ArticleThe Journal of membrane biology2019
Function and Regulation of Acid Resistance Antiporters.
Article in The Journal of membrane biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Genes and physiological strategies in bacterial antibiotic resistance.Frontiers in microbiology · 2026Review
- Examination of conformational dynamics of AdiC transporter with fluorescence-polarization microscopy.The Journal of general physiology · 2025Article
- Molecular mechanism of proteolytic cleavage-dependent activation of CadC-mediated response to acid in E. coli.Communications biology · 2024Article
- Two putative glutamate decarboxylases of Streptococcus pneumoniae as possible antigens for the production of anti-GAD65 antibodies leading to type 1 diabetes mellitus.International microbiology : the official journal of the Spanish Society for Microbiology · 2023Article
- Article
- Alkaline Stress Causes Changes in Polyamine Biosynthesis inInternational journal of molecular sciences · 2022Article
- Integrated AlphaFold2 and DEER investigation of the conformational dynamics of a pH-dependent APC antiporter.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Acid resistance system CadBA is implicated in acid tolerance and biofilm formation and is identified as a new virulence factor of Edwardsiella tarda.Veterinary research · 2021Article
- Green chemical and biological synthesis of cadaverine: recent development and challenges.RSC advances · 2021Review
- Comparative Review of the Responses ofGenes · 2020Review
- Special Issue: Membrane and Receptor Dynamics.The Journal of membrane biology · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial pathogens are a major cause of foodborne diseases and food poisoning. To cope with the acid conditions encountered in different environments such as in fermented food or in the gastric compartment, neutralophilic bacteria have developed several adaptive mechanisms. One of those mechanisms, the amino acid dependent system, consumes intracellular protons in biochemical reactions. It involves an antiporter that facilitates the exchange of external substrate amino acid for internal product and a cytoplasmic decarboxylase that catalyzes a proton-consuming decarboxylation of the substrate. So far, four acid resistance antiporters have been discovered, namely the glutamate-γ-aminobutyric acid antiporter GadC, the arginine-agmatine antiporter AdiC, the lysine-cadaverine antiporter CadB, and the ornithine-putrescine antiporter PotE. The 3D structures of AdiC and GadC, reveal an inverted-repeat fold of two times 5 transmembrane helices, typical of the amino acid-polyamine-organocation (APC) superfamily of transporters. This review summarizes our current knowledge on the transport mechanism, the pH regulation and the selectivity of these four acid resistance antiporters. It also highlights that AdiC is a paradigm for eukaryotic amino acid transporters of the APC superfamily as structural models of several of these transporters built using AdiC structures were exploited to unveil their mechanisms of amino acid recognition and translocation.
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