Interactions between membranes and cytolytic peptides.
The physico-chemical and biological properties of cytolytic peptides derived from diverse living entities have been discussed. The principal sources of these agents are bacteria, higher fungi, cnidarians (coelenterates) and the venoms of snakes, insects and other arthropods. Attention has been directed to instances in which cytolytic peptides obtained from phylogenetically remote as well as from related sources show similarities in nature and/or mode of action (congeneric lysins). The manner in which cytolytic peptides interact with plasma membranes of eukaryotic cells, particularly the membranes of erythrocytes, has been discussed with emphasis on melittin, thiolactivated lysins and staphylococcal alpha-toxin. These and other lytic peptides are characterized in Table III. They can be broadly categorized into: (a) those which alter permeability to allow passage of ions, this process eventuating in colloid osmotic lysis, signs of which are a pre-lytic induction or latent period, pre-lytic leakage of potassium ions, cell swelling and inhibition of lysis by sucrose. Examples of lysins in which this mechanism is involved are staphylococcal alpha-toxin, streptolysin S and aerolysin; (b) phospholipases causing enzymic degradation of bilayer phospholipids as exemplified by phospholipases C of Cl. perfringens and certain other bacteria; (c) channel-forming agents such as helianthin, gramicidin and (probably) staphylococcal delta-toxin in which toxin molecules are thought to embed themselves in the membrane to form oligomeric transmembrane channels.
D000408:Alamethicin / Q000494:pharmacology; D000818:Animals; D000862:Ant Venoms; D001180:Arthropod Venoms / Q000494:pharmacology; D001426:Bacterial Proteins; D001427:Bacterial Toxins / Q000494:pharmacology; D001487:Basidiomycota; D002462:Cell Membrane / Q000648:ultrastructure*; D003064:Cnidarian Venoms / Q000494:pharmacology; D001517:Coleoptera; D003603:Cytotoxins / Q000145:classification / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000648:ultrastructure; D006096:Gramicidin / Q000494:pharmacology; D006460:Hemolysin Proteins; D036341:Intercellular Signaling Peptides and Proteins; D046911:Macromolecular Substances; D008387:Marine Toxins / Q000494:pharmacology; D008555:Melitten / Q000494:pharmacology; D008854:Microscopy, Electron; D009183:Mycotoxins / Q000494:pharmacology; D010455:Peptides / Q000494:pharmacology; D010739:Phospholipase D / Q000494:pharmacology; D010741:Phospholipases A / Q000494:pharmacology; D052899:Pore Forming Cytotoxic Proteins; D011487:Protein Conformation; D037401:Scyphozoa; D012910:Snake Venoms / Q000494:pharmacology; D013301:Streptolysins / Q000494:pharmacology; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D010738:Type C Phospholipases / Q000494:pharmacology; D014733:Vibrio; D014862:Wasp Venoms / Q000494:pharmacology
D000862:Ant Venoms; D001180:Arthropod Venoms; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D003064:Cnidarian Venoms; D003603:Cytotoxins; D006460:Hemolysin Proteins; D036341:Intercellular Signaling Peptides and Proteins; D046911:Macromolecular Substances; D008387:Marine Toxins; D009183:Mycotoxins; D010455:Peptides; D052899:Pore Forming Cytotoxic Proteins; D012910:Snake Venoms; D013301:Streptolysins; D013438:Sulfhydryl Compounds; D014862:Wasp Venoms; C044299:bombolitins; C021091:staphylococcal alpha-toxin; C025971:staphylococcal delta toxin; C026050:streptolysin S; D006096:Gramicidin; D008555:Melitten; D000408:Alamethicin; C032676:aerolysin; C037500:mastoparan; C049465:barbatolysin; C039439:diamphotoxin; C042521:crabrolin; D010741:Phospholipases A; D010738:Type C Phospholipases; D010739:Phospholipase D