ArticlePLoS pathogens2010
Interaction and modulation of two antagonistic cell wall enzymes of mycobacteria.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
71 citing papers in PubMed, 130 citations in OpenAlex.
- Variation in multiple classes of simple sequence repeats can alter drug susceptibility inbioRxiv : the preprint server for biology · 2026Article
- Polar growth factor PgfA regulates polar peptidoglycan synthesis as well as mycolate synthesis inJournal of bacteriology · 2026Article
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- An activator of a two-component system controls cell separation and intrinsic drug resistance inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- The multiple roles of the NlpC_P60 peptidase family in mycobacteria - an underexplored target for antimicrobial drug discovery.FEBS letters · 2025Review
- Age-Dependent Pleomorphism inMicroorganisms · 2025Article
- Lipoarabinomannan mediates localized cell wall integrity during division in mycobacteria.Nature communications · 2024Article
- The fall of the mycobacterial cell wall: interrogating peptidoglycan synthesis for novel anti-TB agents.PeerJ · 2024Review
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- MtrA modulates Mycobacterium tuberculosis cell division in host microenvironments to mediate intrinsic resistance and drug tolerance.Cell reports · 2023Article
- Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host interactions.Cell chemical biology · 2023Review
- Plasma Membrane-Cell Wall Feedback in Bacteria.Journal of bacteriology · 2023Review
- A Structural View at Vaccine Development againstCells · 2023Review
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- Wake Up! Resuscitation of Viable but Nonculturable Bacteria: Mechanism and Potential Application.Foods (Basel, Switzerland) · 2022Review
- FtsEX-independent control of RipA-mediated cell separation inProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Bacterial MtrAB Two-Component System Regulates the Cell Wall Homeostasis Responding to Environmental Alkaline Stress.Microbiology spectrum · 2022Article
- Cell Wall Damage Reveals Spatial Flexibility in Peptidoglycan Synthesis and a Nonredundant Role for RodA in Mycobacteria.Journal of bacteriology · 2022Article
- Polar Growth in Corynebacterium glutamicum Has a Flexible Cell Wall Synthase Requirement.mBio · 2021Article
- Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Bacterial cell growth and division require coordinated cell wall hydrolysis and synthesis, allowing for the removal and expansion of cell wall material. Without proper coordination, unchecked hydrolysis can result in cell lysis. How these opposing activities are simultaneously regulated is poorly understood. In Mycobacterium tuberculosis, the resuscitation-promoting factor B (RpfB), a lytic transglycosylase, interacts and synergizes with Rpf-interacting protein A (RipA), an endopeptidase, to hydrolyze peptidoglycan. However, it remains unclear what governs this synergy and how it is coordinated with cell wall synthesis. Here we identify the bifunctional peptidoglycan-synthesizing enzyme, penicillin binding protein 1 (PBP1), as a RipA-interacting protein. PBP1, like RipA, localizes both at the poles and septa of dividing cells. Depletion of the ponA1 gene, encoding PBP1 in M. smegmatis, results in a severe growth defect and abnormally shaped cells, indicating that PBP1 is necessary for viability and cell wall stability. Finally, PBP1 inhibits the synergistic hydrolysis of peptidoglycan by the RipA-RpfB complex in vitro. These data reveal a post-translational mechanism for regulating cell wall hydrolysis and synthesis through protein-protein interactions between enzymes with antagonistic functions.
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Identifiers
What OpenQuestion holds
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.