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pntd.0008458.g001.tif (2.61 MB)

Schematic representation of constructs used in this study.

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posted on 2020-07-09, 17:54 authored by Juan F. Quintana, Juan Bueren-Calabuig, Fabio Zuccotto, Harry P. de Koning, David Horn, Mark C. Field

A) 3D structural predictions of the AQP2 harbouring three haemagglutinin tags at either terminus. Top panel; lateral and cytoplasmic face view of simulated model of T. brucei AQP2 tetramer embedded in a POPC lipid bilayer. Lipids are shown in surface and line representations in cyan. Each monomer of AQP2 is shown in cartoon representation. Bottom panel; lateral and cytoplasmic face view of T. brucei AQP2 showing key amino acids (in spheres) from NSA (cyan), NPS (orange) and IVLL (magenta) domains. B) N- and C-terminal tagged TbAQP2 variants with a tandem of three hemagglutinin (3xHA) epitopes. Positions of predicted trans-membrane domains (TMD) are indicated with numbers above solid blocks. Similarly, lysine residues that were manipulated in this study are highlighted. C) Wild type TbAQP1 (blue), TbAQP2 (grey), TbAQP3 (green), and chimeras used (40AT, AQP2TMD4, and AQP2TMD5). TMDs for AQP1, 2 and 3 are shown as blocks and in blue, grey and green, respectively.

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