Fig. 1: Purified bacterial GDEs support L. crispatus growth on glycogen.
From: Bacterial amylases enable glycogen degradation by the vaginal microbiome
a, Predicted domains in putative vaginal bacterial extracellular GDEs. α-amylase, α-amylase catalytic domain (GH13); C-malt, cyclomaltodextrinase domain. b, Growth of L. crispatus C0176A1 (pulA−, JAEDCG000000000) and MV-1A-US (pulA+) on different carbon sources. c, L. crispatus C0176A1 (pulA−) grown on oyster glycogen supplemented with 200 nM purified L. crispatus PulA. d, 24 h OD600 values of L. crispatus C0176A1 (pulA−) grown on glucose, maltose or glycogen supplemented with 200 to 400 nM purified protein (L. crispatus PulA vs M. mulieris PulA, P = 0.0084; L. crispatus PulA vs P. bivia PulA, P < 0.0001; L. crispatus PulA vs P. bivia GH13, P < 0.0001). All growth curves are representative of three experimental replicates (n = 3). Error bars represent one standard deviation above and below the mean of all data collected. A multiple comparisons (Tukey) one-way analysis of variance (ANOVA) was performed to determine statistical significance. **P ≤ 0.01, ****P ≤ 0.0001.
