Isolation of soluble immune complexes from serum using protein A bearing Staphylococcus aureus bacteria: Separation of the antigen from immune complex and production of antisera

Natali, P. G.; Walker, Leslie E.; Pellegrino, Michele

doi:10.1016/0090-1229(80)90022-7

Cited by 18 publications

(3 citation statements)

References 20 publications

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“…In our initial studies, 1,500-,ug protein quantities of PEG-precipitated IC from single ICpositive donors were emulsified in 3 ml of complete Freund adjuvant, and 0.5-ml portions of each preparation were injected into each of two nuchal sites; animals were reinjected 7 and 14 days later with the same preparations. Subsequently, we mixed 500 ,ug of PEG-purified IC protein in 1 ml of PBS with an equal volume of a 10% suspension of heat-killed, Formalinfixed Staphylococcus aureus Cowan I strain followed by incubation for 2 h at 4°C (36). The coated staphylococcal suspension was washed three times in PBS and resuspended to a 10% suspension, which was used for immunization.…”

Section: Methodsmentioning

confidence: 99%

Circulating immune complexes in experimental syphilis: identification of treponemal antigens and specific antibodies to treponemal antigens in isolated complexes

Baughn¹,

Adams²,

Musher³

1983

Infect Immun

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As a prelude to characterization of the host and treponemal antigens present in purified immune complexes from the sera of rabbits with disseminated syphilis, autoradiographic and immunoenzymatic analyses of solubilized extracts of Treponema pallidum, Treponema phagedenis biotype Reiter, and Treponema refringens were performed on electroblots of polypeptides first separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Electroblots of purified immune complexes were developed with the same panel of antisera so that protein profiles could be compared. Eight treponemal antigens were consistently present in isolated complexes; four of these cross-reacted with antisera prepared against avirulent treponemes. The average molecular weights of these antigens were 87,000, 76,000, 66,000, and 45,000. Antibodies dissociated from isolated immune complexes, when used for the development of T. pallidum electroblots, reacted with four antigens of comparable molecular weight. Antibodies to those polypeptides were also present in the sera of animals immunized with immune complexes. The demonstration of treponemal antigens in purified immune complexes convincingly argues that their occurrence in experimental syphilis is not merely due to tissue destruction and responses to endogenous host antigens.

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Section: Methodsmentioning

confidence: 99%

Circulating immune complexes in experimental syphilis: identification of treponemal antigens and specific antibodies to treponemal antigens in isolated complexes

Baughn¹,

Adams²,

Musher³

1983

Infect Immun

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“…Staphylococcal protein A (SpA) produced by Staphylococcus aureus is well known for its reactivity with the Fc region of immunoglobulin G (3-6, 15,17), and is now widely used as a useful tool for immunosorbent (2,14) and other purposes in various fields of the biological sciences (1,3,4,7,9). For some experiments, a large amount of highly purified SpA is needed.…”

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confidence: 99%

A Rapid and Simple Method for the Purification of Staphylococcal Protein A from the Culture of Extracellularly Protein A‐Releasing Mutant

Seki

Nishihara

Masuda

1985

Microbiology and Immunology

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“…Each receptor type, confined either to a single or to a few bacterial species, is currently defined by a distinct binding profile when tested with a panel of immunoglobulins representing various mammalian IgG subclasses (17)(18)(19)(20). The interaction of the immunoglobulin molecule with the bacterial IgG receptor does not affect the antigen-binding capacity, and soluble immune complexes produced in vitro are effectively bound by receptor-carrying staphylococci and streptococci (3,24). Several studies have shown that staphylococcal protein A can interact with greater avidity with complexed IgG than with monomeric IgG (12,(14)(15).…”

mentioning

confidence: 99%

INTERACTION OF THERMALLY AGGREGATED HUMAN IgG WITH BACTERIA

Myhre

Kronvall²

1984

Acta Pathologica Microbiologica Scandinavica Series B: Microbio

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Ninety‐three bacterial strains, representing 16 Gram‐positive and Gram‐negative species, were tested for quantitative binding of 125I‐labelled monomeric and thermally aggregated human IgG. Aggregated IgG bound to all bacerial species studied, in contrast to monomeric IgG, which interacted only with S. aureus, group A, C and G streptococci, viz. bacteria possessing previously described IgG‐Fc receptors. A positive correlation was observed between binding of monomeric IgG and the uptake of thermally aggregated IgG (r = 0.92). Monomeric IgG inhibited effectively the binding of monomeric IgG but only partially the uptake of aggregates. Absorption with bacteria revealed that only a fraction of aggregated IgG could interact with bacteria lacking specific IgG‐Fc receptors. A human group G streptococcus strain (G‐148), tested with increasing amounts of immunoglobulin, was capable of binding at least ten times as much aggregates as monomeric IgG, implying binding to separate binding sites. These data indicate that polymeric IgG produced by thermal aggregation of human polyclonal IgG can interact with bacterial surface components found in most pathogenic microorganisms. This interaction seems to be less specific than the binding to previously described IgG‐Fc receptors.

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Isolation of soluble immune complexes from serum using protein A bearing Staphylococcus aureus bacteria: Separation of the antigen from immune complex and production of antisera

Cited by 18 publications

References 20 publications

Circulating immune complexes in experimental syphilis: identification of treponemal antigens and specific antibodies to treponemal antigens in isolated complexes

Circulating immune complexes in experimental syphilis: identification of treponemal antigens and specific antibodies to treponemal antigens in isolated complexes

A Rapid and Simple Method for the Purification of Staphylococcal Protein A from the Culture of Extracellularly Protein A‐Releasing Mutant

INTERACTION OF THERMALLY AGGREGATED HUMAN IgG WITH BACTERIA

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