1,721,259 research outputs found
Editorial: Recent Advances in Recombinant Antibody Therapeutics and Diagnostics for Infectious Diseases
No full textAntibodies to the FbsA protein of streptococcus agalactiae and their use in treating or preventing infections
No full textMonoclonal and polyclonal antibodies are provided which can bind to the FbsA protein of Streptococcus agalactiae (GBS) and which can be used to prevent adherence of the bacteria to host cells and thus be useful in the treatment and protection against infection from S. agalactiae. The antibodies of the invention can also be raised against the fibrinogen binding domain of FbsA or the repeat region therein, and in addition to preventing bacterial adherence, the antibodies to FbsA are advantageous in that they can be used to prevent platelet aggregation and thrombus formatio
Falsely Elevated Whole Blood Cyclosporine Concentrations Measured by an Immunoassay With Automated Pretreatment
No full textTherapeutic drug monitoring of
cyclosporine A (CyA) blood concentrations
is needed to ensure therapeutic
efficacy and to prevent toxicity, because
it exhibits marked pharmacokinetic variability
and, in the case of high concentrations,
a dose reduction is required
Editorial: Cells, Biomaterials, and Biophysical Stimuli for Bone, Cartilage, and Muscle Regeneration
No full textVisai, Livia/0000-0003-1181-3632; Fassina, Lorenzo/0000-0002-5587-4632; Ramalingam, Murugan/0000-0001-6498-9792; Cusella De Angelis, Maria Gabriella/0000-0003-2642-3346[No Abstract Available
Isolation and characterization of a novel collagen-binding protein from Streptococcus pyogenes strain 6414
No full textIn this report we have analyzed the binding of collagen to Streptococcus pyogenes strain 6414. This binding was rapid, specific, and involved a limited number of receptor molecules (11,600 copies per cell). When the proteins in a streptococcal lysate were blotted onto a nitrocellulose filter and probed with 125I-labeled collagen, a prominent collagen-binding protein of 57 kDa was identified as well as minor 130-150-kDa components. The major 57-kDa protein was isolated by affinity chromatography on collagen-Sepharose followed by gel filtration chromatography. The 57-kDa protein purified from S. pyogenes was used to raise a monospecific antibody which also reacted with a collagen-binding protein of similar molecular size isolated from Streptococcus zooepidemicus. The two collagen-binding proteins from streptococci have a similar amino acid composition and isoelectric points. Isolated collagen-binding protein was specifically recognized by 125I-collagen in a solid-phase binding assay and displayed an affinity for the ligand quite similar to that exhibited by intact bacteria (Kd = 3.1 versus 3.5 x 10(-9) M, respectively). Surface-labeled bacteria attached to microtiter wells coated with different collagen types and the 57-kDa protein blocked the adhesion to collagen substrate. We propose that the 57-kDa protein is an adhesin involved in the attachment of streptococci to host tissues
Rapid detection of human metapneumovirus strains in nasopharyngeal aspirates and shell vial cultures by monoclonal antibodies.
Full text linkMonoclonal antibodies to human metapneumovirus (hMPV) were developed for direct fluorescent antibody (DFA) staining of nasopharyngeal aspirates from 40 infants with respiratory infections, as well as for hMPV identification in shell vial cultures. With reference to reverse transcription-PCR, DFA staining showed sensitivity, specificity, and positive and negative predictive values of 73.9%, 94.1%, 94.4%, and 72.7%, respectively. Monoclonal antibodies are useful for direct hMPV detection
Quantification of Staphylococcus aureus cell surface adhesins using flow cytometry.
No full textThe initiation of many infectious diseases involves specific adhesion of bacteria to host tissue proteins and carbohydrates. Staphylococcus aureus is known to bind specifically to several proteins in the extracellular matrix (ECM). We report the quantification of the collagen and fibronectin adhesin densities on the staphylococcal surface using flow cytometry. Our results are in agreement with previous reports on the transcription of the respective genes and demonstrate different patterns of temporal expression for the two adhesins in the strains studied. We demonstrate a convenient technique for quantification of bacterial adhesins that can be used in studies aimed at characterization of bacterial adhesion to ECM components and understanding expression of adhesins during the course of an infection
The role of ionic interactions in the adherence of the Staphylococcus epidermidis adhesin SdrF to prosthetic material
No full texttaphylococcus epidermidis infections are common complications of prosthetic device implantation. SdrF, a surface protein, appears to play a critical role in the initial colonization step by adhering to type I collagen and DacronTM. The role of ionic interactions in S. epidermidis adherence to prosthetic material was examined. SdrF was cloned and expressed in Lactococcus lactis. The effect of pH, cation concentration, and detergents on adherence to different types of plastic surfaces was assessed by crystal violet staining and bacterial cell counting. SdrF, in contrast with controls and other S. epidermidis surface proteins, bound to hydrophobic materials such as polystyrene. Binding was an ionic interaction and was affected by surface charge of the plastic, pH, and cation concentration. Adherence of the SdrF construct was increased to positively charged plastics and was reduced by increasing concentrations of Ca(2+) and Na(+) . Binding was optimal at pH 7.4. Kinetic studies demonstrated that the SdrF B domain as well as one of the B subdomains was sufficient to mediate binding. The SdrF construct also bound more avidly to GoretexTM than the lacotococcal control. SdrF is a multifunctional protein that contributes to prosthetic devices infections by ionic, as well as specific receptor-ligand interactions
Novel Poly(urethane-aminoamides). An in vitro study of the interaction with heparin.
No full textIn order to obtain heparin-binding polyurethanes, tertiary amino-groups have been introduced in the polymer backbone by attributing a key-role to the chain extender, i.e. substituting butanediol, commonly used in polyurethane synthesis, with a tailor-made diamino-diamide-diol. In this work a poly(ether-urethane-aminoamide) (PEU/PIME/al) was obtained with poly(oxytetramethylene) glycol 2000, 1,6-hexamethylene-diisocyanate and the new chain extender, in the molar ratio 1:2:1. The heparin binding capacity of PEU/PIME/al was evaluated with 125I labelled heparin, using for comparison the analogous polymer obtained with a diamide-diol (i.e. the poly(ether-urethane-amide) PEU/PIBLO/al), and two commercially available biomedical polyurethanes (Pellethane 2363 and Corethane). pH and ionic strength dependence of the heparin uptake were investigated by treating all the polyurethanes with solutions of 125I heparin into buffers from pH 4 to 9 or NaCl molarity from 0.0 to 1.0. The stability of the interaction with bound heparin was investigated by sequential washing treatments (PBS, 1 N NaOH, 2% SDS solution), then analysing the residual radioactivity on the materials. Results indicated that the heparin binding of PEU/PIME/al is significantly higher and more stable than that of the other polyurethanes, with a time-dependent kinetic. The interaction with heparin appears to be prevalently ionic, with the contribution of other electrostatic and hydrophobic interactions. Activated partial thromboplastin time (APTT), performed on human plasma with polyurethane-coated, heparinized test tubes, indicate
MONOCLONAL ANTIBODIES THAT ARE CROSS-REACTIVE AGAINST BACTERIAL COLLAGEN BINDING PROTEINS
No full textCross-reactive monoclonal antibodies are provided which are generated from peptides from Enterococcus faecalis, including the ACE40 and the ACE19 protein, and the CNA19 peptide from Staphylococcus aureus, and which can bind to the collagen-binding proteins from bacteria and from a variety of species including enterococcal bacteria, staphylococcal bacteria and streptococcal bacteria. These monoclonal antibodies may then be formed into suitable pharmaceutical compositions, and they are thus particularly effective in providing methods of treating or preventing bacterial infections from a wide range of bacterial species
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