biostudies-literatureYarawsky AEUniversity of CincinnatiNational Institute of General Medical SciencesNIGMS NIH HHSNIH HHSe4707https://www.ebi.ac.uk/biostudies/studies/S-EPMC10367597biostudies-literatureUnknown32(8)Staphylococcus epidermidis and Staphylococcus aureus are highly problematic bacteria in hospital settings. A major challenge is their ability to form biofilms on abiotic or biotic surfaces. Biofilms are well-organized, multicellular bacterial aggregates that resist antibiotic treatment and often lead to recurrent infections. Bacterial cell wall-anchored (CWA) proteins are important players in biofilm formation and infection. Many have putative stalk-like regions or regions of low complexity near the cell wall-anchoring motif. Recent work demonstrated the strong propensity of the stalk region of S. epidermidis accumulation-associated protein (Aap) to remain highly extended under solution conditions that typically induce compaction. This behavior is consistent with the expected function of aProtein science : a publication of the Protein SocietyConvergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.PMC10367597P30 GM138395R01 GM094363S10 OD018090R15 GM115603Ori ALHerr ABWhitten STEnglish LRYarawsky AEfalseConvergent behavior of extended stalk regions from staphylococcal surface proteins with widely divergent sequence patterns.Staphylococcus epidermidis and Staphylococcus aureus are highly problematic bacteria in hospital settings. A major challenge is their ability to form biofilms on abiotic or biotic surfaces. Biofilms are well-organized, multicellular bacterial aggregates that resist antibiotic treatment and often lead to recurrent infections. Bacterial cell wall-anchored (CWA) proteins are important players in biofilm formation and infection. Many have putative stalk-like regions or regions of low complexity near the cell wall-anchoring motif. Recent work demonstrated the strong propensity of the stalk region of S. epidermidis accumulation-associated protein (Aap) to remain highly extended under solution conditions that typically induce compaction. This behavior is consistent with the expected function of a2023-01-01T00:00:00Z2023 Aug2025-04-05T12:35:40.181Z2025-04-05T12:35:40.181ZS-EPMC103675973733449110.1002/pro.470710.1101/2023.01.06.523059