ArticleFrontiers in cellular and infection microbiology2014
Characterization of serine hydroxymethyltransferase GlyA as a potential source of D-alanine in Chlamydia pneumoniae.
Article in Frontiers in cellular and infection microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 34 citations in OpenAlex.
- Characterization of the cell division-associated peptidoglycan amidase AmiA ofJournal of bacteriology · 2026Article
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- The MraY Inhibitor Muraymycin D2 and Its Derivatives Induce Enlarged Cells in Obligate IntracellularAntibiotics (Basel, Switzerland) · 2024Article
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- Gene expression and involvement of signaling pathways during host-pathogen interplay in3 Biotech · 2022Review
- Plant peptidoglycan precursor biosynthesis: Conservation between moss chloroplasts and Gram-negative bacteria.Plant physiology · 2022Article
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- Competing Substrates for the Bifunctional Diaminopimelic Acid Epimerase/Glutamate Racemase Modulate Peptidoglycan Synthesis in Chlamydia trachomatis.Infection and immunity · 2020Article
- Penicillin-binding proteins regulate multiple steps in the polarized cell division process of Chlamydia.Scientific reports · 2020Article
- Chlamydia trachomatis Oligopeptide Transporter Performs Dual Functions of Oligopeptide Transport and Peptidoglycan Recycling.Infection and immunity · 2020Article
- How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation.The FEBS journal · 2020Review
- Building peptidoglycan inside eukaryotic cells: A view from symbiotic and pathogenic bacteria.Molecular microbiology · 2020Review
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- Peptidoglycan in obligate intracellular bacteria.Molecular microbiology · 2018Review
- Simkania negevensis, an Example of the Diversity of the Antimicrobial Susceptibility Pattern among Chlamydiales.Antimicrobial agents and chemotherapy · 2017Article
- Evidence for a peptidoglycan-like structure in Orientia tsutsugamushi.Molecular microbiology · 2017Article
- AmiA is a penicillin target enzyme with dual activity in the intracellular pathogen Chlamydia pneumoniae.Nature communications · 2014Article
- The role of viable but non-infectious developmental forms in chlamydial biology.Frontiers in cellular and infection microbiology · 2014Article
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8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For intracellular Chlamydiaceae, there is no need to withstand osmotic challenges, and a functional cell wall has not been detected in these pathogens so far. Nevertheless, penicillin inhibits cell division in Chlamydiaceae resulting in enlarged aberrant bodies, a phenomenon known as chlamydial anomaly. D-alanine is a unique and essential component in the biosynthesis of bacterial cell walls. In free-living bacteria like Escherichia coli, penicillin-binding proteins such as monofunctional transpeptidases PBP2 and PBP3, the putative targets of penicillin in Chlamydiaceae, cross-link adjacent peptidoglycan strands via meso-diaminopimelic acid and D-Ala-D-Ala moieties of pentapeptide side chains. In the absence of genes coding for alanine racemase Alr and DadX homologs, the source of D-Ala and thus the presence of substrates for PBP2 and PBP3 activity in Chlamydiaceae has puzzled researchers for years. Interestingly, Chlamydiaceae genomes encode GlyA, a serine hydroxymethyltransferase that has been shown to exhibit slow racemization of D- and L-alanine as a side reaction in E. coli. We show that GlyA from Chlamydia pneumoniae can serve as a source of D-Ala. GlyA partially reversed the D-Ala auxotrophic phenotype of an E. coli racemase double mutant. Moreover, purified chlamydial GlyA had racemase activity on L-Ala in vitro and was inhibited by D-cycloserine, identifying GlyA, besides D-Ala ligase MurC/Ddl, as an additional target of this competitive inhibitor in Chlamydiaceae. Proof of D-Ala biosynthesis in Chlamydiaceae helps to clarify the structure of cell wall precursor lipid II and the role of chlamydial penicillin-binding proteins in the development of non-dividing aberrant chlamydial bodies and persistence in the presence of penicillin.
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