BET3 is a component of TRAPP, a complex involved in the tethering of transport vesicles to the cis-Golgi membrane. The crystal structure of human BET3 has been determined to 1.55-Å resolution. BET3 adopts an a/b-plait fold and forms dimers in the crystal and in solution, which predetermines the architecture of TRAPP where subunits are present in equimolar stoichiometry. A hydrophobic pocket within BET3 buries a palmitate bound through a thioester linkage to cysteine 68. BET3 and yeast Bet3p are palmitoylated in recombinant yeast cells, the mutant proteins BET3 C68S and Bet3p C80S remain unmodified. Both BET3 and BET3 C68S are found in membrane and cytosolic fractions of these cells; in membrane extractions, they behave like tightly membrane-associated proteins. In a deletion strain, both Bet3p and Bet3p C80S rescue cell viability. Thus, palmitoylation is neither required for viability nor sufficient for membrane association of BET3, which may depend on protein-protein contacts within TRAPP or additional, yet unidentified modifications of BET3. A conformational change may facilitate palmitoyl extrusion from BET3 and allow the fatty acid chain to engage in intermolecular hydrophobic interactions.

Selective interaction of mutans streptococci with benign bacteria could present an opportunity for their removal from the mouth without disruption of other oral flora. This study was conducted to find probiotic lactobacilli that could specifically co-aggregate in vitro with mutans streptococci, but not with other plaque commensals. A search of 624 lactobacilli among a large culture library revealed 6 strains, all classifiable as L. paracasei or L. rhamnosus, which met this criterion. Such novel, specific co-aggregation, however, was not a general characteristic of these species or the genus Lactobacillus. The co-aggregation by these specific lactobacilli was characterized as heat treatment (autoclaving)- and protease-resistant, lectin-independent, not inactivated by sugar substitutes, operational over a wide pH range, unaffected by whole saliva, but calcium-dependent. It is thus seen to present a potential strategy for in vivo alteration of plaque biofilm and caries.

Reducing the amount of Helicobacter pylori in the stomach by selective bacterial–bacterial cell interaction was sought as an effective and novel method for combating the stomach pathogen. Lactobacillus reuteri DSM17648 was identified as a highly specific binding antagonist to H. pylori among more than 700 wild-type strains of Lactobacillus species. Applying a stringent screening procedure, the strain DSM17648 was identified as selective binder to H. pylori cells under in vivo gastric conditions. The strain DSM17648 co-aggregates the pathogen in vivo and in vitro. The specific co-aggregation occurs between Lact. reuteri DSM17648 and different H. pylori strains and serotypes, as well as H. heilmannii, but not with Campylobacter jejuni or other commensal oral and intestinal bacteria. Lact. reuteri DSM17648 was shown in a proof-of-concept single-blinded, randomized, placebo-controlled pilot study to significantly reduce the load of H. pylori in healthy yet infected adults. Reducing the amount of H. pylori in the stomach by selective bacterial–bacterial cell interaction might be an effective and novel method for combating the stomach pathogen. Lact. reuteri DSM17648 might prove useful as an adhesion blocker in antibiotic-free H. pylori therapies.

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