Other search tools

About this data

The publication data currently available has been vetted by Vanderbilt faculty, staff, administrators and trainees. The data itself is retrieved directly from NCBI's PubMed and is automatically updated on a weekly basis to ensure accuracy and completeness.

If you have any questions or comments, please contact us.

Results: 1 to 9 of 9

Publication Record

Connections

Staphylococcus aureus protein A enhances osteoclastogenesis via TNFR1 and EGFR signaling.
Mendoza Bertelli A, Delpino MV, Lattar S, Giai C, Llana MN, Sanjuan N, Cassat JE, Sordelli D, Gómez MI
(2016) Biochim Biophys Acta 1862: 1975-83
MeSH Terms: Animals, Cell Differentiation, ErbB Receptors, Humans, Mice, Mice, Inbred BALB C, Mice, Knockout, Osteoclasts, Osteomyelitis, RANK Ligand, Receptors, Tumor Necrosis Factor, Type I, Staphylococcal Infections, Staphylococcal Protein A, Staphylococcus aureus, Tumor Necrosis Factor-alpha
Added April 3, 2018
0 Communities
1 Members
0 Resources
15 MeSH Terms
The human polymeric immunoglobulin receptor facilitates invasion of epithelial cells by Streptococcus pneumoniae in a strain-specific and cell type-specific manner.
Brock SC, McGraw PA, Wright PF, Crowe JE
(2002) Infect Immun 70: 5091-5
MeSH Terms: Cell Line, Epithelial Cells, Humans, Pneumococcal Infections, Receptors, Polymeric Immunoglobulin, Species Specificity, Staphylococcal Protein A, Streptococcus pneumoniae
Show Abstract · Added August 6, 2012
Streptococcus pneumoniae is a gram-positive bacterial pathogen that causes invasive life-threatening disease worldwide. This organism also commonly colonizes the upper respiratory epithelium in an asymptomatic fashion. To invade, this pathogen must traverse the respiratory epithelial barrier, allowing it to cause disease locally or disseminate hematogenously throughout the body. Previous work has demonstrated that S. pneumoniae choline-binding protein A, a pneumococcal surface protein, interacts specifically with the human polymeric immunoglobulin receptor, which is expressed by cells in the respiratory epithelium. Choline-binding protein A is required for efficient colonization of the nasopharynx in vivo. Additionally, a recent study showed that the R6x laboratory strain of S. pneumoniae invades a human pharyngeal cell line in a human polymeric immunoglobulin receptor-dependent manner. These findings raised the possibility that the interaction between choline-binding protein A and human polymeric immunoglobulin receptor may be a key determinant of S. pneumoniae pathogenesis. However, the strain used in prior invasion studies, R6x, is an unencapsulated, nonpathogenic strain. In the present study we determined the relative ability of strain R6x or pathogenic strains to invade a variety of human polymeric immunoglobulin receptor-expressing epithelial cell lines. The results of this work suggest that human polymeric immunoglobulin receptor-dependent enhanced invasion of epithelial cells by S. pneumoniae is a limited phenomenon that occurs in a strain-specific and cell type-specific manner.
0 Communities
1 Members
0 Resources
8 MeSH Terms
A functional fibroblast growth factor-1 immunoglobulin fusion protein.
Dikov MM, Reich MB, Dworkin L, Thomas JW, Miller GG
(1998) J Biol Chem 273: 15811-7
MeSH Terms: 3T3 Cells, Animals, Antibodies, Anti-Idiotypic, DNA Replication, Diphtheria Toxin, Fibroblast Growth Factor 1, Flow Cytometry, Heparin, Humans, Immunoglobulin Fc Fragments, Jurkat Cells, Mice, Peptide Fragments, Phosphorylation, Receptor Protein-Tyrosine Kinases, Receptor, Fibroblast Growth Factor, Type 1, Receptors, Fibroblast Growth Factor, Recombinant Fusion Proteins, Staphylococcal Protein A, T-Lymphocytes, Tyrosine
Show Abstract · Added November 6, 2013
Proteins of the fibroblast growth factor (FGF) family play diverse roles in embryonic development, angiogenesis, and wound healing. The most well studied targets of FGF activity typically are cells of mesodermal and neuroectodermal origin; in addition, expression of FGF-1 (acidic FGF) is increased at several sites of chronic immunologic injury, and recent studies show that FGF-1 also may interact with cells of the immune system. In some human T cells, FGF-1 can induce signals necessary for production of interleukin-2, a key cytokine required for T cell proliferation. To better characterize the interaction of FGF-1 with FGF receptors on T cells, a fusion protein was constructed containing a portion of the constant region of human IgG1 (Fc) at the amino terminus of FGF-1. The Fc-FGF-1 fusion protein retained FGF function as determined by stimulation of tyrosine phosphorylation and DNA synthesis in NIH 3T3 cells. Binding of the intact fusion protein to FGF receptor 1 (FGFR1) on T cells was demonstrated by immunoprecipitation of the receptor bound to Fc-FGF-1 and by flow cytometry showing binding of fusion protein to T cells expressing FGFR1. This functional Fc-FGF-1 protein should prove useful in identifying FGFR-expressing cells.
1 Communities
1 Members
0 Resources
21 MeSH Terms
Goodpasture syndrome: selective removal of anti-alpha 3 (IV) collagen autoantibodies. A potential therapeutic alternative to plasmapheresis.
Boutaud AA, Kalluri R, Kahsai TZ, Noelken ME, Hudson BG
(1996) Exp Nephrol 4: 205-12
MeSH Terms: Adsorption, Animals, Anti-Glomerular Basement Membrane Disease, Autoantibodies, Blotting, Western, Cattle, Chromatography, Affinity, Collagen, Electrophoresis, Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Humans, Immunoglobulin G, Kidney Glomerulus, Plasmapheresis, Recombinant Proteins, Staphylococcal Protein A
Show Abstract · Added December 10, 2013
Anti-alpha 3(IV) collagen autoantibodies have been implicated in the pathogenesis of Goodpasture syndrome, an autoimmune disorder causing glomerulonephritis and pulmonary hemorrhage. Currently treatment involves removal of the entire IgG fraction of plasma by plasmapheresis or adsorption to protein A. The present study shows that the anti-alpha 3(IV)NC1 autoantibodies can be removed from plasma specifically and quantitatively by affinity chromatography utilizing either alpha 3 NC1 domain of bovine type IV collagen or recombinant alpha 3 NC1 domain of human type IV collagen immobilized to agarose beads. This study shows the feasibility of using affinity chromatography, as an alternative to plasmapheresis, to exclusively remove the pathogenic autoantibodies from the plasma of patients with Goodpasture syndrome.
1 Communities
1 Members
0 Resources
16 MeSH Terms
Serological, functional, and immunochemical characterization of a monoclonal antibody (MoAb Q2/70) to human Ia-like antigens.
Quaranta V, Indiveri F, Glassy MC, Ng A, Russo C, Molinaro GA, Pellegrino MA, Ferrone S
(1980) Hum Immunol 1: 211-23
MeSH Terms: Animals, Antibodies, Antibodies, Anti-Idiotypic, Antibodies, Monoclonal, Binding Sites, Antibody, Cattle, Cell Separation, Complement System Proteins, Cytotoxicity, Immunologic, Electrophoresis, Polyacrylamide Gel, Goats, Guinea Pigs, Haplorhini, Histocompatibility Antigens Class II, Humans, Macromolecular Substances, Mice, Puromycin, Rabbits, Rats, Rosette Formation, Sheep, Staphylococcal Protein A, Tunicamycin
Show Abstract · Added March 27, 2014
Serological and immunochemical studies showed that monoclonal antibody Q2/70 (MoAb Q2/70), produced by the hybridoma technique, is specific for human Ia-like antigens. This antibody recognizes an antigenic determinant which is different from those defining the serologic polymorphism of Ia-like antigens, and is expressed on subsets of human Ia-like molecules and on lymphoid cells from other species. MoAb Q2/70 inhibits unidirectional MLRs* between allogenic human lymphocytes, but not between murine and human lymphocytes. In ADCC* assays. MoAb Q2/70 mediates lysis of cultured human B lymphoid cells RPMI 4098, effected by murine splenocytes. The antibody is suitable to isolate immunologically functional B lymphocytes from human peripheral blood.
1 Communities
1 Members
0 Resources
24 MeSH Terms
Extracorporeal removal of anti-HLA antibodies in transplant candidates.
Hakim RM, Milford E, Himmelfarb J, Wingard R, Lazarus JM, Watt RM
(1990) Am J Kidney Dis 16: 423-31
MeSH Terms: Adult, Female, HLA Antigens, Histocompatibility Testing, Humans, Immunoglobulin G, Immunosorbent Techniques, Kidney Failure, Chronic, Kidney Transplantation, Male, Plasmapheresis, Renal Dialysis, Staphylococcal Protein A
Show Abstract · Added May 20, 2014
We report on the results of a clinical trial in which 14 transplant candidates were treated with an extracorporeal immunoadsorption system using Protein A that selectively removes immunoglobulin from plasma; we also assessed the dynamics of anti-HLA antibody as a model of IgG removal and re-equilibration, as well as the clinical safety of the procedure. At the end of a treatment course, plasma IgG levels were reduced by 90% +/- 8% of control values (P less than 0.01). In contrast, albumin levels were reduced by only 15% (P less than 0.05). Specific cytotoxic anti-HLA antibody titers were reduced by approximately 18-fold. Panel reactivity was measured as the proportion of a 40-member cell donor panel killed by patients' serum in the presence of complement; in nine of the 14 patients, there was a significant reduction in this parameter (range, 23% to 87%). During the 4-week follow-up period, anti-HLA antibody titers returned to baseline levels. There were no remarkable changes observed in blood chemistries, nor were there any unanticipated adverse reactions seen in the patients treated. We conclude that selective extracorporeal immunoadsorption is a safe and effective way of removing IgG-type antibodies, with potential application to reduction of HLA antibodies in transplant candidates.
0 Communities
1 Members
0 Resources
13 MeSH Terms
An IgG inhibitor against coagulation factor XIII: resolution of bleeding after plasma immunoadsorption with staphylococcal protein A.
Gailani D
(1992) Am J Med 92: 110-2
MeSH Terms: Aged, Factor XIII, Gastrointestinal Hemorrhage, Humans, Immunoglobulin G, Immunosorbent Techniques, Male, Rectal Diseases, Staphylococcal Protein A
Added May 19, 2014
0 Communities
1 Members
0 Resources
9 MeSH Terms
Staphylococci-induced human platelet injury mediated by protein A and immunoglobulin G Fc fragment receptor.
Hawiger J, Steckley S, Hammond D, Cheng C, Timmons S, Glick AD, Des Prez RM
(1979) J Clin Invest 64: 931-7
MeSH Terms: Binding Sites, Binding, Competitive, Blood Platelets, Humans, Immunoglobulin Fc Fragments, Immunoglobulin G, Platelet Aggregation, Staphylococcal Protein A, Staphylococcus aureus
Show Abstract · Added December 10, 2013
Bloodstream infections with staphylococci are accompanied by thromboembolic complications. We have studied the mechanism of the interaction of staphylococci with human blood platelets. Staphylococci that possess protein A, a bacterial receptor for the Fc fragment of immunoglobulin G (IgG), caused aggregation of human platelets in whole plasma accompanied by release of [(3)H]serotonin. These reactions were time and concentration dependent, requiring two or more staphylococci per platelet to give maximal response within 5 min. The interaction between staphylococci and platelets required the presence of cell wall-bound protein A and of IgG with an intact Fc fragment. It did not require an intact complement system. Cell wall-bound protein A (solid phase) was capable of aggregating human platelets in whole plasma. In contrast, free, solubilized protein A (fluid phase) did not cause measurable aggregation, and release of [(3)H]serotonin was reduced. An excess of free, solubilized protein A blocked aggregation of human platelets induced by staphylococci in whole plasma. The role of the Fc fragment of IgG in the staphylococci-human platelet interaction was demonstrated by an experiment in which free, isolated Fc fragment blocked aggregation of platelets in whole plasma induced by staphylococci. Furthermore, binding of (125)I-protein A to human platelets was demonstrated in the presence of complete IgG with intact Fc fragment but not in the presence of the F(ab)(2) fragment. Binding of the protein A-IgG complex to the human platelet Fc receptor was paralleled by the release of [(3)H]serotonin. These results represent a novel example of the interaction of two phylogenetically different Fc receptors, one on prokaryotic staphylococci and the other on human platelets. Their common ligand, IgG, is amplified by one Fc receptor (protein A) to react with another Fc receptor present on human platelets, which results in membrane-mediated aggregation and release reaction occurring in whole plasma. This mechanism can be of significance in the pathomechanism of thromboembolic complications at the site(s) of intravascular staphylococcal infection.
0 Communities
1 Members
0 Resources
9 MeSH Terms
A radioimmunometric antibody-binding assay for evaluation of xenoantisera to melanoma-associated antigens.
McCabe RP, Quaranta V, Frugis L, Ferrone S, Reisfeld RA
(1979) J Natl Cancer Inst 62: 455-63
MeSH Terms: Animals, Antibodies, Neoplasm, Antibody Specificity, Antigens, Neoplasm, Cell Line, Cytotoxicity Tests, Immunologic, Humans, Immunoglobulin G, Male, Melanoma, Neoplasms, Experimental, Rabbits, Radioimmunoassay, Staphylococcal Protein A
Show Abstract · Added March 27, 2014
A radioimmunometric antibody-binding assay was developed with the use of 125I-labeled protein A of Staphylococcus aureus (SpA) for the evaluation of xenoantisera to human melanoma-associated antigens. Antisera were produced in New Zealand male albino rabbits by the injection of cultured human melanoma cells or soluble, partially purified melanoma-associated antigens isolated from these cells. Xenoantisera were rendered operationally specific for melanoma-associated antigens by absorption with human red cells and cultured lymphoblasts. The methodologic parameters and the quantitative relationships among xenoantisera, cultured melanoma target cells, and 125I-labeled SpA and their effect on the measurement of xenoantibody binding were critically evaluated. Data indicated the usefulness of the radioimmunometric assay in monitoring the efficacy of absorption and in characterizing the specificity of xenoantisera to melanoma-associated antigens. The radioimmunometric binding assay when modified and used as a binding inhibition assay was effective in the assessment of the serologic activity of soluble melanoma-associated antigens and thus may be used to monitor the progress of antigen purification.
1 Communities
1 Members
0 Resources
14 MeSH Terms