ArticleMolecular microbiology2016
Lytic transglycosylases LtgA and LtgD perform distinct roles in remodeling, recycling and releasing peptidoglycan in Neisseria gonorrhoeae.
Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- Antimicrobial activity of compounds identified by artificial intelligence discovery engine targeting enzymes involved in Neisseria gonorrhoeae peptidoglycan metabolism.Biological research · 2024Article
- Lytic transglycosylase Slt of Pseudomonas aeruginosa as a periplasmic hub protein.Protein science : a publication of the Protein Society · 2024Article
- Peptidoglycan fragment release and NOD activation by commensalInfection and immunity · 2024Article
- Mutation ofJournal of bacteriology · 2023Article
- Transcriptional activation ofmBio · 2023Article
- Mutation ofbioRxiv : the preprint server for biology · 2023Article
- An MltA-Like Lytic Transglycosylase Secreted by Bdellovibrio bacteriovorus Cleaves the Prey Septum during Predatory Invasion.Journal of bacteriology · 2023Article
- The AmiC/NlpD Pathway Dominates Peptidoglycan Breakdown in Neisseria meningitidis and Affects Cell Separation, NOD1 Agonist Production, and Infection.Infection and immunity · 2022Article
- Turnover Chemistry and Structural Characterization of the Cj0843c Lytic Transglycosylase ofBiochemistry · 2021Article
- Anti-Virulence Therapeutic Approaches forAntibiotics (Basel, Switzerland) · 2021Review
- Article
- Effect of Lipidation on the Localization and Activity of a Lysozyme Inhibitor inJournal of bacteriology · 2020Article
- Article
- Genetic Evidence for Distinct Functions of Peptidoglycan Endopeptidases inFrontiers in microbiology · 2020Article
- The lytic transglycosylase, LtgG, controls cell morphology and virulence in Burkholderia pseudomallei.Scientific reports · 2019Article
- Article
- AFrontiers in microbiology · 2019Article
- Peptidoglycan Muropeptides: Release, Perception, and Functions as Signaling Molecules.Frontiers in microbiology · 2019Review
- The Pathogenic Neisseria Use a Streamlined Set of Peptidoglycan Degradation Proteins for Peptidoglycan Remodeling, Recycling, and Toxic Fragment Release.Frontiers in microbiology · 2019Review
- Antibiotic Targets in Gonococcal Cell Wall Metabolism.Antibiotics (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Neisseria gonorrhoeae releases peptidoglycan (PG) fragments during infection that provoke a large inflammatory response and, in pelvic inflammatory disease, this response leads to the death and sloughing of ciliated cells of the Fallopian tube. We characterized the biochemical functions and localization of two enzymes responsible for the release of proinflammatory PG fragments. The putative lytic transglycosylases LtgA and LtgD were shown to create the 1,6-anhydromuramyl moieties, and both enzymes were able to digest a small, synthetic tetrasaccharide dipeptide PG fragment into the cognate 1,6-anhydromuramyl-containing reaction products. Degradation of tetrasaccharide PG fragments by LtgA is the first demonstration of a family 1 lytic transglycosylase exhibiting this activity. Pulse-chase experiments in gonococci demonstrated that LtgA produces a larger amount of PG fragments than LtgD, and a vast majority of these fragments are recycled. In contrast, LtgD was necessary for wild-type levels of PG precursor incorporation and produced fragments predominantly released from the cell. Additionally, super-resolution microscopy established that LtgA localizes to the septum, whereas LtgD is localized around the cell. This investigation suggests a model where LtgD produces PG monomers in such a way that these fragments are released, whereas LtgA creates fragments that are mostly taken into the cytoplasm for recycling.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.