Preparations of Purified Antigens from Staphylococcus Aureus in Biologic and Serologic Experiments

Löfkvist, Thorvald

doi:10.1159/000229700

Cited by 7 publications

(4 citation statements)

References 15 publications

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“…In addition, such sera also yielded positive results in the PHT, their titers ranging up to 1: 81,920. On the other hand, as reported by others (4,20), individual sera from rabbits, including those used for immunization, were completely negative to protein A in the ADT. The same was true with respect to the PHT.…”

Section: Resultssupporting

confidence: 76%

Serological Activity of Protein A ofStaphylococcus aureus:the Precipitinogen as an Antigen for Determining Antibodies by the Passive Hemagglutination Test

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Ranu

1968

J Bacteriol

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Tanned sheep erythrocytes have been considered incapable of sensitization with the precipitinogen of protein A of Staphylococcus aureus, so that the activity of this antigen in serological reactions has so far been studied by means of the agar diffusion test (ADT) only. The precipitinogen of the protein A in this study was found to become attached to the tanned erythrocytes and to sensitize them for the passive hemagglutination test (PHT). It was determined that, in contrast to nonspecific reactivity between normal human serum and the precipitinogen in the ADT, the reaction in the PHT was of specific nature. Of seven species studied, all normal human, dog, and hog sera tested were positive in the PHT. However, the hemagglutinin titers of the sera of the two animal species by far exceeded those of the human sera. The data emphasized the usefulness of the highly sensitive PHT for assaying antibodies to protein A.

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Section: Resultssupporting

confidence: 76%

Serological Activity of Protein A ofStaphylococcus aureus:the Precipitinogen as an Antigen for Determining Antibodies by the Passive Hemagglutination Test

Live

Ranu

1968

J Bacteriol

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Section: Discussionmentioning

confidence: 99%

“…In addition the tissue reactions could not be related to histamine or histamine like compounds in the challenging staphylococcal material used [ 18-231 . Jensen [24] and later L6fkvist [25] found that an extracted product from S. aureus, antigen A, contracted normal guinea pig ileum. Liifkvist and Sjoquist showed that this antigen preparation contained a protein [26] which was called protein A. Lofkvist suggested [25] that protein A may have been the active agent in the preparations of Dworetzky et al [20-231. The anaphylatic reactions in non-immunized guinea pigs [2] and the Arthus reaction in rabbits [3] elicited by protein A are believed to to depend on conformational changes of IgG resulting from the reaction of the Fc portion with protein A.…”

Section: Discussionmentioning

confidence: 99%

Protein A from Staphylococcus aureus complement fixation by aggregates between protein A and IgG1 or IgG2 from guinea pig

Stålenheim

Malmheden-Eriksson

1971

FEBS Letters

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“…Protein A from Staphylococctis aureus reacts myeloma protein (3) to acid has been shown with normal human IgG (U) and with IgG to render the region between CH2 and CH3 from a number of animal species (7,10,16, susceptible to proteolysis. In the latter case, 18,20). This interaction is not with the an-trypsin was used in the isolation of distinct tigen-binding sites of the Fab regions but with components corresponding antigenically to the the Fc regions of the IgG molecules (5-8, 10, CH2 and CH3 regions, and the CH2 fragment [13][14][15].…”

mentioning

confidence: 99%

Tryptic Fragments of Fc from Normal Human IgG and their Interaction with Staphylococcal Protein A

1974

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Tryptic digests of acid‐treated Fc from normal human IgG were separated into four peaks (I to IV) by gel filtration on Sephadex G‐100. Essentially all the material from peak I reacted with staphylococcal protein A. had a molecular weight (MW) of approximately 55,000, and was indistinguishable from intact Fc on electrophoresis and immunodiffusion. Peaks II and III, MW 42,000 and 32,000. respectively, contained both protein A‐reactive and protein A‐nonreactive material, whereas peak IV. MW 12,000, showed no reaction with protein A The protein A‐reactive material from peaks II and III had an intact Fc chain bound to another peptide, from which a part of the C‐terminal sequence had been removed. The protein A‐nonreactive material from peaks II and III lacked antigenic determinant(s) compared to intact Fc and gave fragments with MWs of 16.000 and 18,000. respectively, after reduction, suggesting that these fragments consist of Fc N‐terminal sequences joined by disulfide bonds. It is concluded that, in contrast to interchain interaction, intrachain interactions influence protein A activity.

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Preparations of Purified Antigens from Staphylococcus Aureus in Biologic and Serologic Experiments

Cited by 7 publications

References 15 publications

Serological Activity of Protein A ofStaphylococcus aureus:the Precipitinogen as an Antigen for Determining Antibodies by the Passive Hemagglutination Test

Serological Activity of Protein A ofStaphylococcus aureus:the Precipitinogen as an Antigen for Determining Antibodies by the Passive Hemagglutination Test

Protein A from Staphylococcus aureus complement fixation by aggregates between protein A and IgG1 or IgG2 from guinea pig

Tryptic Fragments of Fc from Normal Human IgG and their Interaction with Staphylococcal Protein A

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