Abstract
The attP region of the Clostridium difficile phage CD27 was identified, located immediately downstream of the putative recombinase. The phage could integrate into two specific sites (attB) in the C. difficile genome, one of which was in an open reading frame encoding a putative ATPase of an ABC transporter and the other in an open reading frame encoding a putative ATPase of the flagella protein export apparatus. The prophage was capable of excision and formation of a circular molecule and phages were spontaneously released at a low frequency during growth. Infection and lysogeny of a C. difficile strain previously shown to be sensitive to CD27 were demonstrated, leading to a reduction in toxin production. Finally, a putative repressor was identified which is likely to be involved in maintaining lysogeny in these strains.
Highlights
Clostridium difficile infection is the most common cause of antibiotic-associated colitis and represents a considerable burden on healthcare services worldwide (Lo Vecchio & Zacur, 2012)
In some Clostridium spp. toxins are encoded by phage sequences (Eklund et al, 1971) and some homology has been reported between proteins involved in C. difficile toxin production and proteins encoded by C. difficile phages (Goh et al, 2005; Tan et al, 2001)
We determined the sequence of the attP site used by phage wCD27 to integrate into the C. difficile genome
Summary
Clostridium difficile infection is the most common cause of antibiotic-associated colitis and represents a considerable burden on healthcare services worldwide (Lo Vecchio & Zacur, 2012). The integration of phage into host DNA during lysogeny can be beneficial to both the phage and the host bacterium. Genetic elements encoding virulence factors such as toxin genes and antibiotic resistance are often embedded in phage DNA (Bishai & Murphy, 1988; Chen et al, 2011) and acquisition can impart significant competitive advantages, enabling the host bacterium to survive in changing environments. In some Clostridium spp. toxins are encoded by phage sequences (Eklund et al, 1971) and some homology has been reported between proteins involved in C. difficile toxin production and proteins encoded by C. difficile phages (Goh et al, 2005; Tan et al, 2001). We show that in the prophage state a candidate repressor is expressed which may be involved in the maintenance of lysogeny and modulation of toxin production
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