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Full-Text Articles in Medicine and Health Sciences
Staphylococcus Aureus Floating Biofilm Formation And Phenotype In Synovial Fluid Depends On Albumin, Fibrinogen, And Hyaluronic Acid, Samantha Knott, Dylan Curry, Neil Zhao, Pallavi Metgud, Sana Dastgheyb, Caroline Purtill, Marc I. Harwood, Md, Antonia F Chen, Thomas P Schaer, Michael Otto, Noreen J. Hickok
Staphylococcus Aureus Floating Biofilm Formation And Phenotype In Synovial Fluid Depends On Albumin, Fibrinogen, And Hyaluronic Acid, Samantha Knott, Dylan Curry, Neil Zhao, Pallavi Metgud, Sana Dastgheyb, Caroline Purtill, Marc I. Harwood, Md, Antonia F Chen, Thomas P Schaer, Michael Otto, Noreen J. Hickok
Department of Orthopaedic Surgery Faculty Papers
Biofilms are typically studied in bacterial media that allow the study of important properties such as bacterial growth. However, the results obtained in such media cannot take into account the bacterial localization/clustering caused by bacteria–protein interactions in vivo and the accompanying alterations in phenotype, virulence factor production, and ultimately antibiotic tolerance. We and others have reported that methicillin-resistant or methicillin-susceptible Staphylococcus aureus (MRSA or MSSA, respectively) and other pathogens assemble a proteinaceous matrix in synovial fluid. This proteinaceous bacterial aggregate is coated by a polysaccharide matrix as is characteristic of biofilms. In this study, we identify proteins important for this …
Collagen Structure-Function Mapping Informs Applications For Regenerative Medicine., James D San Antonio, Olena Jacenko, Andrzej Fertala, Joseph P R O Orgel
Collagen Structure-Function Mapping Informs Applications For Regenerative Medicine., James D San Antonio, Olena Jacenko, Andrzej Fertala, Joseph P R O Orgel
Department of Orthopaedic Surgery Faculty Papers
Type I collagen, the predominant protein of vertebrates, assembles into fibrils that orchestrate the form and function of bone, tendon, skin, and other tissues. Collagen plays roles in hemostasis, wound healing, angiogenesis, and biomineralization, and its dysfunction contributes to fibrosis, atherosclerosis, cancer metastasis, and brittle bone disease. To elucidate the type I collagen structure-function relationship, we constructed a type I collagen fibril interactome, including its functional sites and disease-associated mutations. When projected onto an X-ray diffraction model of the native collagen microfibril, data revealed a matrix interaction domain that assumes structural roles including collagen assembly, crosslinking, proteoglycan (PG) binding, and …