Copyright information:Taken from "Sequence analyses of fimbriae subunit FimA proteins on genospecies 1 and 2 and with variant carbohydrate binding specificities"BMC Microbiology 2006;6():43-43.Published online 10 May 2006PMCID:PMC1473193.Copyright © 2006
Nicklas Strömberg (72685) +6 more
core +1 more source
Aggregatibacter actinomycetemcomitans:dissecting the roles of fimbriae and secreted proteins in virulence [PDF]
The most prevalent disease on planet earth, periodontitis, is an inflammatory disease that destroys soft tissues and bone surrounding our teeth, ultimately leading to tooth loss.
Fu, Yanyan, Fu, Yanyan; id_orcid
core +1 more source
Inflammatory and Immunological Basis of Periodontal Diseases
The periodontal lesion emerges as an evolving immunological battlefield, where host–microbiome interactions, dysregulated immune responses, fragile resolution mechanisms, and inflammophilic dysbiosis converge to shift the balance from homeostasis to unrestrained tissue destruction.
Giacomo Baima +3 more
wiley +1 more source
Permissive linker insertion sites in the outer membrane protein of 987P fimbriae of Escherichia coli
The FasD protein is essential for the biogenesis of 987P fimbriae of Escherichia coli. In this study, subcellular fractionation was used to demonstrate that FasD is an outer membrane protein. In addition, the accessibility of FasD to proteases established the presence of surface-exposed FasD domains on both sides of the outer membrane.
D M, Schifferli, M A, Alrutz
openaire +3 more sources
Direct evidence that the FimH protein is the mannose-specific adhesin of Escherichia coli type 1 fimbriae [PDF]
Type 1 fimbriae of Escherichia coli are surface organelles which mediate binding to D-mannose-containing structures. By direct binding of FimH to D-mannose attached to a carrier protein, we demonstrated that this protein was uniquely responsible for the receptor specificity.
K A, Krogfelt, H, Bergmans, P, Klemm
openaire +2 more sources
The Keystone‐Pathogen Hypothesis Updated: The Role of Porphyromonas gingivalis in Periodontitis
Porphyromonas gingivalis orchestrates a coordinated manipulation of immune and inflammatory responses in periodontal tissues which leads to the generation of a dysbiotic, subgingival biofilm community, and progression of periodontitis. The type 9 secretion system, lipid A modification, and the formation of outer membrane vesicles are important ...
Mike A. Curtis +2 more
wiley +1 more source
Nanoparticles in Periodontology and Implant Dentistry: From Mechanisms to Clinical Applications
Nanotechnology holds significant promise in improving dental care, yet there is a need for more reliable clinical studies to validate its effectiveness and safety. ABSTRACT Recent advances in nanotechnology are reshaping the landscape of periodontology and implant dentistry, particularly through the application of nanoparticles (NPs).
Chun Xu +4 more
wiley +1 more source
Periodontal Medicine Rewired: Mechanisms Linking Periodontitis to Systemic Diseases
This review reorganizes decades of research in periodontal medicine into a multi‐dimensional framework, illustrating how periodontitis influences systemic health through at least seven interconnected mechanisms. ABSTRACT Periodontitis is now recognized not merely as a localized oral condition but as a systemic disease linked to over 70 communicable and
Mario Romandini +3 more
wiley +1 more source
The Oral‐Gut Axis: Bidirectional Interactions Between Microbiome and Diseases
This study aims to summarize the mechanisms underlying ectopic colonization of the gut by oral pathobionts and the microbial and host factors that regulate this process. ABSTRACT Increased colonization of typically oral microorganisms is frequently observed in the gut mucosa or lumen of individuals with gastrointestinal disorders, including patients ...
Shinya Ebihara, Nobuhiko Kamada
wiley +1 more source
Epithelial cell binding of group A streptococci by lipoteichoic acid on fimbriae denuded of M protein. [PDF]
Group A streptococci were treated with various enzymatic and chemical agents in an attempt to dissociate the type-specific M protein from intact surface "fimbriae." Mild peptic digestion at pH 5.8, which was previously shown to extract serologically active M antigen from intact streptococci had little visible effect on the fimbriae even though ...
E H, Beachey, I, Ofek
openaire +2 more sources

