Pore-forming toxins in Cnidaria

被引:36
|
作者
Podobnik, Marjetka [1 ]
Anderluh, Gregor [1 ]
机构
[1] Natl Inst Chem, Dept Mol Biol & Nanobiotechnol, Hajdrihova 19, Ljubljana 1000, Slovenia
关键词
Pore-forming toxins; Cnidaria; Actinoporins; Aerolysin-like proteins; MACPF/CDC toxins; Cry-like toxins; JELLYFISH SEA WASP; CHOLESTEROL-DEPENDENT CYTOLYSINS; EQUINATOXIN-II; MEMBRANE-BINDING; NEMATOCYST VENOM; PROTEIN TOXIN; EVOLUTIONARY ORIGIN; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; STICHOLYSIN-II;
D O I
10.1016/j.semcdb.2017.07.026
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The ancient phylum of Cnidaria contains many aquatic species with peculiar lifestyle. In order to survive, these organisms have evolved attack and defense mechanisms that are enabled by specialized cells and highly developed venoms. Pore-forming toxins are an important part of their venomous arsenal. Along some other types, the most representative are examples of four protein families that are commonly found in other kingdoms of life: actinoporins, Cry-like proteins, aerolysin-like toxins and MACPF/CDC toxins. Some of the homologues of pore-forming toxins may serve other functions, such as in food digestion, development and response against pathogenic organisms. Due to their interesting physicochemical properties, the cnidarian pore-forming toxins may also serve as tools in medical research and nanobiotechnological applications. (C) 2017 Elsevier Ltd. All rights reserved.
引用
收藏
页码:133 / 141
页数:9
相关论文
共 50 条
  • [41] Emerging enterococcus pore-forming toxins with MHC/HLA-I as receptors
    Xiong, Xiaozhe
    Tian, Songhai
    Yang, Pan
    Lebreton, Francois
    Bao, Huan
    Sheng, Kuanwei
    Yin, Linxiang
    Chen, Pengsheng
    Zhang, Jie
    Qi, Wanshu
    Ruan, Jianbin
    Wu, Hao
    Chen, Hong
    Breault, David T.
    Wu, Hao
    Earl, Ashlee M.
    Gilmore, Michael S.
    Abraham, Jonathan
    Dong, Min
    CELL, 2022, 185 (07) : 1157 - +
  • [42] How protein engineering has revealed the molecular mechanisms of pore-forming toxins
    Evans, Jordan C.
    Tweten, Rodney K.
    PORE-FORMING TOXINS, 2021, 649 : 47 - 70
  • [43] The use of giant unilamellar vesicles to study functional properties of pore-forming toxins
    Aden, Sasa
    Snoj, Tina
    Anderluh, Gregor
    PORE-FORMING TOXINS, 2021, 649 : 219 - 251
  • [44] Role of MAPK p38 in the cellular responses to pore-forming toxins
    Porta, Helena
    Cancino-Rodezno, Angeles
    Soberon, Mario
    Bravo, Alejandra
    PEPTIDES, 2011, 32 (03) : 601 - 606
  • [45] Pharmacological Targeting of Pore-Forming Toxins as Adjunctive Therapy for Invasive Bacterial Infection
    Escajadillo, Tamara
    Nizet, Victor
    TOXINS, 2018, 10 (12):
  • [46] Structure and assembly of pore-forming proteins
    Iacovache, Ioan
    Bischofberger, Mirko
    van der Goot, F. Gisou
    CURRENT OPINION IN STRUCTURAL BIOLOGY, 2010, 20 (02) : 241 - 246
  • [47] Unraveling the Pore-Forming Steps of Pneumolysin from Streptococcus pneumoniae
    van Pee, Katharina
    Mulvihill, Estefania
    Muller, Daniel J.
    Yildiz, Oezkan
    NANO LETTERS, 2016, 16 (12) : 7915 - 7924
  • [48] pH dependence of listeriolysin O aggregation and pore-forming ability
    Bavdek, Andrej
    Kostanjsek, Rok
    Antonini, Valeria
    Lakey, Jeremy H.
    Serra, Mauro Dalla
    Gilbert, Robert J. C.
    Anderluh, Gregor
    FEBS JOURNAL, 2012, 279 (01) : 126 - 141
  • [49] Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins
    Yamashita, Daichi
    Sugawara, Takaki
    Takeshita, Miyu
    Kaneko, Jun
    Kamio, Yoshiyuki
    Tanaka, Isao
    Tanaka, Yoshikazu
    Yao, Min
    NATURE COMMUNICATIONS, 2014, 5
  • [50] Pore-forming toxins: Properties, diversity, and uses as tools to image sphingomyelin and ceramide phosphoethanolamine
    Yamaji-Hasegawa, Akiko
    Hullin-Matsuda, Francoise
    Greimel, Peter
    Kobayashi, Toshihide
    BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2016, 1858 (03): : 576 - 592