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In many bacterial species, including the aquatic bacterium and human pathogen  Vibrio cholerae , the second messenger cyclic diguanylate (c-di-GMP) modulates processes such as biofilm formation, motility, and virulence factor production. By interacting with various effectors, c-di-GMP regulates gene expression or protein function. One type of c-di-GMP receptor is the class I riboswitch, representatives of which have been shown to bind c-di-GMP  in vitro . Herein, we examined the  in vitro  and  in vivo  function of the putative class I riboswitch in  Vibrio cholerae , Vc1, which lies upstream of the gene encoding GbpA, a colonization factor that contributes to attachment of  V .  cholerae  to environmental and host surfaces containing N-acetylglucosamine moieties. We provide evidence that Vc1 RNA interacts directly with c-di-GMP  in vitro , and that nucleotides conserved among this class of riboswitch are important for binding. Yet the mutation of these conserved residues individually in the  V .  cholerae  chromosome inconsistently affects the expression of  gbpA  and production of the GbpA protein. By isolating the regulatory function of Vc1, we show that the Vc1 element positively regulates downstream gene expression in response to c-di-GMP. Together these data suggest that the Vc1 element responds to c-di-GMP  in vivo . Positive regulation of  gbpA  expression by c-di-GMP via Vc1 may influence the ability of  V .  cholerae  to associate with chitin in the aquatic environment and the host intestinal environment.

The RNA Domain Vc1 Regulates Downstream Gene Expression in Response to Cyclic Diguanylate in Vibrio cholerae