TY  - JOUR
AU  - Burda, Paul-Christian
AU  - Crosskey, Thomas
AU  - Lauk, Katharina
AU  - Zurborg, Aimo
AU  - Söhnchen, Christoph
AU  - Liffner, Benjamin
AU  - Wilcke, Louisa
AU  - Pietsch, Emma
AU  - Strauss, Jan
AU  - Jeffries, Cy M.
AU  - Svergun, Dmitri I.
AU  - Wilson, Danny W.
AU  - Wilmanns, Matthias
AU  - Gilberger, Tim-Wolf
TI  - Structure-Based Identification and Functional Characterization of a Lipocalin in the Malaria Parasite Plasmodium falciparum
JO  - Cell reports
VL  - 31
IS  - 12
SN  - 2211-1247
CY  - [New York, NY]
PB  - Elsevier
M1  - PUBDB-2020-02482
SP  - 107817 -
PY  - 2020
N1  - PIF-2018-87
AB  - Proteins of the lipocalin family are known to bind small hydrophobic ligands and are involved in various physiological processes ranging from lipid transport to oxidative stress responses. The genome of the malaria parasite Plasmodium falciparum contains a single protein PF3D7_0925900 with a lipocalin signature. Using crystallography and small-angle X-ray scattering, we show that the protein has a tetrameric structure of typical lipocalin monomers; hence we name it P. falciparum lipocalin (PfLCN). We show that PfLCN is expressed in the intraerythrocytic stages of the parasite and localizes to the parasitophorous and food vacuoles. Conditional knockdown of PfLCN impairs parasite development, which can be rescued by treatment with the radical scavenger Trolox or by temporal inhibition of hemoglobin digestion. This suggests a key function of PfLCN in counteracting oxidative stress-induced cell damage during multiplication of parasites within erythrocytes.
LB  - PUB:(DE-HGF)16
C6  - pmid:32579913
UR  - <Go to ISI:>//WOS:000543381400031
DO  - DOI:10.1016/j.celrep.2020.107817
UR  - https://bib-pubdb1.desy.de/record/441413
ER  -