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Structure
Aerolysin is a pore-forming protein (PFT) belonging to the beta-PFT family. It is a protein that is secreted by the bacterium as a water-soluble protein. It binds to receptors on its target cell membrane and, upon proteolytic activation, forms oligomers that insert into the plasma membrane. The soluble monomer has a molecular weight of 52 kDa, and its structure has been resolved by X-ray crystallography.
Its secondary structure is predominantly composed of beta sheets. These beta sheets fold and organize into a characteristic conformation, forming a hollow cylindrical structure. This cylindrical conformation is functionally important as it allows the protein to permeabilize the cell membrane and form pores. Regarding the tertiary structure, aerolysin is a compact globular protein. It has several antiparallel beta helices that organize into a cylindrical structure, enclosing a central cavity. This central cavity is believed to be the region responsible for the protein's interaction with the cell membrane and pore formation. As for the quaternary structure, aerolysin is typically found in an oligomeric configuration, with the active form consisting of 4 to 6 subunits that associate to form the quaternary complex.
Regarding the functional domains, it is known that aerolysin has 4 domains. Domains 1 and 2 are responsible for binding to glycosylphosphatidylinositol (GPI) proteins, which act as aerolysin receptors. Domain 2 binds directly to the GPI anchor glycan core, while domain 1 binds to sugar modifications present on the receptor. Domain 3 consists of a five-stranded beta sheet and a pre-stem loop, which is curled against the beta sheet to form the transmembrane beta barrel. Domain 4 is an extension of the beta sheet of domain 3 and is opened by the C-terminal peptide (CTP) into a twisted double-fold of the beta sheet. The CTP is a propeptide present in the secreted form of aerolysin and needs to be cleaved by proteases for the toxin to be activated. The protein has a predominant beta sheet (β) structure, comprising 40% of its composition, and 17% alpha helix (α).
Function
Aerolysin plays several roles in the pathogenicity of Aeromonas spp. One of its main functions is its ability to promote lysis (rupture) of host cells, such as epithelial cells and immune cells. Aerolysin exhibits cytotoxic activity, causing damage to the cell membranes of host cells, which can lead to cell death and contribute to the bacterium's pathogenicity.
Furthermore, aerolysin may be involved in the invasion and dissemination of the bacterium within the host. It can assist in tissue degradation, facilitating the bacterium's invasion into different organs and tissues of the host.
It is important to note that the exact function of aerolysin may vary among different species and strains of Aeromonas. Additionally, there are other proteins and virulence factors produced by Aeromonas spp. that also play important roles in the pathogenicity of these bacteria.
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