ArticleJournal of bacteriology2007
Antigen 84, an effector of pleiomorphism in Mycobacterium smegmatis.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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.
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.
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Who cites it
55 citing papers in PubMed, 122 citations in OpenAlex.
- Functional dissection ofmBio · 2026Article
- Unravelling the protective effects: PknJ modulates MmaA4 expression and rifampicin susceptibility in Mycobacterium bovis BCG.Archives of microbiology · 2026Article
- Essential and dispensable domains of DivIVA for walled growth in filamentous Actinomycetota.Open biology · 2025Article
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- A dispensable SepIVA orthologue in Streptomyces venezuelae is associated with polar growth and not cell division.BMC microbiology · 2024Article
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- Cell Wall Damage Reveals Spatial Flexibility in Peptidoglycan Synthesis and a Nonredundant Role for RodA in Mycobacteria.Journal of bacteriology · 2022Article
- Polar protein Wag31 both activates and inhibits cell wall metabolism at the poles and septum.Frontiers in microbiology · 2022Article
- Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA.International journal of molecular sciences · 2021Article
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- Structural basis of self-assembly in the lipid-binding domain of mycobacterial polar growth factor Wag31.IUCrJ · 2020Article
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- DivIVA Controls Progeny Morphology and Diverse ParA Proteins Regulate Cell Division or Gliding Motility inFrontiers in microbiology · 2020Article
- EF1025, a Hypothetical Protein FromFrontiers in microbiology · 2020Article
- ¡vIVA la DivIVA!Journal of bacteriology · 2019Review
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Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While in most rod-shaped bacteria, morphology is based on MreB-like proteins that form an actin-like cytoskeletal scaffold for cell wall biosynthesis, the factors that determine the more flexible rod-like shape in actinobacteria such as Mycobacterium species are unknown. Here we show that a Mycobacterium smegmatis protein homologous to eubacterial DivIVA-like proteins, including M. tuberculosis antigen 84 (Ag84), localized symmetrically to centers of peptidoglycan biosynthesis at the poles and septa. Controlled gene disruption experiments indicated that the gene encoding Ag84, wag31, was essential; when overexpressed, cells became longer and wider, with Ag84 asymmetrically distributed at one pole. Many became grossly enlarged, bowling-pin-shaped cells having up to 80-fold-increased volume. In these cells, Ag84 accumulated predominantly at a bulbous pole that was apparently generated by uncontrolled cell wall expansion. In some cells, Ag84 was associated with exceptional sites of cell wall expansion (buds) that evolved into branches. M. bovis BCG Ag84 was able to form oligomers in vitro, perhaps reflecting its superstructure in vivo. These data suggested a role for Ag84 in cell division and modulating cell shape in pleiomorphic actinobacteria.
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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.