Evidence map›Paper›PMID 26114871›Full record

ArticlePLoS pathogens2015

Phosphorylation of the Peptidoglycan Synthase PonA1 Governs the Rate of Polar Elongation in Mycobacteria.

Karen J Kieser, Cara C Boutte, Jemila C Kester, Christina E Baer, Amy K Barczak, Xavier Meniche, Michael C Chao, E Hesper Rego, Christopher M Sassetti, Sarah M Fortune and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
6.1field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

70 citing papers in PubMed, 127 citations in OpenAlex.

  1. Trial
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  3. Ribosomal protection as a linezolid resistance mechanism inAntimicrobial agents and chemotherapy · 2026
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  4. 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 · 2026
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  5. Review
  6. [Fe(phen)ACS omega · 2025
    Article
  7. Ribosomal protection as a linezolid resistance mechanism inbioRxiv : the preprint server for biology · 2025
    Article
  8. Article
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  11. Article
  12. Article
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  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

10 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 1 country.

Karen J KieserDepartment of Immunology and Infectious Disease, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, United States of America.
Cara C BoutteDepartment of Immunology and Infectious Disease, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, United States of America.
Jemila C KesterDepartment of Immunology and Infectious Disease, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, United States of America.
Christina E BaerDepartment of Microbiology and Physiological Systems, Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, United States of America.
Amy K BarczakDivision of Infectious Disease, Massachusetts General Hospital, Boston, Massachusetts, United States of America.
Xavier MenicheDepartment of Microbiology and Physiological Systems, Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, United States of America.
Michael C ChaoDepartment of Immunology and Infectious Disease, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, United States of America.
E Hesper RegoDepartment of Immunology and Infectious Disease, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, United States of America.
Christopher M SassettiDepartment of Microbiology and Physiological Systems, Howard Hughes Medical Institute, University of Massachusetts Medical School, Worcester, Massachusetts, United States of America.
Sarah M FortuneDepartment of Immunology and Infectious Disease, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, United States of America.
Eric J RubinDepartment of Immunology and Infectious Disease, Harvard T. H. Chan School of Public Health, Boston, Massachusetts, United States of America; Department of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, United States of America.
Harvard University · USHoward Hughes Medical Institute · USMassachusetts General Hospital · USUniversity of Massachusetts Chan Medical School · US

Funding

Vulnerabilities in Mycobacterial Cell-Wall BiogenesisP01AI095208 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI ZHANG, JUNJIE · 2012 to 2022
$19.8M
INFECTIOUS DISEASE AND BASIC MICROBIOLOGICAL MECHANISMST32AI007061 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI Marcia B Goldberg · 1985 to 2026
$12.1M
Structures of Mtb proteins conferring susceptibility to known Mtb inhibitorsU01GM094568 · NIGMS · TEXAS A&M UNIVERSITY · PI TERWILLIGER, THOMAS C. · 2010 to 2014
$6.0M
Tuberculosis Pathogenesis and Drug ResponseR01AI064282 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SASSETTI, CHRISTOPHER M · 2007 to 2017
$3.9M
Howard Hughes Medical InstituteNIAID NIH HHS AI064282NIAID NIH HHS AI095208NIAID NIH HHS P01 AI095208NIAID NIH HHS R01 AI064282NIAID NIH HHS R01 AI09719101A3NIAID NIH HHS T32 AI007061NIGMS NIH HHS U01 GM094568NIGMS NIH HHS U01-GM094568
6 · The paper itself

Abstract

Cell growth and division are required for the progression of bacterial infections. Most rod-shaped bacteria grow by inserting new cell wall along their mid-section. However, mycobacteria, including the human pathogen Mycobacterium tuberculosis, produce new cell wall material at their poles. How mycobacteria control this different mode of growth is incompletely understood. Here we find that PonA1, a penicillin binding protein (PBP) capable of transglycosylation and transpeptidation of cell wall peptidoglycan (PG), is a major governor of polar growth in mycobacteria. PonA1 is required for growth of Mycobacterium smegmatis and is critical for M. tuberculosis during infection. In both cases, PonA1's catalytic activities are both required for normal cell length, though loss of transglycosylase activity has a more pronounced effect than transpeptidation. Mutations that alter the amount or the activity of PonA1 result in abnormal formation of cell poles and changes in cell length. Moreover, altered PonA1 activity results in dramatic differences in antibiotic susceptibility, suggesting that a balance between the two enzymatic activities of PonA1 is critical for survival. We also find that phosphorylation of a cytoplasmic region of PonA1 is required for normal activity. Mutations in a critical phosphorylated residue affect transglycosylase activity and result in abnormal rates of cell elongation. Together, our data indicate that PonA1 is a central determinant of polar growth in mycobacteria, and its governance of cell elongation is required for robust cell fitness during both host-induced and antibiotic stress.

Indexed as

Cell CycleCell DivisionCell Growth ProcessesCell WallMycobacterium smegmatisMycobacterium tuberculosisPenicillin-Binding ProteinsPeptidoglycanPhosphorylationPenicillin-Binding ProteinsPeptidoglycan

Identifiers

PMID26114871
PMCPMC4483258
OpenAlexW746093339

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.