HIV type 1 abrogates TAP-mediated transport of antigenic peptides presented by MHC class I. Transporter associated with antigen presentation.

Downregulation of MHC class I expression following human immunodeficiency virus 1 (HIV-1) infection is thought to play an important role in viral escape from immune recognition by cytotoxic T-lymphocytes (CTLs). Since exogenous addition of HIV-1-derived peptides restores susceptibility of HIV-1-infected cells to CTL-mediated lysis, we tested whether endogenous peptide loading is impaired in these cells. Our results show that in HIV-1-infected cells the ability of the transporter associated with antigen presentation (TAP) to translocate antigenic peptides from the cytosol to the lumen of the ER for presentation on MHC class I molecules is abolished. These data suggest that interference with the supply of antigenic peptides to the MHC class I pathway provides an additional mechanism by which HIV-1 evades the CTL-mediated immune response.

Susceptibility in vitro of Helicobacter pylori to cetylpyridinium chloride.

The antimicrobial agent cetylpyridinium chloride (CPC) which is used in therapy of oro-pharyngeal infections and for antiseptic treatment of the oral cavity is active against different bacterial species. Determination of the minimal inhibitory concentration (MIC) using the agar dilution technique revealed that the gastric pathogen Helicobacter pylori in vitro is highly susceptible to CPC as indicated by an MIC of 10 microM (3.4 microg ml(-1)) which was significantly lower than the MIC of CPC against other bacterial species, which were analyzed in comparison to H. pylori. Bacteria of the genus Campylobacter, various Streptococcus spp., Staphylococcus aureus and Escherichia coli showed higher MICs ranging from 100 microM to 2 mM. In summary, this finding renders CPC-containing drugs candidates possibly useful for eradication or for the prevention of transmission of the gastric pathogen.

Cloning and characterization of the fur gene from Helicobacter pylori.

The fur homologue of Helicobacter pylori was isolated by screening a plasmid-based, genomic DNA library using the Fur titration assay (FURTA). The analysis of the DNA sequence revealed significant homology with Fur proteins from various other bacterial species. The highest degree of homology was observed for the Fur protein from Campylobacter jejuni. The H. pylori fur gene on a plasmid could partially complement the fur mutation in Escherichia coli strain H1681. The repressor activity depended on addition of iron to the medium indicating that iron acts as a co-repressor for the H. pylori protein similar to Fur from other bacteria. Comparison of Fur from H. pylori strain NCTC11638 with the recently published genomic DNA sequence of another strain (26695) confirmed the identity of the fur homologue and revealed that the fur locus is highly conserved in both strains.