ArticleThe Biochemical journal2003
Amoebapores and NK-lysin, members of a class of structurally distinct antimicrobial and cytolytic peptides from protozoa and mammals: a comparative functional analysis.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 70 citations in OpenAlex.
- Study of microbe-microbe interactions between the sexually transmitted parasitebioRxiv : the preprint server for biology · 2026Article
- An ancient lysozyme in placozoans participates in acidic extracellular digestion.Communications biology · 2026Article
- Article
- pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents.Pharmaceuticals (Basel, Switzerland) · 2016Review
- Immune Response of Amebiasis and Immune Evasion by Entamoeba histolytica.Frontiers in immunology · 2016Review
- Chew on this: amoebic trogocytosis and host cell killing by Entamoeba histolytica.Trends in parasitology · 2015Review
- Article
- Regulation of virulence of Entamoeba histolytica.Annual review of microbiology · 2014Review
- Structure-function correlations of pulmonary surfactant protein SP-B and the saposin-like family of proteins.European biophysics journal : EBJ · 2013Review
- Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba.Nature chemical biology · 2013Article
- Surfactant protein B propeptide contains a saposin-like protein domain with antimicrobial activity at low pH.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- An ex-vivo human intestinal model to study Entamoeba histolytica pathogenesis.PLoS neglected tropical diseases · 2009Article
- A short guided tour through functional and structural features of saposin-like proteins.The Biochemical journal · 2005Review
- Biophysical characterization of endotoxin inactivation by NK-2, an antimicrobial peptide derived from mammalian NK-lysin.Antimicrobial agents and chemotherapy · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amoebapores, the pore-forming polypeptides of the protozoan parasite Entamoeba histolytica, and NK-lysin, an effector molecule of porcine NK (natural killer) and cytotoxic T cells, belong to the same protein family, the saposin-like proteins. As both types of protein are implicated in the killing of microbes in vivo, it appears that phylogenetically diverse organisms such as amoebae and mammals use similar effector molecules to fulfil a comparable task. However, structural features have led to the assumption that the proteins display their activities according to different modes of action. To address this question, we analysed the antibacterial, cytotoxic and pore-forming activities of these proteins in parallel and in comprehensive detail. Interestingly, the comparison of activities revealed significant differences. Whereas NK-lysin, recombinantly expressed, is efficient at a broad range of pH values, the amoebapores exhibited a pronounced pH dependence of all their activities, with markedly decreased activity at pH values above 6. Moreover, increasing salinity affects amoebapores more drastically than NK-lysin. All of the proteins compared were found to be potently active against Gram-positive bacteria, but only NK-lysin was equally efficient against Gram-negative bacteria. However, the amoebapores displayed five times higher pore-forming activity than NK-lysin, which is in accordance with the more hydrophobic character of the amoebapores compared with the essentially cationic NK-lysin.
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