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. 2017 Jul 10;8:16044. doi: 10.1038/ncomms16044

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Copyright © 2017, The Author(s)

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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(a) Silver-stained SDS-PAGE of material eluted from IPs of crosslinked PfEMP1F and PfEMP1B parasite lysates. Examples of protein bands enriched in the PfEMP1B eluate are marked with asterisks. Full-length PfEMP1F and PfEMP1B are indicated with arrows. Molecular masses are shown in kDa. (b) Peptides identified by tandem mass spectrometry in PfEMP1B IPs sorted according to function or known localization of the parent proteins. (c) Relative abundance of co-precipitated PTEX components with PfEMP1B as determined by dividing the number of peptides identified by the number of amino acids (a.a.) of the individual PTEX proteins. (d) Human peptide matches identified in PfEMP1B IPs sorted according to the functions of the parent proteins. (e) The top 10 human proteins (by fold enrichment) identified in PfEMP1B IPs. (b–e) Peptide numbers are based on averages from two independent experiments. All identified proteins are listed in Supplementary Tables 1 and 2.