Abstract:
:The cyclophilins are a large family of proteins implicated in folding, transport and regulation of other proteins and are potential drug targets in cancer and in some viral and parasitic infections. The functionality of cyclophilins appears to depend on peptidyl-prolyl cis-trans isomerase (foldase) and/or molecular chaperone activities. In this study we assessed the peptidyl-prolyl isomerase and chaperone activities of 8 members of the Plasmodium falciparum cyclophilin family, all produced recombinantly using a common host/vector system. While only two of these proteins had isomerase activity, all of them displayed chaperone function as judged by the ability to prevent the thermal aggregation of model substrates. We suggest that the cyclophilins constitute a family of molecular chaperones in malarial parasites that complement the functions of other chaperones such as the heat-shock proteins.
journal_name
Mol Biochem Parasitoljournal_title
Molecular and biochemical parasitologyauthors
Marín-Menéndez A,Monaghan P,Bell Adoi
10.1016/j.molbiopara.2012.04.006subject
Has Abstractpub_date
2012-07-01 00:00:00pages
44-7issue
1eissn
0166-6851issn
1872-9428pii
S0166-6851(12)00099-0journal_volume
184pub_type
杂志文章abstract::The origin of membraneous structures in the cytoplasm of human erythrocytes infected with the malaria parasite, Plasmodium falciparum, was determined by confocal fluorescence imaging microscopy. When infectious merozoites invaded erythrocytes labeled with the fluorescent, lipophilic, non-exchangeable molecules DiIC16 ...
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