, 1998; Aoki et al., 2000). However, in the current study, false-positive amplifications with the primer sets SA1B10-1-F and SA1B10-1-R3, LG-1 and pLG-2, and cG-F and Lc-R5 were observed for genomic DNA of L. lactis subsp. lactis, Enterococcus casseliflavus, Enterococcus solitarius, Streptococcus pyogenes, and Streptococcus anginosus. Therefore, the new DNA signatures CAUF58 and CAUF64 show higher specificity for PCR-based detection

of L. garvieae compared with those of the current primers. Lactococcus garvieae, the leading agent of lactococcosis, affects many fish species worldwide. In addition, this bacterium is considered a potential zoonotic microorganism because it is known to cause human infections, and L. garvieae outbreaks in humans have recently been reported in Italy (Reimundo et al., 2011). Our data indicate that SSH can be exploited for the development of more stable and robust chromosome-specific selleck chemical DNA signatures that will supplement the previously reported diagnostic markers including 16S rRNA for accurate identification of L. garvieae. This paper was sponsored by Wonkwang University in 2010. W.K. and H.K.P. contributed equally to this work. “
“A lipopolysaccharide mutant of Leptospira interrogans (LaiMut) was obtained by growth in the presence of an agglutinating monoclonal

antibody (mAb) against lipopolysaccharide. ABT-263 molecular weight Agglutination reactions with anti-lipopolysaccharide mAbs and polyclonal antibodies showed that LaiMut had lost some serogroup Icterohaemorrhagiae agglutinating epitopes. However, LaiMut displayed an increased reactivity to antisera against related serogroups,

suggesting that the disruption Idelalisib mw of some lipopolysaccharide epitopes resulted in greater exposure to cross-reactive epitopes, not accessible to antibodies in the wild type (LaiWT). Comparison of the nucleotide sequences of the lipopolysaccharide loci of LaiMut and Lai wild type (LaiWT) strains showed an inframe stop mutation in the gene encoding undecaprenyl-galactosyltransferase, a protein that provides a fundamental and nonredundant function essential for lipopolysaccharide biosynthesis. Despite this, the biosynthesis of lipopolysaccharide agglutinating antigens was not abolished by the mutation. Based on the phenotype of LaiMut and analysis of the domain structure of the undecaprenyl-galactosyltransferase in relation to the mutation, we propose that the mutation results in the expression of two functional proteins in place of the undecaprenyl-galactosyltransferase. We hypothesize that the loss of coordination of the coupled function afforded by the intact dual function protein present in the parent strain results in an inefficient production of lipopolysaccharide in LaiMut. The genus Leptospira is classified genetically into more than 17 species, which can be more generally classified into three groups based on the genetic relationships between the species; these groups comprise the pathogenic, saprophytic, and intermediate species (Morey et al., 2006).