Disease relevance of hdeB

• Acid resistance is perceived to be an important property of enterohemorrhagic Escherichia coli strains, enabling the organisms to survive passage through the acidic environment of the stomach so that they may colonize the mammalian gastrointestinal tract and cause disease [1].
• Acid resistance in enteric bacteria [2].
• Intracellular Accumulation of Trehalose Protects Lactococcus lactis from Freeze-Drying Damage and Bile Toxicity and Increases Gastric Acid Resistance [3].

High impact information on hdeB

• Acid resistance was restored in one of these mutants by a plasmid carrying the entire hdeAB operon [4].
• The hdeA and hdeB mutants both display reduced viability upon acid stress, and only the HdeA/HdeB expression plasmid can restore their viability to close to the wild-type level, suggesting that both proteins are required for optimal protection of the bacterial periplasm against acid stress [5].
• We cloned, expressed, and purified the hdeB gene product, which belongs to the hdeAB acid stress operon [5].
• Acid resistance under these defined conditions can be inhibited by the glutamate analog L-trans-pyrrolidine-2,4-dicarboxylic acid which blocks uptake of glutamate/glutamine by selective inhibition [6].
• 5. Acid resistance system 2 (AR2) is glutamate dependent and stationary phase induced, requires the presence of glutamate decarboxylase and a putative glutamate:GABA antiporter, and provides the highest level of protection [7].

Chemical compound and disease context of hdeB

• Acid resistance of E. coli and coliform populations was determined by exposure of the samples for 1 h in pH 2, 4, and 7 citric acid/sodium phosphate buffers [8].

Associations of hdeB with chemical compounds

• Acid resistance system 3 (AR3) is arginine dependent and acid induced under anaerobic conditions, requires the presence of arginine decarboxylase (AdiA), and provides only a modest level of protection [7].

References