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. 2016 Apr 15;8(4):101. doi: 10.3390/v8040101

Figure 1.

Figure 1

A functional SH3 binding motif in the non-structural protein-1 (NS1) is required for interaction with Crk-like adapter protein (CrkL) in influenza A virus (IAV)-infected cells. (A) The consensus sequence of class II SH3 binding motif, and its presence (+) or absence (−) in the C-terminal region (residues 212–217 shown) of NS1 proteins of the recombinant IAV strains used in this study. In SH3 binding consensus x indicates any residue, ɸ a hydrophopic residue, and + a positively charged amino acid, which for Crk-family SH3 domains is preferable a lysine residue; (B,C) Co-immunoprecipation of NS1 proteins with CrkL from lysates of A549 cells infected with recombinant A/WSN-based IAV strains expressing wild-type or mutant NS1 proteins derived from A/Mallard (B) or A/WSN (C) for 24 h at a multiplicity of infections (MOI) 2. Note that these NS1 proteins naturally differ in their SH3 binding capacity, and the mutations introduced in them thus have opposite effects. NS1 and nucleoprotein (NP) blots from whole cell extracts (WCE) before anti-CrkL immunoprecipitation are shown to control equal infection of the cells by the different viruses.