A multilocus sequence typing method was developed for H. suis, revealing that H. suis is a genetically diverse bacterial species on the pig herd level [46]. In addition, strain typing revealed that the H. suis strain colonizing the pig veterinarian described above [3] showed a very close relationship

to porcine H. suis strains. Moodley et al. [47] described how the H. pylori phylogeny splits into 2 primary superlineages, after which the closely related H. acinonychis originated from a host jump from the San people to large felines approximately 43,000–56,000 years ago. The complete genome sequence of H. cinaedi strain PAGU611 isolated in a case of human bacteremia was reported [48]. The PAGU611 genome is comprised of a 2,078,348-bp chromosome and a 23,054-bp plasmid Romidepsin cell line (pHci1) with average G+C contents of 38.6% and 31.6%, respectively. Synteny plots identified a unique H. cinaedi genomic island (HciGI1)

containing 173 protein-coding sequences including 147 hypothetical protein genes and 12 genes to assemble a type VI secretion system (T6SS). Okoli et al. [49] reported the effects of human and porcine bile on the proteome of H. hepaticus, Opaganib manufacturer revealing that 46 proteins of H. hepaticus were differentially expressed in human bile, and 32 proteins were differentially expressed in porcine bile. These data suggest that bile is an important factor that determines

the virulence, host adaptation, localization, and colonization of specific niches within the host environment. Kaakoush et al. [50] identified 104 proteins of H. trogontum that were bioinformatically predicted to be secreted, including 11, 11, 3, and 3 proteins involved in the response to oxidative stress or redox reactions, motility, virulence, and the T6SS, respectively. An apoprotein form of the Helicobacter mustelae iron urease, encoded by ureA2B2 genes, was shown to be activated with ferrous ions in the absence of auxiliary proteins, but not with nickel ions, as goes for the “standard” gastric Helicobacter ureAB, which also needs accessory proteins click here for its proper activity [51]. Schur et al. [52] cloned and expressed HAC1267 and HAC1268, 2 sialyltransferase enzymes of the GT-42 family from H. acinonychis strain ATCC 51104, revealing that HAC1268 is the first member of this family showing α2,6-sialyltransferase activity. The construction and characterization of a nikR mutant strain of H. hepaticus was reported [53]. Disruption of this gene, encoding the nickel-responsive regulator NikR, led to increased activities of two Ni-requiring enzymes: urease and hydrogenase. In addition, the mutant strain had a two- to threefold lower growth yield than the wild-type strain, suggesting that the regulatory protein might play additional roles in this mouse liver pathogen.