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. 2021 Jul 15;13(7):1375. doi: 10.3390/v13071375

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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VP40 cysteine mutants have increased binding to the anionic lipid phosphatidylserine. (A) Representative SDS-PAGE of supernatant (SN) and pellet (P) samples from an large unilamellar vesicle (LUV) pelleting assay (control: DPPC:cholesterol:danyslPE (49:49:2), 5% PI(4,5)P₂: (DPPC:cholesterol:PI(4,5)P₂:dansylPE (46.5:46.5:5:2), or 40% POPS: DPPC:cholesterol:POPS:dansylPE (29:29:40:2)) with VP40-WT, VP40-C311A, VP40-C314A, and VP40-C311A/C314A. (B) Fraction of VP40 bound to lipids (P/(SN + P)) is shown as the average fraction bound over three independent experiments. Error bars represent the standard error of the mean, and * marks significance of a p value of 0.05 or less.