Ethanol-Induced Alcohol Dehydrogenase E (AdhE) Potentiates Pneumolysin in Streptococcus pneumoniae

Luong, Truc Thanh; Kim, Eun Hye; Bak, Jong Phil; Nguyen, Cattien V.; Choi, Sangdun; Briles, David E.; Pyo, Suhkneung; Rhee, Dong Kwon

doi:10.1128/iai.02434-14

Cited by 39 publications

(35 citation statements)

References 59 publications

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“…pneumoniae , as well as host cell myeloperoxidase activity, proinflammatory cytokine secretion, and inflammation, were significantly attenuated in D39 Δ adhE compared to D39 wild-type [11]. Thus, AdhE appears to be a pneumococcal virulence factor [11]. These differentially expressed genes may provide us valuable targets for drugs and may be potential vaccine candidates.…”

Section: Discussionmentioning

confidence: 95%

Impact of aspirin on the transcriptome of Streptococcus pneumoniae D39

Afzal

Shafeeq

2017

Genomics Data

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Aspirin or acetylsalicylic acid (ASA) is a medicine used to treat pain, fever, and inflammation. Here, we for the very first time reported the genome-wide transcriptional profiling of aspirin-regulated genes in Streptococcus pneumoniae in the presence of 5 mM aspirin in chemically-defined medium (CDM) using microarray analysis. Our results showed that expression of several genes was differentially expressed in the presence of aspirin. These genes were further grouped into COG (Clusters of Orthologous Groups) functional categories based on the putative functions of the corresponding proteins. Most of affected genes belong to COG category E (Amino acid transport and metabolism), G (Carbohydrate transport and metabolism), J (Translation, ribosomal structure and biogenesis), and I (Lipid transport and metabolism). Transcriptional profiling data of aspirin-regulated genes was deposited to Gene Expression Omnibus (GEO) database under accession number GSE94514.

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Section: Discussionmentioning

confidence: 95%

Impact of aspirin on the transcriptome of Streptococcus pneumoniae D39

Afzal

Shafeeq

2017

Genomics Data

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“…In Listeria monocytogenes, the Listeria adhesion protein LAP (homologous to AdhE) promotes bacterial adhesion by interacting with a receptor of intestine cells 7,8 . It has also been reported in Streptococcus pneumoniae that AdhE also promotes bacterial adherence 9 . In E. coli, this enzyme would play a role during colonization by regulating the expression of key virulence genes 10 .…”

mentioning

confidence: 91%

Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation

et al. 2020

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Acetaldehyde-alcohol dehydrogenase (AdhE) enzymes are a key metabolic enzyme in bacterial physiology and pathogenicity. They convert acetyl-CoA to ethanol via an acetaldehyde intermediate during ethanol fermentation in an anaerobic environment. This two-step reaction is associated to NAD + regeneration, essential for glycolysis. The bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae. It is found as an oligomeric form called spirosomes, for which the function remains elusive. Here, we use cryo-electron microscopy to obtain structures of Escherichia coli spirosomes in different conformational states. We show that spirosomes contain active AdhE monomers, and that AdhE filamentation is essential for its activity in vitro and function in vivo. The detailed analysis of these structures provides insight showing that AdhE filamentation is essential for substrate channeling within the filament and for the regulation of enzyme activity.

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“…In Listeria monocytogenes, the Listeria adhesion protein LAP (homologous to AdhE) promotes bacterial adhesion by interacting with a receptor of intestine cells 7,8 . It has also been reported in Streptococcus pneumoniae that AdhE also promotes bacterial adherence 9 . In Escherichia coli, this enzyme would play a role during colonization by regulating the expression of key virulence genes 10 .…”

mentioning

confidence: 91%

Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation

Pony

Rapisarda

Terradot

et al. 2019

Preprint

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Acetaldehyde -alcohol dehydrogenase (AdhE) enzymes are a key metabolic enzyme in bacterial physiology and pathogenicity. They convert acetyl-CoA to ethanol via an acetaldehyde intermediate during ethanol fermentation in anaerobic environment. This twostep reaction is associated to NAD + regeneration, essential for glycolysis. The bifunctional AdhE enzyme is conserved in all bacterial kingdoms but also in more phylogenetically distant microorganisms such as green microalgae. In synthetic biology and biotechnology, because of its central role in bacterial alcoholic fermentation, AdhE raised a lot of attention as a key enzyme to produce ethanol from bacterial cultures.AdhE is commonly found as an oligomeric form called spirosomes. While these helical macromolecular assemblies are conserved, their function remains elusive. We used cryoelectron microscopy to obtain structures of Escherichia coli spirosomes in different conformational states. We confirm that spirosomes contain active AdhE monomers and show that AdhE filamentation is essential for its activity in vitro and function in vivo. The detailed analysis of these structures provides insight showing that AdhE filamentation is essential for substrate channeling within the filament and for the regulation of enzyme activity. These new data will help to design molecules or mutations that control AdhE activity to fight bacterial pathogens or to optimize ethanol production in biotechnology.

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Ethanol-Induced Alcohol Dehydrogenase E (AdhE) Potentiates Pneumolysin in Streptococcus pneumoniae

Cited by 39 publications

References 59 publications

Impact of aspirin on the transcriptome of Streptococcus pneumoniae D39

Impact of aspirin on the transcriptome of Streptococcus pneumoniae D39

Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation

Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation

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