Preferential binding of 4-hydroxynonenal to lysine residues in specific parasite proteins in plakortin-treated Plasmodium falciparum-parasitized red blood cells.

Evelin Schwarzer,Valentina Gallo,Elena Valente,Daniela Ulliers,Oleksii A Skorokhod,Orazio Taglialatela-Scafati,Paolo Arese

doi:10.1016/j.dib.2015.11.003

Evelin Schwarzer, Valentina Gallo + Show 5 more

Open Access

https://doi.org/10.1016/j.dib.2015.11.003

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Abstract

The data show the frequencies by which the amino acid residues lysine, histidine and cysteine of six proteins of the malaria parasite Plasmodium falciparum are post-translationally modified by the lipoperoxydation endproduct 4-hydroxynonenal after challenging the parasitized red blood cell with plakortin. Plakortin is an antimalarial endoperoxide whose molecular anti-parasitic effect is described in Skorokhod et al. (2015) [1]. Plakortin did not elicit hemoglobin leakage from host red blood cells and did not oxidize reduced glutathione.

Highlights

The data show the frequencies by which the amino acid residues lysine, histidine and cysteine of six proteins of the malaria parasite Plasmodium falciparum are post-translationally modified by the lipoperoxydation endproduct 4-hydroxynonenal after challenging the parasitized red blood cell with plakortin
There is no particular imbalance between the portion of 4-HNE-conjugated amino acids in the proteins extracted from plakortin treated parasites
Culture of red blood cells (RBC) infected with trophozoite-stage Plasmodium falciparum were treated with 0-10 μM of plakortin and hemoglobin release was measured in culture supernatant (Figure 1)

Summary

Experimental features

Data source location Data accessibility cell culture up to 24 h. Thiol-reaction with DTNB and OD at 412 nm. Mass spectrometric analysis of peptides after trypsin-digestion of proteins

Value of the data

Data for hemoglobin release from RBC under plakortin treatment

Hemoglobin quantification

Findings

Preparation of protein extracts from pRBC