The Apicomplexan CDC/MACPF-like pore-forming proteins.

Kristin R Wade, Rodney K Tweten

Journal: Current opinion in microbiology 2016;26():48-52

PMID: 26025132

Free Full Text on PubMed Central View on PubMed

Abstract

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.

Address: Department of Microbiology and Immunology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA.; Department of Microbiology and Immunology, The University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. Electronic address: [email protected].

DOI: 10.1016/j.mib.2015.05.001

Link outs

Free resources

Full Text Sources:

Other Literature Sources:

https://scite.ai/reports/26025132

Research Materials:

https://antibodies.cancer.gov/detail/CPTC-PTHrP-1

Subscription / membership required

Full Text Sources:

MeSH Terms: Apicomplexa, Host-Pathogen Interactions, Macromolecular Substances, Perforin, Protein Conformation, Protein Multimerization