Corrigendum: Assessing the function of STAS domain protein SypA in Vibrio fischeri using a comparative analysis [Front. Microbiol., 6, (2015), (760)] doi: 10.3389/fmicb.2015.00760

Abstract

Our work investigated the structure/function relationship of V. fischeri SypA using comparative analyses and mutagenesis approaches. We found that orthologs of SypA (RbdA, SypAVP) encoded by other Vibrio species (V. vulnificus, V. parahaemolyticus) were able to complement the biofilm defect of a V. fischeri sypA mutant. These results indicated that the function of these proteins is conserved. We also identified and disrupted a set of conserved residues in SypA; a number of these mutations diminished or abolished SypA function in promoting biofilm formation. Our conclusions with respect to these studies remain intact. However, we also reported results with respect to control of SypA by SypE. In subsequent experiments, we discovered that two of our strains were incorrect. This affects some of our results and conclusions with respect to the data shown in Figures 5, 7. In Figure 5, we reported that strains expressing rbdA could largely overcome the inhibitory effect of SypE; however, we subsequently determined that this strain was incorrect as it did not express sypE. In the correct strain background, RbdA remains susceptible to control by SypE. Similarly, in Figure 7, we reported that a strain expressing a mutant form of SypA, SypA-R27A, was resistant to control by SypE, but that strain also proved to be incorrect as it did not express sypE. In the correct strain background SypA-R27A remains sensitive to SypE.