Kingella kingae strain:KKGP01
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ABSTRACT:
PROVIDER: PRJNA1097560 | ENA |
REPOSITORIES: ENA
Similar Datasets
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Project description:Type IV Pili (T4P) are dynamic surface appendages that mediate adherence, motility, and DNA uptake in Kingella kingae, an important pediatric pathogen that causes osteoarticular infections, bacteremia, and endocarditis. While the major pilin subunit in K. kingae T4P is well characterized, the contribution of minor pilins to T4P structure and function remains unknown. Here, we used proteomics, molecular genetics, biochemical analyses, and structural modeling to identify and characterize all eight minor pilins in K. kingae. We identified a conserved operon of core minor pilin genes encoding FimT, PilV, PilW, PilX, and PilE that promotes surface piliation, adherence to epithelial cells, twitching motility, and natural transformation. Deletion of the fimTpilVWXE locus phenocopied loss of the PilC1 and PilC2 adhesins, and AlphaFold modeling combined with bacterial two-hybrid analysis suggested that FimT, PilV, PilW, and PilX form a complex at the pilus tip. The PilA2, ComP, and KK03_01180 minor pilins were dispensable for adherence and motility but promoted natural transformation and formed protein-protein interactions with the major pilin, suggesting that these proteins are incorporated throughout the pilus shaft. These findings support a new model for the architecture of the K. kingae type IV pilus, with distinct minor pilins localizing to different sites on the pilus fiber and mediating specialized functions essential for virulence.
2025-10-06 | PXD068177 | Pride
Project description:Kingella negevensis is a newly described gram-negative bacterium in the Neisseriaceae family and is closely related to Kingella kingae, an important cause of pediatric osteoarticular infections and other invasive diseases. Like K. kingae, K. negevensis can be isolated from the oropharynx of young children, although at a much lower rate. Due to the potential for misidentification as K. kingae, the burden of disease due to K. negevensis is currently unknown. Similarly, there is little known about virulence factors present in K. negevensis and how they compare to virulence factors in K. kingae. Using a variety of approaches, we show that K. negevensis produces many of the same putative virulence factors that are present in K. kingae, including a polysaccharide capsule, a secreted exopolysaccharide, a Knh-like trimeric autotransporter, and type IV pili, suggesting that K. negevensis may have significant pathogenic potential.
| S-EPMC7598479 | biostudies-literature
Project description:The RtxA cytotoxin, a member of the RTX (Repeats in ToXin) family of pore-forming toxins, is the primary virulence factor of the paediatric facultative pathogen Kingella kingae. Although structure-function studies of RTX toxins have defined their characteristic domains and features, the exact membrane topology of RTX toxins remains unknown. Here, we used labelling of cell-bound RtxA with a membrane-impermeable, lysine-reactive reagent and subsequent detection of the labelled lysine residues by mass spectrometry, which revealed that most of the membrane-bound toxin is localised extracellularly. A trypsin protection assay with cell-bound RtxA demonstrated that five of seven transmembrane α-helices, predicted by various algorithms within the N-terminal half of the molecule, are irreversibly embedded in the membrane. Structure-function analysis showed that these α-helices, four of which are arranged as two pairs of back-to-back helices, are essential for the formation of an ion-conducting membrane pore. In contrast, the C-terminal half of RtxA is required for the interaction with the cell surface and for the irreversible insertion of the toxin into the membrane via acyl chains covalently linked to the molecule. These findings advance our understanding of the structure-function relationships of RtxA and enable us to propose a membrane topology model of the toxin.
2025-02-18 | PXD060913 | Pride