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Record W4416719097 · doi:10.1128/mbio.02680-25

Compartmentalized cell envelope biosynthesis in <i>Mycobacterium tuberculosis</i>

2025· article· en· W4416719097 on OpenAlexaff
Júlia Puffal, Ian L. Sparks, James R. Brenner, Xuni Li, John Leszyk, Jennifer M. Hayashi, Scott A. Shaffer, Yasu S. Morita

Bibliographic record

VenuemBio · 2025
Typearticle
Languageen
FieldMedicine
TopicTuberculosis Research and Epidemiology
Canadian institutionsIONICS Mass Spectrometry (Canada)
FundersNational Institute of Allergy and Infectious DiseasesCoordenação de Aperfeiçoamento de Pessoal de Nível Superior
KeywordsCompartmentalization (fire protection)Membrane proteinGlycolipidMembraneEnzymeCell membraneProtein domainMembrane lipidsBiosynthesisCell fractionation

Abstract

fetched live from OpenAlex

ABSTRACT The inner membrane domain (IMD) is a metabolically active and laterally discrete membrane domain initially discovered in Mycobacterium smegmatis . The IMD correlates both temporally and spatially with the polar cell envelope elongation in M. smegmatis . Whether or not a similar membrane domain exists in pathogenic species remains unknown. Here, we show that the IMD is a conserved membrane structure found in Mycobacterium tuberculosis . We used two independent approaches, density gradient fractionation of membrane domains and visualization of IMD-associated proteins through fluorescence microscopy, to determine the characteristics of the plasma membrane compartmentalization in M. tuberculosis . Proteomic analysis revealed that the IMD is enriched in metabolic enzymes that are involved in the synthesis of conserved cell envelope components such as arabinogalactan and phosphatidylinositol mannosides. Using a fluorescent protein fusion of IMD-associated proteins, we demonstrated that this domain is concentrated in the subpolar region of the rod-shaped cells, where active cell envelope biosynthesis is taking place. Proteomic analysis further revealed the enrichment of enzymes involved in synthesis of phthiocerol dimycocerosates and phenolic glycolipids in the IMD. We validated the IMD association of two enzymes, α1,3-fucosyltransferase and fucosyl 4- O -methyltransferase, which are involved in the final maturation steps of phenolic glycolipid biosynthesis. Taken together, these data indicate that functional compartmentalization of membrane is an evolutionarily conserved feature found in both M. tuberculosis and M. smegmatis , and M. tuberculosis utilizes this membrane location to enrich biosynthetic enzymes for its surface-exposed lipid virulence factors. IMPORTANCE M. tuberculosis remains an important public health threat, with more than one million deaths every year. The pathogen’s ability to survive in the human host for decades highlights the importance of understanding how this bacterium regulates and coordinates its metabolism, cell envelope elongation, and growth. The IMD is a membrane structure that associates with the subpolar growth zone of actively growing mycobacterial cell, but its existence is only known in a non-pathogenic model, M. smegmatis . Here, we demonstrated the presence of the IMD in M. tuberculosis , making the IMD an evolutionarily conserved plasma membrane compartment in mycobacteria. Furthermore, our study revealed that the IMD may function as the factory for synthesizing phenolic glycolipids, virulence factors produced by slow-growing pathogenic species.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Observational · Consensus signal: Observational
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.150
Threshold uncertainty score0.549

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0010.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.018
GPT teacher head0.309
Teacher spread0.292 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designObservational
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations1
Published2025
Admission routes1
Has abstractyes

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