Autor: |
Asad, Mohd, Yamaryo-Botté, Yoshiki, Hossain, Mohammad E., Thakur, Vandana, Jain, Shaifali, Datta, Gaurav, Botté, Cyrille Y., Mohmmed, Asif |
Rok vydání: |
2021 |
DOI: |
10.6084/m9.figshare.15153716 |
Popis: |
Additional file 1: Table S1. List of putative phospholipases in P. falciparum, their expression pattern in different parasite stages and domain architecture. Figure S1. Clustal W alignment of amino acid sequences of lysophospholipase (LPL1) homologues from different species of Plasmodium. Figure S2. Clustal W alignment of amino acid sequences showing the conserved GXSXG motif in homologues of LPL1. Figure S3. Biochemical characterization of recombinant PfLPL1. Figure S4. Fluorescent and time-lapse microscopy to show localization as well as trafficking of PfLPL1-RFA fusion protein in transgenic P. falciparum parasites. Figure S5. Structured illumination microscopy (SIM) images of live transgenic parasites showing labelling of membranes in infected RBCs and localization of PfLPL1. Figure S6. Generation of transgenic parasites expressing PfLPL1 with ddFKBP degradation domain tag, PiLPLl-DD parasite line. Figure S7. Expression and localization of the PfLPLl-DD fusion protein in transgenic parasites. Figure S8. Inducible knock-down of PfLPL1 protein in the PfLPL1-DD transgenic parasites and its effect on growth and development of the parasites. Figure S9. Replicative data sets for Fig. 5C. Figure S10. Replicative data sets for Fig. 6A and 6B. Figure S11. Host-derived LPC is not able to complement PfLPL1 iKO. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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