Interestingly, our own predictions of enzyme localization Opaganib cell line using signalp 3.0 (Bendtsen et al., 2004) and lipop v. 1.0 (Juncker et al., 2003), as well as the locatep database (Zhou et al., 2008) indicate that EF2863 is a secreted protein, whereas the leader peptide of EF0114 seems to have no signal peptidase I cleavage site, meaning that this protein may be N-terminally anchored to the cell membrane. Different localization of the two endoglycosidases may reflect different physiological roles. Proteins with high-mannose N-linked glycans are frequently found in human

glycoproteins (Fujiwara et al., 1988, Furukawa et al., 1989). Even though the release of nutrients from these glycoproteins

seems to be a physiologically important role of enzymes such as EfEndo18A, one may speculate about additional physiological roles such as modulation of the host immune system. Interestingly, it has been shown that EfEndo18A from E. faecalis V583 is up-regulated in blood and urine (Vebo et al., 2009, 2010), where E. faecalis frequently causes infection. The prevalence of endoglycosidases that exploit, alter or inactivate host glycoproteins may give pathogenic bacteria PDGFR inhibitor an advantage during infection. This work was supported by grant 183637/S10 from the Research Council of Norway. We thank Britt Dahl for technical assistance during the cloning experiments. “
“The Pectobacterium atrosepticum strain SCRI1043 genome contains two complete prophage

sequences. One, ECA41, is Mu-like and is able to integrate into, and excise from, Dimethyl sulfoxide various genomic locations. The other, ECA29, is a P2 family prophage, and is also able to excise from the genome. Excision of both prophages is rare and we were unable to induce lysis of cultures. Deletion of the entire prophages, both separately and in combination, did not affect the growth rate or the secretion of plant cell wall-degrading enzymes, but swimming motility was decreased. The virulence of prophage deletion strains in the potato host was decreased. Lysogenization of a bacterial host by temperate bacteriophages can alter bacterial physiology. Most dramatically, this manifests itself as lysogenic conversion, where a previously avirulent strain becomes a serious pathogen. Enterohaemorrhagic Escherichia coli and Vibrio cholerae are prime examples, where Stx phage and CTXΦ provide the Shiga toxin and cholera toxin genes, respectively (O’Brien et al., 1984; Waldor & Mekalanos, 1996). Phage-encoded functions are diverse. Bor and Lom, carried by phage λ, are involved in resistance to the host immune system and cell adhesion, respectively (Barondess & Beckwith, 1990; Pacheco et al., 1997); SopE is an effector protein secreted by the Type III secretion system in Salmonella that activates human Rho GTPases (Hardt et al.