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Wottrich et al. Microbiome Res Rep 2024;3:27  https://dx.doi.org/10.20517/mrr.2023.42  Page 13 of 17







































                Figure 6. The predicted structure of Aquarius gp41 resembles factors that facilitate protein-protein interactions. (A) Aquarius
                gp41structure predicted by AlphaFold2. Structure is colored by confidence and functional motifs are labeled; (B) Closest structural
                homologs to Aquarius gp41 as determined by the DALI structural homology server - Vir8B (Green: pdbid is 6IQT) and mouse Cystatin
                (orange:pdbid 6UIO); (C) Structural alignment between gp41 95-179 (blue) and mouse cystatin (orange); (D) Electrostic potential was
                solved using the APBS for Aquarius gp41 (left) and TP-J34 Ltp (right). Electrostatic potential scale is given in kT/e where negative (red)
                and positive (blue) surface potentials are shown. APBS: Adaptive Poisson-Boltzmann Solver.




























                Figure 7. Gp41 expression relative to the uninfected control. The average fold increase in phage Aquarius gp41 mRNA expression
                averaged over three PCR trials, normalized to the bacterial housekeeping gene  RecA. A one-way ANOVA with post hoc Tukey HSD
                                                                                        *
                comparison indicated a significant difference between the active infection and pseudolysogen groups ( P < 0.05). Error bars the
                Standard Error.
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