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. 2017 Aug 17;7:8577. doi: 10.1038/s41598-017-09017-3

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© The Author(s) 2017

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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FBN30 interacts with clinically circulating Plasmodium falciparum isolates. (a) FBN30 does not bind to laboratory P. falciparum strain NF54. There is no significant difference between uninfected RBC and NF54 infected RBC in ELISA assays. (b) The ELISA data show that significantly more FBN30 bound to blood lysates from the malaria infected patients (15 individuals) than that from the uninfected human subjects (6 individuals) (p = 0.018). (c) FBN30 interacts with the cultured wild type P. falciparum ookinetes determined by IFA. Images in the first row are the control group in which the anti-FBN30 was replaced with BSA. Arrows show the location of ookinetes.