Protein A of Staphylococcus uureus and Related lrnmunog lobul in Receptors Produced by Streptococci and Pneumonococci

Iangone, John J.

doi:10.1016/s0065-2776(08)60722-1

Cited by 500 publications

(209 citation statements)

References 301 publications

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“…Proteins A (soluble extracellular from Staphylococcus aureus, Fluka, Buchs, Switzerland) are globular proteins of 44.2 kDa. They have an average diameter of 3 nm [7] and their isoelectrical point is pI =5.1 [8]. We diluted them in nanodeionized water, which has been stocked under air conditions, so that due to the CO 2 absorption, the water pH was comprised between 5 and 6, near the pI of protein A.…”

Section: Proteinsmentioning

confidence: 99%

Creation of nanostructures to study the topographical dependency of protein adsorption

Galli

Coen

Hauert

et al. 2002

Colloids and Surfaces B: Biointerfaces

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Nanostructures of sizes comparable to protein dimensions are created on Si and Ti surfaces by local anodic oxidation (LAO) using the atomic force microscope (AFM). The characterization of the surface by X-ray photoelectron spectroscopy (XPS) reveals that this method assures a modification of the topography of the surface without a change of its chemical composition. Surfaces structured by LAO therefore represent ideal systems to study the dependence of protein adsorption on topography. We are able to visualize the created nanostructures with an AFM and successively adsorb the proteins in situ, rinse and image the new surface. The densities of adsorbed proteins on the nanostructured and neat surfaces are compared and we find that the protein arrangement depends on the underlying nanostructures, showing that proteins can ''sense'' the topography of surfaces at the nanometer scale. This result can be considered as the nanoscale analogous of the adsorption found for cell systems on micrometer structures.

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Section: Proteinsmentioning

confidence: 99%

Creation of nanostructures to study the topographical dependency of protein adsorption

Galli

Coen

Hauert

et al. 2002

Colloids and Surfaces B: Biointerfaces

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“…Langone reported that protein A might play a role in the pathogenesis of S. aureus (17), although the virulence of protein A was ambiguous (15,16,20). The biological roles of protein A in the antiphagocytotic activity and pathogenesis remained to be clarified in further investigations.…”

Section: Comparison Of the CL Responses To Opsonized S Aureus Strainsmentioning

confidence: 99%

Chemiluminescence Response of Human Phagocytes against IgG‐Opsonized Staphylococci with and without Protein A Activities

Yamada

1990

Microbiology and Immunology

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The effects of immunological IgG binding to Staphylococcus aureus and IgG binding via protein A on the chemiluminescence (CL) response of human phagocytes were examined. The results obtained by enzyme immunoassay showed a clear correlation between the magnitude of the CL response and amount of IgG on protein A-deficient HL-87 strain. Despite no difference in protein A activity between 209P and Cowan I strains, the CL response to IgG-opsonized 209P cells was lower than that to Cowan I cells similarly opsonized. Moreover, the CL response to opsonized HL-87 cells was identical with that of opsonized Cowan I cells, which was a protein A-rich parent strain of the HL-87. The protein A activity of Cowan I cells was significantly decreased when the cells were treated with the Fc fraction of IgG before opsonization, but such a treatment did not change the phagocytic CL response. These results strongly suggest that IgG bound to protein A via its Fc portion has no efkct on the phagocytic CL response and that IgG immunologically bound to S. aureus is responsible for the opsonization of the bacteria.

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“…Protein A is a cell-wall-associated protein of the Gram-positive pathogenic bacterium Staphylococcus aureus (for reviews see Langone, 1982;Fosgren et al, 1983). Five repeated domains which bind immunoglobulin molecules at a site on the Fc region protrude from the cell surface (Lofdahl et al, 1983;Uhlkn et al, 1984).…”

Section: Introductionmentioning

confidence: 99%

Physical and Genetic Mapping of the Protein A Gene in the Chromosome of Staphylococcus aureus 8325-4

Patel

Foster²,

Pattee³

1989

Microbiology

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The gene coding for protein A (spa) has been mapped close to nov on the genetic map of the chromosome of Staphylococcus aureus 8 325-4. A rapid mapping procedure has been developed which first allowed the region of the chromosome carrying the spa gene to be identified by blot hybridization of large DNA fragments which had been separated by pulsed-field gel electrophoresis. Restriction endonuclease SmaI fragment G was shown to carry the spa gene. An insertion mutation in spa was constructed by in vitro insertion of a fragment of DNA expressing resistance to kanamycin and neomycin. A spa : :KanrNeof mutation was isolated in S. aureus 8325-4 by allele replacement. This provided a selectable marker which allowed the spa gene to be mapped by transformation analysis.

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Protein A of Staphylococcus uureus and Related lrnmunog lobul in Receptors Produced by Streptococci and Pneumonococci

Cited by 500 publications

References 301 publications

Creation of nanostructures to study the topographical dependency of protein adsorption

Creation of nanostructures to study the topographical dependency of protein adsorption

Chemiluminescence Response of Human Phagocytes against IgG‐Opsonized Staphylococci with and without Protein A Activities

Physical and Genetic Mapping of the Protein A Gene in the Chromosome of Staphylococcus aureus 8325-4

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