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Updated: May 31, 2026

Deciphering the Molecular Mechanism and Function of Pore-Forming Toxins Using Leishmania major
Published on: October 28, 2022
Proteomic dataset of non-specific interactors in Leishmania infantum
Wesley Klaysson Pereira Regatieri1, Camila Rolemberg Santana Travaglini Berti de Correia1, Felipe Roberti Teixeira1
1Department of Genetics and Evolution, Federal University of São Carlos, São Paulo, Brazil.
Abstract:
This dataset provides a proteomic resource of non-specific protein interactions in Leishmania infantum identified by affinity purification coupled to mass spectrometry (AP-MS/MS). Protein extracts from promastigotes expressing Cas9/T7 RNA polymerase were subjected to immunoprecipitation using HA, myc, and His affinity systems, followed by LC-MS/MS analysis. Raw spectral data were processed using MaxQuant against the L. infantum reference proteome from UniProtKB. The dataset includes raw mass spectrometry files, peptide and protein identification tables, and label-free quantification (LFQ) data, all publicly available via the ProteomeXchange Consortium under the identifier PXD067464. After data filtering, a total of 566 unique proteins were identified across all conditions, including 60 proteins consistently detected in all three affinity systems, representing putative non-specific binders. Among these, metabolism-related proteins (30%) and ribosomal components (28%) were the most abundant functional classes. This dataset provides a valuable reference for background protein binding in AP-MS/MS experiments in Leishmania, supporting improved interpretation of interactome studies and benchmarking of affinity purification strategies.
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