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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Polycationic polymers have been noted for their effects in promoting cell adhesion to various surfaces, but previous studies have failed to describe a mechanism dealing with this type of adhesion. In the present study, three polycationic polymers (chitosan, poly-L-lysine, and lysozyme) were tested for their effects on microbial hydrophobicity, as determined by adhesion to hydrocarbon and polystyrene. Test strains (Escherichia coli, Candida albicans, and a nonhydrophobic mutant, MR-481, derived from Acinetobacter calcoaceticus RAG-1) were vortexed with hexadecane in the presence of the various polycations, and the extent of adhesion was measured turbidimetrically. Adhesion of all three test strains rose from near zero values to over 90% in the presence of low concentrations of chitosan (125 to 250 micrograms/ml). Adhesion occurred by adsorption of chitosan directly to the cell surface, since E. coli cells preincubated in the presence of the polymer were highly adherent, whereas hexadecane droplets pretreated with chitosan were subsequently unable to bind untreated cells. Inorganic cations (Na+, Mg2+) inhibited the chitosan-mediated adhesion of E. coli to hexadecane, presumably by interfering with the electrostatic interactions responsible for adsorption of the polymer to the bacterial surface. Chitosan similarly promoted E. coli adhesion to polystyrene at concentrations slightly higher than those which mediated adhesion to hexadecane. Poly-L-lysine also promoted microbial adhesion to hexadecane, although at concentrations somewhat higher than those observed for chitosan. In order to study the effect of the cationic protein lysozyme, adhesion was studied at 0 degree C (to prevent enzymatic activity), using n-octane as the test hydrocarbon. Adhesion of E. coli increased by 70% in the presence of 80 micrograms of lysozyme per ml. When the negatively charged carboxylate residues on the E. coli cell surface were substituted for positively charged ammonium groups, the resulting cells became highly hydrophobic, even in the absence of polycations. The observed "hydrophobicity" of the microbial cells in the presence of polycations is thus probably due to a loss of surface electronegativity. The data suggest that enhancement of hydrophobicity by polycationic polymers is a general phenomenon.
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PMID:Mechanism of enhancement of microbial cell hydrophobicity by cationic polymers. 221 2

Alysiella bovis adheres to surfaces by means of short, ruthenium red-staining, rod-like fimbriae. The fimbriae remain associated with the cell envelope of A. bovis, even when sonicated or exposed sequentially to toluene, Triton X-100, lysozyme, ribonuclease, and deoxyribonuclease. Adhesion of outer membrane-derived cell wall ghosts of A. bovis to glass was inhibited by IO4-, sodium dodecyl sulfate, urea, pronase, and trypsin. Protease treatment digested the fimbriae from the distal end, and exposure to sodium dodecyl sulfate depolymerized the fimbriae. Exposure of ghosts to 1% sodium dodecyl sulfate preferentially solubilized a 16,500-dalton protein which was subsequently purified by gel filtration and demonstrated to be a glycoprotein (ca. 17% carbohydrate). Antibodies raised against the 16,500-dalton glycoprotein agglutinated whole cells and inhibited adhesion of ghosts to glass.
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PMID:Mechanism of adhesion of Alysiella bovis to glass surfaces. 620 60

An in vitro quantitative study of the adhesion of a Staphylococcus aureus strain to two types of disposable contact lenses has been carried out. The first type was an ionic/high-water-content (I-HWC) lens (42% Etafilcon A, 58% water) and the second was a non-ionic/low-water-content (Nl-LWC) lens (61.4% poly(2-hydroxyethyl methacrylate), 38.6% water). Adhesion to the two lens types was evaluated both in basic conditions and after treatment with lysozyme. The results showed that I-HWC lenses are more prone to Staphylococcus aureus adhesion than NI-LWC lenses, both untreated (+15.4%) and treated with lysozyme (+20.5%). Lysozyme increased bacterial adhesion by 30.5% on the lenses with lower water content, and by 36.3% on those with higher water content.
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PMID:Disposable contact lenses and bacterial adhesion. In vitro comparison between ionic/high-water-content and non-ionic/low-water-content lenses. 757 71

T cell recognition of foreign Ag/MHC class II complexes is sensitive down to approximately 100 complexes per cell or approximately 0.2 complexes/micron2. To better understand the physical basis of the recognition stage of Ag presentation, we examined adhesion of the lysozyme- specific T cell hybridoma, 3A9, to artificial bilayers containing covalent MHC class II/peptide complexes or adhesion molecules. Adhesion of 3A9 cells required a superphysiologic density of the MHC class II/peptide complex and was partly dependent on CD4; cells adhered but did not crawl. No adhesion was observed to bilayers containing MHC class II molecules without the lysozyme peptide. Activated 3A9 cells adhered and crawled on bilayers containing ICAM-1. The physical strength of contacts was tested with fluid shear. 3A9 cells adherent to bilayers containing MHC class II/peptide complexes shed their contact, which remained on the substrate and contained TCR. In contrast, 3A9 cells peeled from the ICAM-1 bilayer, and held firmly on LFA-1 bilayers; in a manner dependent on filamentous actin. When ICAM-1 and the MHC/peptide complexes were combined, the 3A9 cells adhered tightly and spread, but did not crawl, on the bilayers and TCR clustered at the center of the contact area. Physiologically, the TCR is unlikely to directly initiate adhesion. TCR clusters formed with the assistance of adhesion mechanisms may have to be shed to allow de-adhesion, and this may contribute to TCR down-regulation.
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PMID:TCR-mediated adhesion of T cell hybridomas to planar bilayers containing purified MHC class II/peptide complexes and receptor shedding during detachment. 875 22

It has previously been shown that Lactobacillus fermentum strain 104r releases compounds into its culture fluid that inhibit the adhesion of enterotoxigenic Escherichia coli K88. The aim of the present study was to purify and identify this compound. Judged by gel filtration, the compound was found to be approximately 1700 kDa. The amount of active compound increased upon prolonged incubation, while the number of viable cells reduced, suggesting that the activity was coming from dead cells. As the activity can be destroyed by lysozyme treatment and contains glucose, N-acetylglucosamine and galactose, it was concluded that cell wall fragments are the active agent, although cell wall preparations did not have the same effect. Adhesion to some mucus fractions could be inhibited by spent culture fluid, indicating specific interaction between mucus and the active compound. The compound was not able to interfere with the adhesion of E. coli 1107 to neutral lipids from mucus which contain a glycolipid receptor for K88 fimbriae.
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PMID:Purification and characterization of a component produced by Lactobacillus fermentum that inhibits the adhesion of K88 expressing Escherichia coli to porcine ileal mucus. 885 78

Adhesion of yeasts and bacteria to silicone rubber is one of the first steps in the biodeterioration of silicone rubber voice prostheses. In this paper, adhesion of two streptococcal, staphylococcal, Candida albicans and Candida tropicalis strains, isolated from explanted voice prostheses was investigated to silicone rubber with and without a salivary conditioning film in a parallel-plate flow chamber. Within each microbial pair of one species, the strain with the most negative zeta potential adhered most slowly to negatively charged silicone rubber. No other clear relationships were obvious between adhesion to silicone rubber and microbial zeta potentials of cell-surface hydrophobicities, as by water contact angles. A 1.5-h adsorbed salivary conditioning film appeared to possess components, presumably albumin and lysozyme, slowing down the deposition of the yeasts and some of the streptococcal and staphylococcal isolates. In addition, microbial adhesion in a stationary end point was generally lower to silicone rubber with an adsorbed salivary conditioning film than without one. Nearly all microorganisms adhering to an adsorbed salivary conditioning film, yeasts as well as bacteria, were stimulated to detach by the passage of an air bubble through the chamber, but microorganisms adhering directly to the silicone rubber, especially C tropicalis strains, detached in far lower numbers under the influence of a passing air bubble. The present observations are in agreement with clinical in vivo findings that in patients with reduced saliva production after radiotherapy, the device life of the voice prosthesis is significantly shortened and suggests that isolated salivary components might be used as an anti-adhesive.
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PMID:Adhesion to silicone rubber of yeasts and bacteria isolated from voice prostheses: influence of salivary conditioning films. 902

Tear-protein adhesion to contact lenses contributes to lens contamination and deterioration, and depends primarily on the type of contact-lens material used. Adhesion of tear proteins to contact lenses and glass vials was examined using spectrophotometry, hydrophobic-interaction HPLC and bicinchoninic acid (BCA) protein assay. Using spectrophotometry at 280 nm, vials containing two proteins (lysozyme and milk lipocalin) at three different concentrations were examined for changes in their protein concentrations over a 3-week period. Vials containing 5.0 mg/ml lysozyme lost about one-third of their protein (P<0.005), while vials containing 5.0 mg/ml milk lipocalin lost two-thirds of their protein (P<0.01). Conversely, vials containing 1.0 mg/ml lysozyme lost two-thirds of their protein (P<0.005), while vials containing 1.0 mg/ml milk lipocalin lost one-third of their protein (P>0.05). Subsequently, lysozyme deposition on both glass vials and contact lenses was monitored for 5 days using spectrophotometry, to determine lysozyme content in the vials, and HPLC, to determine lysozyme deposition on contact lenses stored in the same vials. This experiment indicated considerable variation in lysozyme deposition on vials and contact lenses, with vial deposition remaining relatively constant (P>0.05) while lens deposition decreased and then increased (P<0.05). Finally, the same experiment was repeated, monitoring lysozyme deposition using the BCA assay. This experiment yielded the most consistent results, with lysozyme deposition on vials continuing throughout the 5 day experiment (P<0.05), while deposition on lenses again decreased and then increased, although to a much lesser extent than in the previous experiment (P>0.05).
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PMID:Adhesion of tear proteins to contact lenses and vials. 1148 48

Bacterial surfaces contain proteins, polysaccharides, and other biopolymers that can affect their adhesion to another surface. To better understand the role of proteins in bacterial adhesion, the interactions between two different model colloids (glass beads and carboxylated latex microspheres) and four proteins covalently bonded to glass surfaces were examined using colloid probes and an atomic force microscope (AFM). Adhesion forces between an uncoated glass colloid probe and protein-coated surfaces, measured in retraction force curves, decreased in the order poly-D-lysine > lysozyme > protein A > BSA. This ordering was consistent with the relative calculated charges of the proteins at neutral pH and the zeta-potentials measured for glass beads and latex microspheres coated with these proteins. When the glass bead was coated with a protein (BSA), overall adhesion forces between the protein-coated colloid and the protein-coated surfaces were reduced, and the adhesion force for each protein decreased in the same order observed in experiments with the uncoated glass bead. When latex colloid probes were coated with BSA, adhesion forces were significantly larger than those measured with BSA-coated glass colloid probes under the same conditions, demonstrating that the nature of the underlying colloid can affect the measured interaction forces. In addition, the adhesion forces measured with the BSA-coated latex colloid increased in a different order (BSA < lysozyme < protein A < poly-D-lysine) than that observed using the BSA-coated glass colloid. It was also found that increasing the solution ionic strength consistently decreased adhesion forces. This result is contrary to the general observation that bacterial adhesion increases with ionic strength. It was speculated that conformational changes of the protein produced this decrease in adhesion with increased ionic strength. These results suggest the need to measure nanoscale adhesion forces in order to understand better molecular scale interactions between colloids and surfaces.
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PMID:Interaction forces between colloids and protein-coated surfaces measured using an atomic force microscope. 1595 63

Exopolymers are thought to influence bacterial adhesion to surfaces, but the time-dependent nature of molecular-scale interactions of biopolymers with a surface are poorly understood. In this study, the adhesion forces between two proteins and a polysaccharide [Bovine serum albumin (BSA), lysozyme, or dextran] and colloids (uncoated or BSA-coated carboxylated latex microspheres) were analyzed using colloid probe atomic force microscopy (AFM). Increasing the residence time of an uncoated or BSA-coated microsphere on a surface consistently increased the adhesion force measured during retraction of the colloid from the surface, demonstrating the important contribution of polymer rearrangement to increased adhesion force. Increasing the force applied on the colloid (loading force) also increased the adhesion force. For example, at a lower loading force of approximately 0.6 nN there was little adhesion (less than -0.47 nN) measured between a microsphere and the BSA surface for an exposure time up to 10 s. Increasing the loading force to 5.4 nN increased the adhesion force to -4.1 nN for an uncoated microsphere to a BSA surface and to as much as -7.5 nN for a BSA-coated microsphere to a BSA-coated glass surface for a residence time of 10 s. Adhesion forces between colloids and biopolymer surfaces decreased inversely with pH over a pH range of 4.5-10.6, suggesting that hydrogen bonding and a reduction of electrostatic repulsion were dominant mechanisms of adhesion in lower pH solutions. Larger adhesion forces were observed at low (1 mM) versus high ionic strength (100 mM), consistent with previous AFM findings. These results show the importance of polymers for colloid adhesion to surfaces by demonstrating that adhesion forces increase with applied force and detention time, and that changes in the adhesion forces reflect changes in solution chemistry.
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PMID:Residence time, loading force, pH, and ionic strength affect adhesion forces between colloids and biopolymer-coated surfaces. 1604 84

Proteins are important in bacterial adhesion, but interactions at molecular-scales between proteins and specific functional groups are not well understood. The adhesion forces between four proteins [bovine serum albumin (BSA), protein A, lysozyme, and poly-d-lysine] and COOH, NH2 and OH-functionalized (latex) colloids were examined using colloid probe atomic force microscopy (AFM) as the function of colloid residence time (T) and solution ionic strength (IS). For three of the proteins, OH-functionalized colloids produced higher adhesion forces to proteins (2.6-30.5 nN; IS=1 mM, T=10s) than COOH- and NH2-functionalized colloids (1.6-6.8 nN). However, protein A produced the largest adhesion force (8.1+/-1.0 nN, T=10 s) with the COOH-functionalized colloid, demonstrating the importance of specific and unanticipated protein-functional group interactions. The NH2-functionalized colloid typically produced the lowest adhesion forces with all proteins, likely due to repulsive electrostatic forces and weak bonds for NH2-NH2 interactions. The adhesion force (F) between functionalized colloids and proteins consistently increased with residence time (T), and data was well fitted by F=ATn. The constant value of n=0.21+/-0.07 for all combinations of proteins and functionalized colloids indicated that water exclusion and protein rearrangement were the primary factors affecting adhesion over time. Adhesion forces decreased inversely with IS for all functional groups interacting with surface proteins, consistent with previous findings. These results demonstrate the importance of specific molecular-scale interactions between functional groups and proteins that will help us to better understand factors colloidal adhesion to surfaces.
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PMID:Adhesion forces between functionalized latex microspheres and protein-coated surfaces evaluated using colloid probe atomic force microscopy. 1650 91


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