Abstract
The hydrocoral Millepora alcicornis, known as fire coral, biosynthesize protein toxins with phospholipase A2 (PLA2) activity as a main defense mechanism; proteins that rapidly catalyse the hydrolysis at the sn-2 position of phosphatidylcholine-type phospholipids of cellular membranes. This hydrolysis mechanism triggers a structural damage in the outer leaflet of the red blood cells (RBC) membrane, by generating pores in the lipid bilayer that leads to a depletion of the cellular content of the damaged cell. A secondary mechanism, tentatively caused by pore-forming proteins toxins (PFTs), has been observed. The use of atomic force microscopy (AFM) has allowed to visualize the evolution of damages produced on the surface of the cells at the nanoscale level along the time.
Highlights
The hydrocoral Millepora alcicornis (Linnaeus, 1758) known as fire coral has an amphi-Atlantic distribution as evidenced by its presence in the Caribbean, Brazil, Bermuda, Ascension Island[1], Cape Verde Islands[2], Canary Islands[3] and Madeira Island[4]
The fire coral, Millepora alcicornis, causes hemolytic effects upon contact attributed to the biosynthesis of proteins of the phosholipase A2 (PLA2) type as a main defense mechanism
These proteins rapidly catalyse the hydrolysis at the sn-2 position of the glycerol moiety of phosphatidylcholine-type phospholipids of cellular membranes
Summary
The red blood cell (RBC) membrane comprises a typical lipid bilayer. This lipid bilayer is composed of cholesterol and phospholipids in equal proportions by weight. In the outer leaflets phosphatidylcholine (PC) and sphingomyelin (SM) predominate; whereas phosphatidylethanolamine (PE), phosphatidylserine (PS) and phosphoinositol (PI) constitute the inner leaflets of the bilayer section (Fig. 2). This lipid composition determines the physical properties of the membrane, such as permeability and fluidity. In RBCs, spectrin forms a hexagonal arrangement, forming a scaffold and playing an important role in the maintenance of plasma membrane integrity and cytoskeletal structure (Fig. 3). When the structure is observed in a small scale (Fig. 6b) a very flat surface with a
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