User:Davi de Souza/Sandbox 1
From Proteopedia
| Line 12: | Line 12: | ||
'''Functional domains and their roles''' | '''Functional domains and their roles''' | ||
| - | <scene name='97/973994/Proaerolysin/5'> | + | Using the <scene name='97/973994/Proaerolysin/5'>monomere structure (proaerolysin)</scene> as a model of study, it is possible to see that the protein has <scene name='97/973994/Proaerolysin/6'>4 domains</scene>. Domains 1 and 2 are responsible for binding to N-glycosylated phosphatidylinositol (GPI) proteins, which are present in the membranes of eukaryotic cells. Domain 1 binds to specific sugar modifications found on the GPI, while domain 2 directly binds to the glycan core located in the central portion of GPI proteins. Therefore, both domain 1 and domain 2 are involved in anchoring the aerolysin proprotein to the target cell membrane. Domain 3 is composed of a five-stranded beta sheet and a pre-stem loop, which are important for the insertion and anchoring of the protein into the cell membrane.Domain 4 is an extension of the beta sheet from domain 3, but it is opened by the C-terminal peptide (CTP), forming a twisted double-fold in the beta sheet. This conformational change induced by the CTP propeptide allows the protein to fold into its soluble form. When the CTP is cleaved from the main body of the protein, the proaerolisin oligomerizes into a heptameric ring on the target cell membrane, forming a pore. |
| - | + | ||
| - | Domains 1 and 2 are responsible for binding to N-glycosylated phosphatidylinositol (GPI) proteins, which are present in the membranes of eukaryotic cells. Domain 1 binds to specific sugar modifications found on the GPI, while domain 2 directly binds to the glycan core located in the central portion of GPI proteins. Therefore, both domain 1 and domain 2 are involved in anchoring the aerolysin proprotein to the target cell membrane. Domain 3 is composed of a five-stranded beta sheet and a pre-stem loop, which are important for the insertion and anchoring of the protein into the cell membrane.Domain 4 is an extension of the beta sheet from domain 3, but it is opened by the C-terminal peptide (CTP), forming a twisted double-fold in the beta sheet. This conformational change induced by the CTP propeptide allows the protein to fold into its soluble form. When the CTP is cleaved from the main body of the protein, the proaerolisin oligomerizes into a heptameric ring on the target cell membrane, forming a pore. | + | |
In the box at the right, it is possible to see the 4 domains painted in diferrent colors: | In the box at the right, it is possible to see the 4 domains painted in diferrent colors: | ||
Revision as of 20:18, 25 June 2023
General Aspects and function
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]. About the structure of the protein, it is known that the aerolysin can be found in the soluble form, which is the monomere unactivated called proaerolysin and in the oligomere form, unsoluble and containing the activated forms of the monomere.
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.
| |||||||||||
References
- ↑ Altwegg M, Geiss HK. Aeromonas as a human pathogen. Crit Rev Microbiol. 1989;16(4):253-86. PMID:2649316 doi:10.3109/10408418909105478
