1980
DOI: 10.1111/j.1365-3083.1980.tb00037.x
|View full text |Cite
|
Sign up to set email alerts
|

Interaction of Human Polyclonal IgE and IgG from Different Species with Protein A from Staphylococcus aureus: Demonstration of Protein‐A‐reactive Sites Located in the Fab2 Fragment of Human IgG

Abstract: The peptic fragments F(ab')2 and Fc" of human polyclonal IgE were tested by the SpA-IgE radioimmunoassay for interaction with protein A from Staphylococcus aureus. The Fab'2 epsilon fragment but not the Fc" epsilon fragment retained the ability to react with protein A. IgG preparations from different species were tested for ther capacity to inhibit the reaction between 125I-IgE and protein A. IgG preparations from man and the dog, pig, guinea-pig and rhesus monkey were all potent inhibitors whereas those from … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

6
66
0
1

Year Published

1985
1985
2016
2016

Publication Types

Select...
6
2

Relationship

0
8

Authors

Journals

citations
Cited by 119 publications
(73 citation statements)
references
References 31 publications
6
66
0
1
Order By: Relevance
“…ϩ had no effect. This suggests that protein A's releasing activity depends on binding to an Ig structure located in the V H 3 domain, a fragment common to all Ig classes and subclasses (23,25,52,56). The releasing activity of protein L-containing bacteria, such as P. magnus strain 312, and soluble protein L appears to be mediated by interaction with IgE present on HHMC.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…ϩ had no effect. This suggests that protein A's releasing activity depends on binding to an Ig structure located in the V H 3 domain, a fragment common to all Ig classes and subclasses (23,25,52,56). The releasing activity of protein L-containing bacteria, such as P. magnus strain 312, and soluble protein L appears to be mediated by interaction with IgE present on HHMC.…”
Section: Discussionmentioning
confidence: 99%
“…We first studied the effect on protein A-induced HHMC activation of molecules that show only Fc␥-protein A reactivity, such as RIgG, and those with both Fc␥ and F(abЈ) 2 reactivity, such as HIgG (23,52). HIgG dose dependently inhibited protein A-induced histamine release, whereas RIgG, which does not bind the alternative site of protein A (25), had no such effect (Fig. 4A).…”
Section: Effect Of S Aureus Cowan 1 and Wood 46 And Of Protein A Onmentioning
confidence: 95%
“…SAC appears to be a particularly potent stimulator of RF production. While it is assumed that SAC has a direct effect on responsive lymphocytes, the mechanism of action may be related to an interaction between SAC and the F(ab')* and/or the Fc portion of IgG (13,14), either on the surfaces of the B cells or in the culture supernatant after IgG secretion. Theoretically, it is possible that this interaction mod-ifies the IgG molecule in such a way that it more readily stimulates RF response.…”
Section: Discussionmentioning
confidence: 99%
“…As a consequence of the availability of commercial tests, these studies were restricted to five classical enterotoxins: SEA to SED and TSST-1. Furthermore, the immunological methods used thus far are known to be limited in sensitivity and specificity (6,16,32). To date, no valid data are available concerning the prevalence of the more recently described enterotoxins in S. aureus isolates derived from clinical specimens.…”
mentioning
confidence: 99%