:
1635:. Retrieved
1631:the original
1611:(3): 163–4.
1608:
1604:
1594:
1567:
1563:
1557:
1549:
1504:
1500:
1480:
1435:
1431:
1425:
1407:
1366:
1362:
1356:
1331:
1327:
1320:
1285:
1282:J. Bacteriol
1281:
1271:
1256:
1246:
1203:
1199:
1189:
1156:
1152:
1146:
1122:(1): 271–8.
1119:
1115:
1105:
1049:
1042:
1010:(2): 141–3.
1007:
1003:
993:
956:activity of
923:
917:
911:
903:Applications
886:
878:
850:
846:
840:
824:
815:
808:phagocytosis
786:
759:
750:
747:cyclodextrin
738:
731:inflammasome
716:
715:produced by
697:
691:
689:
686:
633:
613:erythrocytes
606:
591:
576:
546:
544:
533:
527:
518:
510:
489:
483:
465:
453:
443:
442:Secreted by
441:
435:
418:
413:
400:
359:
343:
335:
331:
327:
325:
313:target cells
310:
294:erythrocytes
287:
275:
263:
246:
240:
234:
223:
217:
205:
200:
180:
174:
173:
2321:Tetraspanin
869:phosphatase
793:phagocytize
702:necrotizing
629:arrhythmias
617:bloodstream
598:pathologies
480:γ-Hemolysin
450:β-hemolysin
426:α-hemolysin
364:oligomerize
323:complexes.
261:and death.
255:macrophages
181:haemolysins
60:Identifiers
2623:Categories
2525:Presenilin
2049:Hemolysins
1658:2012-11-24
1637:2007-06-17
1200:Biophys. J
986:References
889:folic acid
882:antibodies
831:phagosomes
812:chemotaxis
804:leukocytes
800:chemotaxis
789:leukocytes
755:antibodies
743:immunology
735:pyroptosis
705:infections
670:meningitis
421:hemolysins
368:permeation
298:leukocytes
243:leucocytes
214:Properties
175:Hemolysins
126:structures
68:Leukocidin
18:Hemolysins
2573:see also
2552:Dysferlin
1768:Autophagy
1493:;
1420:;
1095:ignored (
1085:cite book
919:IPR005015
875:Treatment
862:threonine
854:mutations
762:S. aureus
713:pneumonia
681:phagosome
540:octameric
507:Structure
491:IPR003963
466:S. aureus
410:Enzymatic
352:pneumonia
317:receivers
302:platelets
272:Mechanism
259:autolysis
251:cytotoxic
197:pathogens
104:IPR036435
54:).
2613:Medicine
2510:Calnexin
2115:Arrestin
2033:22543197
1998:19380475
1949:20552019
1909:PLOS ONE
1890:23325588
1798:23047465
1749:23113475
1708:22279123
1627:16912433
1541:21969538
1472:21502531
1399:45663016
1348:16309251
1251:271—276.
1238:22261056
1138:20692229
1077:15350795
1034:16199139
964:See also
930:oncology
914:InterPro
908:Medicine
851:in-vitro
847:S.aureus
822:attack.
796:bacteria
751:S.aureus
739:S.aureus
721:necrotic
717:S.aureus
698:S.aureus
647:cystitis
555:β barrel
524:β-barrel
486:InterPro
348:pathogen
321:heptamer
224:in vitro
201:in vitro
143:RCSB PDB
99:InterPro
2601:Biology
2587:Portals
2494:TSPAN34
2489:TSPAN33
2484:TSPAN32
2479:TSPAN31
2474:TSPAN30
2469:TSPAN29
2464:TSPAN28
2459:TSPAN27
2454:TSPAN26
2449:TSPAN25
2444:TSPAN24
2439:TSPAN23
2434:TSPAN22
2429:TSPAN21
2424:TSPAN20
2419:TSPAN19
2414:TSPAN18
2409:TSPAN17
2404:TSPAN16
2399:TSPAN15
2394:TSPAN14
2389:TSPAN13
2384:TSPAN12
2379:TSPAN11
2374:TSPAN10
2102:enzymes
2092:: cell
2090:Protein
1989:2708543
1940:2884019
1917:Bibcode
1882:3065477
1847:6752033
1789:3541307
1699:3274379
1586:9615434
1532:3198349
1509:Bibcode
1463:3088620
1440:Bibcode
1391:8943190
1371:Bibcode
1363:Science
1312:4964474
1229:3297801
1208:Bibcode
1181:8237698
1173:3042445
1025:1592130
916::
820:E. coli
816:in vivo
778:RAPGEF3
643:E. coli
621:fatigue
488::
460:) is a
79:PF07968
2369:TSPAN9
2364:TSPAN8
2359:TSPAN7
2354:TSPAN6
2349:TSPAN5
2344:TSPAN4
2339:TSPAN3
2334:TSPAN2
2329:TSPAN1
2246:Myelin
2236:MS4A18
2231:MS4A15
2226:MS4A14
2221:MS4A13
2216:MS4A12
2211:MS4A10
2201:MS4A8B
2191:MS4A6E
2186:MS4A6A
2176:MS4A4E
2171:MS4A4A
2104:, and
2055:(MeSH)
2031:
1996:
1986:
1947:
1937:
1888:
1880:
1845:
1838:347633
1835:
1796:
1786:
1747:
1706:
1696:
1625:
1584:
1539:
1529:
1470:
1460:
1397:
1389:
1346:
1310:
1303:276826
1300:
1236:
1226:
1179:
1171:
1136:
1075:
1065:
1032:
1022:
897:spleen
865:kinase
858:serine
655:sepsis
653:, and
457:Q2FWP1
378:, and
356:sepsis
300:, and
158:PDBsum
132:
122:
92:CL0636
65:Symbol
2535:PSEN2
2530:PSEN1
2206:MS4A9
2196:MS4A7
2181:MS4A5
2166:MS4A3
2161:MS4A2
2156:MS4A1
2133:ARRB2
2128:ARRB1
1886:S2CID
1395:S2CID
1177:S2CID
782:RAP2B
728:NLRP3
372:water
346:is a
220:fungi
185:lysis
2562:OTOF
2557:STRC
2271:PLP1
2259:PMP2
2138:ARR3
2029:PMID
2017:1820
1994:PMID
1945:PMID
1878:PMID
1843:PMID
1794:PMID
1745:PMID
1704:PMID
1623:PMID
1582:PMID
1537:PMID
1490:3b07
1468:PMID
1417:3o44
1387:PMID
1344:PMID
1308:PMID
1234:PMID
1169:PMID
1134:PMID
1120:1808
1097:help
1073:PMID
1063:ISBN
1030:PMID
942:Ca2+
893:iron
891:and
867:and
841:The
810:and
780:and
774:cAMP
625:pain
587:heme
551:axis
390:and
376:ions
354:and
151:PDBj
147:PDBe
130:ECOD
120:Pfam
88:clan
86:Pfam
74:Pfam
51:7AHL
2542:HFE
2123:SAG
2021:doi
1984:PMC
1976:doi
1935:PMC
1925:doi
1870:doi
1833:PMC
1825:doi
1784:PMC
1776:doi
1735:doi
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