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== Structure ==
== 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.
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.
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Its secondary structure is predominantly composed of <scene name='97/973994/Betasheet/1'>beta sheets</scene>. 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 7 <scene name='97/973994/Monomero_2/1'>subunits</scene> that associate to form the quaternary complex.
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Its secondary structure is predominantly composed of <scene name='97/973994/Betasheet/1'>beta sheets</scene>. These beta sheets fold and organize into a characteristic conformation, forming a <scene name='97/973994/Folhasbetas/1'>hollow cylindrical</scene> 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 7 <scene name='97/973994/Monomero_2/1'>subunits</scene> that associate to form the quaternary complex.

Revision as of 18:08, 24 June 2023

Abstract

Aerolysin is a protein synthesized by some species of bacteria belonging to the genus Aeromonas, such as Aeromonas hydrophila. The exact function of Aerolysin may vary among different species and strains of Aeromonas. However, it is evident that it is the main macromolecule responsible for the pathogenicity of Aeromonas hydrophila, being associated with diarrheal diseases and deep wound infections [1].

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.


Oligomer strucuture of Aerolysin

Drag the structure with the mouse to rotate

References

  1. ↑ Altwegg M, Geiss HK. Aeromonas as a human pathogen. Crit Rev Microbiol. 1989;16(4):253-86. PMID:2649316 doi:10.3109/10408418909105478
  2. ↑ Iacovache I, De Carlo S, Cirauqui N, Dal Peraro M, van der Goot FG, Zuber B. Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process. Nat Commun. 2016 Jul 13;7:12062. doi: 10.1038/ncomms12062. PMID:27405240 doi:http://dx.doi.org/10.1038/ncomms12062
  3. ↑ Parker MW, Buckley JT, Postma JP, Tucker AD, Leonard K, Pattus F, Tsernoglou D. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature. 1994 Jan 20;367(6460):292-5. PMID:7510043 doi:http://dx.doi.org/10.1038/367292a0
  4. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  5. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

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