The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structure of the bacterial cell division determinant GpsB and its interaction with penicillin‐binding proteins
Open accessAbstract
Summary: Each bacterium has to co‐ordinate its growth with division to ensure genetic stability of the population. Consequently, cell division and growth are tightly regulated phenomena, albeit different bacteria utilise one of several alternative regulatory mechanisms to maintain control. Here we consider GpsB, which is linked to cell growth and division in Gram‐positive bacteria. Δ gpsB mutants of the human pathogen Listeria monocytogenes show severe lysis, division and growth defects due to distortions of cell wall biosynthesis. Consistent with this premise, GpsB interacts both in vitro and in vivo with the major bi‐functional penicillin‐binding protein. We solved the crystal structure of GpsB and the interaction interfaces in both proteins are identified and validated. The inactivation of gpsB results in strongly attenuated virulence in animal experiments, comparable in degree to classical listerial virulence factor mutants. Therefore, GpsB is essential for in vitro and in vivo growth of a highly virulent food‐borne pathogen, suggesting that GpsB could be a target for the future design of novel antibacterials.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Predicted structures for gpsB/0353 from AlphaFold2 and RoseTTAFold align nearly exactly with the crystal structure of the GpsB protein from B. subtilis (RCSB PDB: 4UG3) when aligned at the N-terminal coiled-coil domain using STAMP.
“Predicted structures for gene gpsB/0353 from AlphaFold222 (and the related protein structure prediction software RoseTTAFold36) align nearly exactly with the crystal structure of the GpsB protein from B. subtilis (RCSB PDB: 4UG3(58)) when aligned only at the N-terminal coiled-coil domain using STAMP41 and visualizing in VMD42 as is shown in Figure 1A.”
From Toward the Complete Functional Characterization of a Minimal Bacterial Proteome (2022) · cites this paper as [58]
The AlphaFold2 predicted structure of gpsB/0353 aligns to experimental structure 4UG3 with p-value 2.72 × 10-6, RMSD 1.10 Å, 100% aligned.
“gpsB/0353 | 4UG358 | 2.72 × 10–6 | 1.10 (100%)”
From Toward the Complete Functional Characterization of a Minimal Bacterial Proteome (2022) · cites this paper as [58]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Crystal structure of an isoleucine-zipper trimer
Harbury, P. B., Kim, P. S., & Alber, T. (1994) · Nature · doi:10.1038/371080a0 · Cited by 472
Cytological Characterization of YpsB, a Novel Component of the Bacillus subtilis Divisome
Tavares, J. R., de Souza, R. F., Meira, G. L. S., & Gueiros-Filho, F. J. (2008) · Journal of Bacteriology · doi:10.1128/jb.00064-08 · Cited by 51 · cited 9×
“subtilis GpsB at the septal ring occurs simultaneously with DivIVA and depends on late-acting division proteins, including DivIC and PBP 2B (Tavares et al., 2008; Gamba et al., 2009), but it is not yet known how GpsB is recruited to the septum and then back to the side wall of the cell.”
BackgroundInfluential
Flagged first, then by citations
Research works printed but not linked: 54
- 10.1038/nrmicro2198 · DOI
- 10.1107/S0907444909052925 · DOI · Paper page
- 10.1128/JB.02171-12 · DOI
- 10.1074/jbc.M508646200 · DOI
- 10.1107/S0907444909042073 · DOI · Paper page
- 10.1111/j.1365-2958.2008.06210.x · DOI
- 10.1107/S0907444906022116 · DOI
- 10.1111/j.1365-2958.2012.08011.x · DOI
- 10.1073/pnas.1313978110 · DOI · Paper page
- 10.1107/S0907444910007493 · DOI · Paper page
- 10.1128/mBio.00257‐11 · DOI
- 10.1107/S0907444905036693 · DOI
- 10.1107/S0907444913000061 · DOI
- 10.1128/JB.185.20.6209-6214.2003 · DOI
- 10.1371/journal.pgen.1004275 · DOI
- 10.1128/JB.01758-08 · DOI
- 10.1111/mmi.13050 · DOI
- 10.1128/AAC.01211-07 · DOI
- 10.1111/j.1365-2958.2012.07969.x · DOI
- 10.1074/mcp.M114.041327 · DOI
- 10.1016/S0092-8674(00)81838-3 · DOI
- 10.1517/14656566.5.8.1727 · DOI
- 10.1111/j.1365-2958.2012.08107.x · DOI
- 10.1016/S0092-8674(02)00905-4 · DOI
- 10.1107/S0907444909047337 · DOI · Paper page
- 10.1073/pnas.0502390102 · DOI
- 10.1073/pnas.95.10.5752 · DOI
- 10.4161/viru.20747 · DOI
- 10.1016/j.jmb.2007.05.022 · DOI
- 10.1111/mmi.12408 · DOI
- 10.1038/nprot.2008.91 · DOI · Paper page
- 10.1093/jac/dki094 · DOI
- 10.1038/emboj.2009.129 · DOI
- 10.1128/JB.01934-07 · DOI
- 10.1002/cm.21126 · DOI
- 10.1107/S0021889807021206 · DOI · Paper page
- Marquis H.(2006)Tissue culture cell assays used to analyzeListeria monocytogenes. Current protocols in microbiology Chapter 9: Unit 9B 4. · DOI
- 10.1101/gad.12.21.3419 · DOI
- 10.1099/00221287-144-11-3069 · DOI
- 10.1128/AEM.00314-08 · DOI
- 10.1128/AEM.01301-09 · DOI
- 10.1128/JB.00726-07 · DOI
- 10.1073/pnas.1504281112 · DOI
- 10.1038/emboj.2010.99 · DOI
- 10.1111/j.1365-2958.2005.04522.x · DOI
- 10.1073/pnas.0906851106 · DOI
- 10.1099/mic.0.27718-0 · DOI
- 10.1111/mmi.12873 · DOI
- Sambrook J., 1989, Molecular Cloning: A Laboratory Manual, 3 v
- 10.1038/nmeth.2644 · DOI
- 10.1107/S0021889808006985 · DOI
- 10.1016/j.micinf.2007.05.011 · DOI
- 10.1093/nar/gkn675 · DOI
- 10.1093/nar/gnh110 · DOI
Cited by
Sorted by citations
Toward the Complete Functional Characterization of a Minimal Bacterial Proteome
Bianchi, D. M., Pelletier, J. F., Hutchison, C. A., Glass, J. I., & Luthey-Schulten, Z. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04188 · Cited by 22
Metadata
- Authors
- Rismondo, J., Cleverley, R. M., Lane, H. V., Großhennig, S., Steglich, A., Möller, L., Mannala, G. K., Hain, T., Lewis, R. J., & Halbedel, S.
- Affiliations
- Robert Koch Institute (DE)
- Newcastle University (GB)
- ZBS 4 – Advanced Light and Electron Microscopy Robert Koch Institute Berlin Germany
- Justus-Liebig-Universität Gießen (DE)
- Corresponding author
- Halbedel, Sven
- ORCID
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2015-12-18
- Volume
- 99
- Issue
- 5
- Pages
- 978-998
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2179454313
- Cited by
- 55
- References
- 2
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 4 · 2023: 5 · 2022: 7 · 2021: 2 · 2020: 4 · 2019: 13 · 2018: 3 · 2017: 5 · 2016: 7
- FWCI
- 3.42
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by)
- Newcastle University ePrints (Newcastle Univesity) (cc-by-nc-nd)
- Funders
- DFG (HA 6830/1-1)
- UK BBSRC (BB/G015902/1, BB/M001180/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Keywords
- bacterial cell division, penicillin-binding proteins, Listeria monocytogenes, cell wall biosynthesis, crystal structure, protein-protein interaction, virulence, antibiotic targets, cell growth regulation
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Cell Division, Cell Wall, Listeria monocytogenes, Models, Molecular, Structure-Activity Relationship, Protein Structure, Secondary, Cell Cycle Proteins, Virulence Factors, Penicillin-Binding Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
