We have located links that may give you full text access.
Concomitant loss of the glyoxalase system and glycolysis makes the uncultured pathogen " Candidatus Liberibacter asiaticus" an energy scavenger.
Applied and Environmental Microbiology 2017 September 23
Methylglyoxal (MG) is a cytotoxic, non-enzymatic byproduct of glycolysis that readily glycates proteins and DNA, resulting in carbonyl stress. Glyoxalase I and II (GloA and GloB) sequentially convert MG into D-lactic acid using glutathione (GSH) as a cofactor. The glyoxalase system is essential for the mitigation of MG-induced carbonyl stress, preventing subsequent cell death, and recycling GSH for maintenance of cellular redox poise. All pathogenic Liberibacters identified to date are uncultured, including " Candidatus Liberibacter asiaticus", a psyllid endosymbiont and causal agent of the severely damaging citrus disease 'huanglongbing'. In silico analysis revealed the absence of gloA in " Ca. L. asiaticus" and all other pathogenic Liberibacters. Both gloA and gloB are present in L. crescens, the only Liberibacter that has been cultured. L. crescens GloA was functional in a heterologous host. Marker interruption of gloA in L. crescens appeared to be lethal. Key glycolytic enzymes were either missing or significantly downregulated in " Ca. L. asiaticus", as compared to (cultured) L. crescens Marker interruption of sut , a sucrose transporter gene in L. crescens, decreased its ability to uptake exogenously supplied sucrose in culture. " Ca. L. asiaticus" lacks a homologous sugar transporter, but has a functional ATP/ADP translocase, enabling it to thrive in both psyllids and in the sugar rich citrus phloem by a) avoiding sucrose uptake; b) avoiding MG generation via glycolysis, and c) directly importing ATP from the host cell. MG detoxification enzymes appear to be predictive of " Candidatus " status for many uncultured pathogenic and environmental bacteria. IMPORTANCE Discovered more than 100 years ago, the glyoxalase system is thought to be present across all domains of life and fundamental to cellular growth and viability. The glyoxalase system protects against carbonyl stress caused by methylglyoxal (MG), a highly reactive, mutagenic and cytotoxic compound that is non-enzymatically formed as a byproduct of glycolysis. The uncultured alphaproteobacterium " Ca. L. asiaticus" is a well-adapted endosymbiont of the Asian citrus psyllid, which transmits the severely damaging citrus disease 'huanglongbing' " Ca L. asiaticus" lacks a functional glyoxalase pathway. We report here that, the bacterium is able to thrive in both psyllids and in the sugar rich citrus phloem by a) avoiding sucrose uptake; b) avoiding (significant) MG generation via glycolysis, and c) directly importing ATP from the host cell. We hypothesize that failure to culture " Ca. L. asiaticus" is at least partly due to its dependence on host cells for both ATP and MG detoxification.
Full text links
Related Resources
Trending Papers
Heart failure with preserved ejection fraction: diagnosis, risk assessment, and treatment.Clinical Research in Cardiology : Official Journal of the German Cardiac Society 2024 April 12
Proximal versus distal diuretics in congestive heart failure.Nephrology, Dialysis, Transplantation 2024 Februrary 30
Efficacy and safety of pharmacotherapy in chronic insomnia: A review of clinical guidelines and case reports.Mental Health Clinician 2023 October
World Health Organization and International Consensus Classification of eosinophilic disorders: 2024 update on diagnosis, risk stratification, and management.American Journal of Hematology 2024 March 30
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app
All material on this website is protected by copyright, Copyright © 1994-2024 by WebMD LLC.
This website also contains material copyrighted by 3rd parties.
By using this service, you agree to our terms of use and privacy policy.
Your Privacy Choices
You can now claim free CME credits for this literature searchClaim now
Get seemless 1-tap access through your institution/university
For the best experience, use the Read mobile app