Clostridium perfringens delta toxin is sequence related to beta toxin, NetB, and Staphylococcus pore-forming toxins, but shows functional differences.
Clostridium perfringens delta toxin is sequence related to beta toxin, NetB, and Staphylococcus pore-forming toxins, but shows functional differences.
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灌注芽孢杆菌三角毒素是与β毒素,NETB和葡萄球菌形成孔形成毒素有关的序列,但显示功能差异。
DOI:
10.1371/journal.pone.0003764
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发表时间:
2008
期刊:
影响因子:
3.7
通讯作者:
Popoff MR
中科院分区:
文献类型:
--
作者:
Manich M;Knapp O;Gibert M;Maier E;Jolivet-Reynaud C;Geny B;Benz R;Popoff MR
Clostridium perfringens produces numerous toxins, which are responsible for severe diseases in man and animals. Delta toxin is one of the three hemolysins released by a number of C. perfringens type C and possibly type B strains. Delta toxin was characterized to be cytotoxic for cells expressing the ganglioside GM2 in their membrane. Here we report the genetic characterization of Delta toxin and its pore forming activity in lipid bilayers. Delta toxin consists of 318 amino acids, its 28 N-terminal amino acids corresponding to a signal peptide. The secreted Delta toxin (290 amino acids; 32619 Da) is a basic protein (pI 9.1) which shows a significant homology with C. perfringens Beta toxin (43% identity), with C. perfringens NetB (40% identity) and, to a lesser extent, with Staphylococcus aureus alpha toxin and leukotoxins. Recombinant Delta toxin showed a preference for binding to GM2, in contrast to Beta toxin, which did not bind to gangliosides. It is hemolytic for sheep red blood cells and cytotoxic for HeLa cells. In artificial diphytanoyl phosphatidylcholine membranes, Delta and Beta toxin formed channels. Conductance of the channels formed by Delta toxin, with a value of about 100 pS to more than 1 nS in 1 M KCl and a membrane potential of 20 mV, was higher than those formed by Beta toxin and their distribution was broader. The results of zero-current membrane potential measurements and single channel experiments suggest that Delta toxin forms slightly anion-selective channels, whereas the Beta toxin channels showed a preference for cations under the same conditions. C. perfringens Delta toxin shows a significant sequence homolgy with C. perfringens Beta and NetB toxins, as well as with S. aureus alpha hemolysin and leukotoxins, but exhibits different channel properties in lipid bilayers. In contrast to Beta toxin, Delta toxin recognizes GM2 as receptor and forms anion-selective channels.
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DOI:
10.1016/s0925-4439(99)00026-5
发表时间:
1999-05-31
影响因子:
6.2
作者:
Nagahama, M;Kihara, A;Sakurai, J
通讯作者:
Sakurai, J
影响因子:
2.7
作者:
Geny, Blandine;Popoff, Michel R.
通讯作者:
Popoff, Michel R.
DOI:
10.1016/0005-2736(89)90002-3
发表时间:
1979-01-01
期刊:
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子:
--
作者:
BENZ, R;JANKO, K;LAUGER, P
通讯作者:
LAUGER, P
影响因子:
2.9
作者:
Heuck, AP;Tweten, RK;Johnson, AE
通讯作者:
Johnson, AE
影响因子:
2.3
作者:
JOLIVETREYNAUD, C;ESTRADA, J;CHEDID, L
通讯作者:
CHEDID, L