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. 2015 May 12;6(3):e00453-15. doi: 10.1128/mBio.00453-15

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Copyright © 2015 Moradali et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited.

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FIG 3 — Localization, stability, and protein-protein interaction of Alg44 variants. (A) Schematic view of the deleted or point-mutated region of Alg44. (B) Immunoblots of the envelope fraction developed using anti-Alg44 (upper) and anti-His tag (lower) antibodies showed with the various Alg44 variants localized to the envelope fraction (immunoblot B, lanes 1 to 3). Lanes 4 to 7 represent negative and positives controls (blot C, lanes 1 to 4). Immunoblots suggested protein-protein interaction of Alg44 variants with Alg8, AlgK, and AlgX by using pulldown experiments using His-tagged variants of Alg44. C-terminal deletion of Alg44 had a destabilizing effect on Alg8. Immunoblots were developed using anti-Alg8 (1), anti-AlgK (2), and anti-AlgX (3) antibodies, respectively. Asterisks indicate full-length Alg44. 300, PDO300; MCS5, pBBR1MCS-5; ab, antibody; Co+/−, positive/negative control.