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SURFIN<sub>4.2</sub> protein forms a complex with GLURP and RON4.

By Maria del Pilar Quintana (103441), Jun-Hong Ch’ng (5617079), Arash Zandian (3344603), Maryam Imam (2170612), Kjell Hultenby (183330), Michael Theisen (81720), Peter Nilsson (3305), Ulrika Qundos (3387659), Kirsten Moll (21631), Sherwin Chan (5233421) and Mats Wahlgren (21639)


<p>IP with αSURFIN<sub>4.2</sub> specifically pulls down SURFIN<sub>4.2</sub> from schizont (<b>A</b>) and merozoite (<b>B</b>) protein extract as compared with control IgGs. (<b>C)</b> IP with αSURFIN<sub>4.2</sub> also pulls down GLURP and RON4. (<b>D)</b> IP with αGLURP R2 also pulls down RON4 but not SURFIN<sub>4.2</sub>; IP with αRON4 also pulls down GLURP and SURFIN<sub>4.2</sub>. Input corresponds to the supernatant fraction after SB3-10 extraction followed by detergent removal and pre-clearing on control beads; FT: Flow-through corresponds to unbound material; E1 and 2: Eluted fraction corresponds to bound material to the antibody-coupled beads.</p

Topics: Biophysics, Biochemistry, Microbiology, Cell Biology, Molecular Biology, Evolutionary Biology, Immunology, Developmental Biology, Cancer, Infectious Diseases, Virology, Physical Sciences not elsewhere classified, merozoite invasion Plasmodium falciparum invasion, CRD, 4-GLURP, SURGE, rhoptry neck protein 4, PV, RON, SURFIN 4.2, MJ, SURFIN 4.2 forms, Glutamate Rich Protein, RBC plasma membranes, SURFIN 4.2 mediates binding, GLURP
Year: 2018
DOI identifier: 10.1371/journal.pone.0201669.g003
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Provided by: FigShare
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