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Analysis of structure and function of the giant protein Pf332 in Plasmodium falciparum

Hodder, Anthony N.; Maier, Alex; Rug, Melanie; Brown, Monica; Hommel, Mirja; Pantic, Ivan; Puig-de-Morales-Marinkovic, Marina; Smith, Brian J.; Triglia, Tony; Beeson, James G; Cowman, A

Description

Virulence of Plasmodium falciparum, the most lethal parasitic disease in humans, results in part from adhesiveness and increased rigidity of infected erythrocytes. Pf332 is trafficked to the parasite-infected erythrocyte via Maurer's clefts, structures for protein sorting and export in the host erythrocyte. This protein has a domain similar to the Duffy-binding-like (DBL) domain, which functions by binding to receptors for adherence and invasion. To address structure of the Pf332 DBL domain, we...[Show more]

CollectionsANU Research Publications
Date published: 2009
Type: Journal article
URI: http://hdl.handle.net/1885/79748
Source: Molecular Microbiology
DOI: 10.1111/j.1365-2958.2008.06508.x

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