Teeth offer nonshedding surfaces on which a wide range of bacterial species accumulate as thick, cohesive plaques. Intergeneric coaggregation mediated by specific recognition between surface "cohesins" is thought to contribute to both the cohesiveness of plaque and the sequence in which bacteria colonize the tooth surface. There is some evidence that Gram-positive species, like the efficient tooth colonizer Actinomyces viscosus, enhance subsequent tooth colonization by the more virulent periodontal pathogen Bacteroides gingivalis. To study their mechanism of cohesion, we have developed an in vitro assay that measures the sequential binding of tritium-labeled B. gingivalis to A. viscosus adsorbed to saliva-coated hydroxyapatite beads, mimicking teeth (actinobeads). The assay yields equilibrium and kinetics data amenable to statistical analysis. The presence of A. viscosus significantly increased the number of B. gingivalis cells bound. Inhibition studies were conducted to test the sensitivity of binding to heat; to various saccharides and sugar amines; to proteolytic treatment of Bacteroides; and to incorporation of various chaotropic agents, increased KCl, and saliva in the suspension buffer. Heating the Bacteroides cells but not the actinobeads diminished Bacteroides adherence. Proteolysis and various saccharides had little, if any, effect. Among chaotropic agents, NaSCN and LiCl reduced numbers of cells bound by 40%, but tetramethylurea had no effect. Increasing the ionic concentration of KCl reduced binding by 50 to 60%. Diluted saliva showed a concentration-dependent inhibition of B. gingivalis adherence to actinobeads. To begin examining B. gingivalis surface molecules significant to these reactions, lipopolysaccharide was extracted by the phenol-water method and analyzed by biochemical assays and polyacrylamide gel electrophoresis.(ABSTRACT TRUNCATED AT 250 WORDS)
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Sci Adv
January 2025
Simpson Querrey Institute for Epigenetics, Department of Biochemistry and Molecular Genetics Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
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View Article and Find Full Text PDFPLoS One
January 2025
Virology Group, Vice-chancellor of Research, Universidad El Bosque, Bogotá, Colombia.
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View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Cellular and Structural Physiology Laboratory, Advanced Research Initiative, Institute of Integrated Research, Institute of Science Tokyo, Bunkyo-ku, Tokyo 113-8510, Japan.
Pathogen mutations present an inevitable and challenging problem for therapeutics and the development of mutation-tolerant anti-infective drugs to strengthen global health and combat evolving pathogens is urgently needed. While spike proteins on viral surfaces are attractive targets for preventing viral entry, they mutate frequently, making it difficult to develop effective therapeutics. Here, we used a structure-guided strategy to engineer an inhibitor peptide against the SARS-CoV-2 spike, called CeSPIACE, with mutation-tolerant and potent binding ability against all variants to enhance affinity for the invariant architecture of the receptor-binding domain (RBD).
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January 2025
Student Research Committee, Urmia University of Medical Sciences, Urmia, Iran.
Ferroptosis is a type of cell death that multiple mechanisms and pathways contribute to the positive and negative regulation of it. For example, increased levels of reactive oxygen species (ROS) induce ferroptosis. ferroptosis unlike apoptosis, it is not dependent on caspases, but is dependent on iron.
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January 2025
Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Central 5 1-1-1 Higashi, Tsukuba 305-8565, Ibaraki, Japan.
Nestin is a type VI intermediate filament protein and a well-known neural stem cell marker. It is also expressed in high-grade cancer cells, forming copolymerized filaments with vimentin. We previously showed that nestin inhibits the binding of vimentin's tail domain to actin filaments (AFs) by steric hindrance through its large nestin tail domain (NTD), thereby increasing three-dimensional cytoskeleton network mobility, enhancing cell flexibility, and promoting cancer progression.
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