Fig. 2

In vitro activity of the EntF* peptide. a The relative importance of the amino acids of EntF* on E-cadherin expression ranked in five different classes. Ranking (blue to red: increasing significance) was performed using the Fisher’s LSD p-values, which was confirmed using the Jenks natural breaks algorithm. Based on ranking, it is likely that the first, second and tenth amino acid of EntF* are the most important residues for EntF* activity. b Alignment between EntF* and the active domain of CXCL12. Black amino acids with a line indicate a match. Dark grey amino acids with two dots mark a similarity between the two residues. Light grey amino acids with one dot are not similar, but no gap is formed. c Antagonistic effects of Nef-M1 on EntF*-mediated E-cadherin downregulation in HCT-8 cells (EntF* n = 15; Nef-M1 n = 6; EntF* + Nef-M1 n = 6). Statistically significant differences were determined by a one-sided student's t test. d Antagonistic effects of EntF*1A on EntF*-mediated E-cadherin downregulation in HCT-8 cells (EntF* n = 15; EntF*1A n = 18; EntF* + EntF*1A n = 6). Statistically significant differences were determined by a one-sided Student’s t test. e Effect of EntF* on E-cadherin expression. A significant decrease in E-cadherin levels following EntF* or CXCL12 treatments was observed in HT-29 (n = 12), Caco-2 (n = 6) and HCT-8 (n = 15) cells. Statistically significant differences were determined by one-way ANOVA test. f Proposed E-cadherin-regulating pathway for EntF*. Schematic representation of the CXCR4 receptor and its signaling pathways, leading to the activation of EMT transcription factors, followed by the downregulation of E-cadherin expression (see also Additional file 5: Fig. S5)