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. 2014 Feb 4;11:13. doi: 10.1186/1742-4690-11-13

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Copyright © 2014 Heigele et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. 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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Amino acid alignment of VNP- and P-Nef proteins. Nef alleles from VNPs and Ps are compared. Some conserved sequence elements in Nef, including the N-terminal myristoylation signal, the M20 and WL residues (involved in MHC-I or CD4 down-modulation, respectively), the acidic, proline-rich and diarginine motifs, a thioesterase binding site, a C-proximal adaptor-protein (AP) interaction site and a diacidic putative V1H binding site are indicated. Residues 22 and 62 are highlighted yellow. Dots specify identity with the NL4-3 Nef sequence; dashes indicate gaps introduced to optimize the alignment.