ArticleNature microbiology2026
The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture.
Article in Nature microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Defining the order of assembly of theJournal of bacteriology · 2026Article
- The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture.Nature microbiology · 2026Article
- Acid-dependent beta-lactam resistance inmBio · 2026Article
- Peptidoglycan recycling is critical for cell division, cell wall integrity, and β-lactam resistance ineLife · 2026Article
- Enzymatic activity of PBP1B is required for growth rate-independent ppGpp-mediated resistance to PBP2 inhibitors inJournal of bacteriology · 2026Article
- Defining the order of assembly of thebioRxiv : the preprint server for biology · 2026Article
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Authors and funding
10 authors.
Funding
Abstract
The divisome apparatus synthesizes septal peptidoglycan (PG) during bacterial division. In Escherichia coli, the class A penicillin-binding protein (aPBP) called PBP1b has been implicated in division, but its role in the process has remained unclear. Here we show using in situ cryo-electron tomography, genetics and other imaging methods that PBP1b is required to produce a wedge-like density of PG at the division site and that loss of this structure weakens the division site, making it hypersusceptible to osmotic lysis. Surprisingly, the activator LpoB needed for general PBP1b function was not required for its role in division. Of the two PBP1b isoforms produced in cells, we show that the one with an extended cytoplasmic N terminus localizes to and functions at the division site, probably via recruitment by the FtsA component of the divisome. The conservation of aPBPs with extended cytoplasmic N termini suggests that other Gram-negative bacteria may use similar mechanisms for division site reinforcement.
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