The Apicomplexan CDC/MACPF-like pore-forming proteins
| Autor: | Kristin R. Wade, Rodney K. Tweten |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Microbiology (medical)
Host cell membrane MACPF biology Macromolecular Substances Perforin Protein Conformation Cell Virulence Microbiology Article Transmembrane protein Cell biology Infectious Diseases medicine.anatomical_structure Protein structure Host-Pathogen Interactions medicine biology.protein Protein Multimerization Complement membrane attack complex Apicomplexa |
| Zdroj: | Current Opinion in Microbiology. 26:48-52 |
| ISSN: | 1369-5274 |
| DOI: | 10.1016/j.mib.2015.05.001 |
| Popis: | Pore-forming proteins (PFPs) encompass a broad family of proteins that are used for virulence or immune defense. Members of the cholesterol-dependent cytolysins (CDCs) and membrane attack complex/perforin (MACPF) family of PFPs form large β-barrel pores in the membrane. The CDC/MACPF proteins contain a characteristic four-stranded β-sheet that is flanked by two α-helical bundles, which unfold to form two transmembrane β-hairpins. Apicomplexan eukaryotic parasites express CDC/MACPFs termed perforin-like proteins (PLPs). Here we review recent studies that provide key insights into the assembly and regulation of the Apicomplexan PLP (ApiMACPF) molecular pore-forming mechanisms, which are necessary for the osmotically driven rupture of the parasitophorous vacuole and host cell membrane, and cell traversal by these parasites. |
| Databáze: | OpenAIRE |
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