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. Author manuscript; available in PMC: 2019 Mar 1.
Published in final edited form as: J Cell Physiol. 2017 Aug 28;233(3):2343–2359. doi: 10.1002/jcp.26106

Fig. 9. The majority of the charged residues on the hydrophilic surface play critical roles Agno release.

Fig. 9

Fig. 9

(A) The expression analysis of the charged residue mutants located on the hydrophilic surface by Western blot as describe for Fig. 5A. (B) The intensities of the band for Agno on Western blots on panel A were quantified and graphed as described for Fig. 5B. (C) The release analysis of the mutants by Western blotting as described for Fig. 5C. (D) The intensities of Agno bands on Western blots on panel C were quantified and graphed as described for Fig. 5D. **** P< 0.001: indicates statistical differences between the Agno WT and mutant samples. (E) Locations of the amino acid residues involved in Agno release on hydrophilic surface are illustrated by a fill-in representation format of Agno structure. (F) Positions of all the amino acid residues involved or not involved in Agno release are illustrated by a fill-in representation format of Agno structure. (G) Amino acid sequence comparison for JCV, BKV and SV40 Agno primarily in the major alpha helix area. Amino acid residues involved in Agno release are encased in boxes and numbered.