ArticleJournal of molecular biology2017
The Proline/Glycine-Rich Region of the Biofilm Adhesion Protein Aap Forms an Extended Stalk that Resists Compaction.
Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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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
22 citing papers in PubMed, 32 citations in OpenAlex.
- Assembly landscape of the complete B-repeat superdomain from Staphylococcus epidermidis strain 1457.Biophysical journal · 2025Article
- The pathogenicity and virulence of the opportunistic pathogenVirulence · 2024Review
- Hydrodynamic Radii of Intrinsically Disordered Proteins: Fast Prediction by Minimum Dissipation Approximation and Experimental Validation.The journal of physical chemistry letters · 2024Article
- Diversity of hydrodynamic radii of intrinsically disordered proteins.European biophysics journal : EBJ · 2023Article
- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.Protein science : a publication of the Protein Society · 2023Article
- Convergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.bioRxiv : the preprint server for biology · 2023Article
- Expression, purification, and characterisation of the p53 binding domain of Retinoblastoma binding protein 6 (RBBP6).PloS one · 2023Article
- Antibacterial and anti-biofilm activities of Disaspidin BB againstFrontiers in microbiology · 2023Article
- Solution Structural Studies of Pre-amyloid Oligomer States of the Biofilm Protein Aap.Journal of molecular biology · 2022Article
- Expression, Purification, Characterization and Cellular Uptake of MeCP2 Variants.The protein journal · 2022Article
- A targeted bioinformatics approach identifies highly variable cell surface proteins that are unique to Glomeromycotina.Mycorrhiza · 2022Article
- Article
- Seeing Keratinocyte Proteins through the Looking Glass of Intrinsic Disorder.International journal of molecular sciences · 2021Review
- Biofilms by bacterial human pathogens: Clinical relevance - development, composition and regulation - therapeutical strategies.Microbial cell (Graz, Austria) · 2021Review
- The staphylococcal biofilm protein Aap forms a tetrameric species as a necessary intermediate before amyloidogenesis.The Journal of biological chemistry · 2020Article
- The biofilm adhesion protein Aap fromThe Journal of biological chemistry · 2020Article
- Combination of Biodata Mining and Computational Modelling in Identification and Characterization of ORF1ab Polyprotein of SARS-CoV-2 Isolated from Oronasopharynx of an Iranian Patient.Biological procedures online · 2020Article
- Staphylococcal Biofilms.Microbiology spectrum · 2018Review
- Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions.Annual review of biophysics · 2018Article
- Staphylococcal Biofilms in Atopic Dermatitis.Current allergy and asthma reports · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Staphylococcus epidermidis is one of the primary bacterial species responsible for healthcare-associated infections. The most significant virulence factor for S. epidermidis is its ability to form a biofilm, which renders the bacteria highly resistant to host immune responses and antibiotic action. Intercellular adhesion within the biofilm is mediated by the accumulation-associated protein (Aap), a cell wall-anchored protein that self-assembles in a zinc-dependent manner. The C-terminal portion of Aap contains a 135-aa-long, proline/glycine-rich region (PGR) that has not yet been characterized. The region contains a set of 18 nearly identical AEPGKP repeats. Analysis of the PGR using biophysical techniques demonstrated the region is a highly extended, intrinsically disordered polypeptide with unusually high polyproline type II helix propensity. In contrast to many intrinsically disordered polypeptides, there was a minimal temperature dependence of the global conformational state of PGR in solution as measured by analytical ultracentrifugation and dynamic light scattering. Furthermore, PGR was resistant to conformational collapse or α-helix formation upon the addition of the osmolyte trimethylamine N-oxide or the cosolvent 2,2,2-trifluoroethanol. Collectively, these results suggest PGR functions as a resilient, extended stalk that projects the rest of Aap outward from the bacterial cell wall, promoting intercellular adhesion between cells in the biofilm. This work sheds light on regions of low complexity often found near the attachment point of bacterial cell wall-anchored proteins.
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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.