Apicomplexan Pore-Forming Toxins

被引:1
作者
Carruthers, Vern B. [1 ]
机构
[1] Univ Michigan, Med Sch, Dept Microbiol & Immunol, Ann Arbor, MI 48109 USA
基金
美国国家卫生研究院;
关键词
protozoa; helminths; perforin-like proteins; saposin-like proteins; egress; cell traversal; HOST-CELL TRAVERSAL; MEMBRANE-BINDING; PLASMODIUM-BERGHEI; STRUCTURAL BASIS; PLASMA-MEMBRANE; PROTEIN; PERFORIN; PARASITE; SPOROZOITES; TRICHURIS;
D O I
10.1146/annurev-micro-041222-025939
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Pore-forming toxins (PFTs) are released by one cell to directly inflict damage on another cell. Hosts use PFTs, including members of the membrane attack complex/perforin protein family, to fight infections and cancer, while bacteria and parasites deploy PFTs to promote infection. Apicomplexan parasites secrete perforin-like proteins as PFTs to egress from infected cells and traverse tissue barriers. Other protozoa, along with helminth parasites, utilize saposin-like PFTs prospectively for nutrient acquisition during infection. This review discusses seminal and more recent advances in understanding how parasite PFTs promote infection and describes how they are regulated and fulfill their roles without causing parasite self-harm. Although exciting progress has been made in defining mechanisms of pore formation by PFTs, many open questions remain to be addressed to gain additional key insights into these remarkable determinants of parasitic infections.
引用
收藏
页码:277 / 291
页数:15
相关论文
共 72 条
  • [1] Host cell traversal is important for progression of the malaria parasite through the dermis to the liver
    Amino, Rogerio
    Giovannini, Donatella
    Thiberge, Sabine
    Gueirard, Pascale
    Boisson, Bertrand
    Dubremetz, Jean-Francois
    Prevost, Marie-Christine
    Ishino, Tomoko
    Yuda, Masao
    Menard, Robert
    [J]. CELL HOST & MICROBE, 2008, 3 (02) : 88 - 96
  • [2] Amoebapores, archaic effector peptides of protozoan origin, are discharged into phagosomes and kill bacteria by permeabilizing their membranes
    Andrä, J
    Herbst, R
    Leippe, M
    [J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY, 2003, 27 (04) : 291 - 304
  • [3] Sequential Membrane Rupture and Vesiculation during Plasmodium berghei Gametocyte Egress from the Red Blood Cell
    Andreadaki, Maria
    Hanssen, Eric
    Deligianni, Elena
    Claudet, Cyrille
    Wengelnik, Kai
    Mollard, Vanessa
    McFadden, Geoffrey I.
    Abkarian, Manouk
    Braun-Breton, Catherine
    Siden-Kiamos, Inga
    [J]. SCIENTIFIC REPORTS, 2018, 8
  • [4] BINDING OF PERFORIN TO MEMBRANES IS SENSITIVE TO LIPID SPACING AND NOT HEADGROUP
    ANTIA, R
    SCHLEGEL, RA
    WILLIAMSON, P
    [J]. IMMUNOLOGY LETTERS, 1992, 32 (02) : 153 - 158
  • [5] Isolation of a gene family that encodes the porin-like proteins from the human parasitic nematode Trichuris trichiura
    Barker, GC
    Bundy, DAP
    [J]. GENE, 1999, 229 (1-2) : 131 - 136
  • [6] Soluble Membrane Attack Complex: Biochemistry and Immunobiology
    Barnum, Scott R.
    Bubeck, Doryen
    Schein, Theresa N.
    [J]. FRONTIERS IN IMMUNOLOGY, 2020, 11
  • [7] pH-dependent perforation of macrophage phagosomes by listeriolysin O from Listeria monocytogenes
    Beauregard, KE
    Lee, KD
    Collier, RJ
    Swanson, JA
    [J]. JOURNAL OF EXPERIMENTAL MEDICINE, 1997, 186 (07) : 1159 - 1163
  • [8] Bracha Rivka, 2006, PLoS Pathog, V2, pe48, DOI 10.1371/journal.ppat.0020048
  • [10] Differential expression and localization of saposin-like protein 2 of Fasciola hepatica
    Caban-Hernandez, Kimberly
    Espino, Ana M.
    [J]. ACTA TROPICA, 2013, 128 (03) : 591 - 597