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. 2016 Nov 21;13:81. doi: 10.1186/s12977-016-0312-7

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© The Author(s) 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 4 — The entire V2 region of JRCSF is the primary determinant of JRCSF specificity towards PG9/PGT145 class of bNAbs. a Schematic representation showing swapping mutants of JRFL domains in JRCSF used in this experiment. b Sequence analysis of V2 domain of JRFL and JRCSF and position of mutants used in this experiment. c FACS-based cell surface staining assay of JRFL, JRCSF and the domain swapped mutants V1*C2 and V2*C2 with PG9 and PGT145 over a range of antibody concentrations. d Comparative binding of V2 domain mutants of JRCSF in a FACS-based cell surface assay with PG9 and PGT145 over a range of antibody concentrations. The bar diagram represents the binding of the respective antibodies to the wild type and different mutant Envs at 20 µg/ml of antibody concentration