Interaction of Penicillin with HLA-A and -B antigens

Claas, Frans H.J.; Nieuwkoop, Riemke Runia-van; Berge, Wendy van den; Rood, Jon J. van

doi:10.1016/0198-8859(82)90033-7

Cited by 25 publications

(8 citation statements)

References 12 publications

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“…Recent evidence suggests that antibodies to HLA can block receptors for other mediators of cell function such as insulin, glucagon, -y-endorphin, and epidermal growth factor (24). Other nonimmune functions proposed for molecules of the major histocompatibility complex (MHC) include binding of penicillin (25) and viruses (26) as well as participation in cellular adhesion and contact inhibition (27). If P2m or the HLA complex are functionally related to the TXA2 receptor, it is a new role for class I MHC molecules that will strengthen the concept that their function in cell biology is larger than that defined by their participation in immune (1-3).…”

mentioning

confidence: 99%

Inhibition of Platelet Aggregation by Monoclonal Antibody Reactive with β ₂ -Microglobulin Chain of HLA Complex

Curry

Messner

Johnson

1984

Science

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A mouse monoclonal antibody that reacts with beta 2-microglobulin, the light chain of class I major histocompatibility antigens, inhibited the second wave of human platelet aggregation induced by adenosine diphosphate and epinephrine and blocked aggregation and platelet protein phosphorylation induced by sodium arachidonate. Thrombin-induced platelet aggregation was inhibited at threshold concentrations but not at higher concentrations. The antibody also inhibited aggregation and secretion in response to thromboxane A2 or the stable endoperoxide analog, U46619. These results suggest that beta 2-microglobulin in the histocompatibility complex is intimately associated with transmission of the endoperoxide-thromboxane signal at the platelet membrane.

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mentioning

confidence: 99%

Inhibition of Platelet Aggregation by Monoclonal Antibody Reactive with β ₂ -Microglobulin Chain of HLA Complex

Curry

Messner

Johnson

1984

Science

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“…Recently, we described that antibiotics can interact with polymorphic m e m b r a n e determinants in such a way that these determinants cannot react any m o r e with their corresponcling antisera (Claas et al 1981(Claas et al , 1982. T h c present experiments show that antibiotics like penicillin and streptomycin.…”

Section: Discussionmentioning

confidence: 50%

“…

Recently we could dcmonstrate that antibiotics can interact with polymorphic membrane determinants. As a result, these determinants can no longer react with their corrcsponding antisera (Claas et al 1981(Claas et al , 1982. In the present cxpcriments it was found that allogcneic cytotoxic T cells (CTLs), which were cultured in thc prcscnce of antibiotics, induced significantly stronger lysis against the specific target than C'l".s which were cultured in the absence of antibiotics.

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confidence: 71%

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The outcome of cell mediated lympholysis is influenced by the antibiotics in the culture medium

et al. 1982

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Recently we could demonstrate that antibiotics can interact with polymorphic membrane determinants. As a result, these determinants can no longer react with their corresponding antisera (Claas et al. 1981, 1982). In the present experiments it was found that allogeneic cytotoxic T cells (CTLs), which were cultured in the presence of antibiotics, induced significantly stronger lysis against the specific target than CTLs which were cultured in the absence of antibiotics. In some cases the CML assay was only positive according to the European Workshop criteria when penicillin was added to the cultures, whereas the assay was negative in the absence of penicillin. On the other hand when CTLs were induced in an MLC culture without penicillin, lysis was higher against the target cell in the absence of penicillin than in the presence of penicillin. By adding penicillin to the effector phase, inhibition of lysis was observed. No difference in 3H-thymidine-incorporation was observed between MLC cultures with and without antibiotics. We conclude that antibiotics in the culture medium can influence the outcome of CML experiments.

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“…It is also unclear whether immunogenic neoepitopes consist of penicillin bound to MHC molecules, or to peptides associated with MHC molecules. In the latter case, two mechanisms are possible: penicillin may bind to cell surface or soluble proteins that are processed into penicillinated peptides and loaded onto MHC molecules: alternatively, penicillin may bind directly to the peptide of a preformed complex (13)(14)(15)(16)(17)(18)(19)(20). These novel mechanisms for epitope generation have provoked controversy as to whether penicillin-self protein conjugates always require processing before recognition by hapten allergen-specific T cells (13)(14)(15)(16)(17)(18)(19)(20),…”

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Allergy to antibiotics: T‐cell recognition of amoxicillin is HLA‐DR restricted and does not require antigen processing

Horton

Weston

Hewitt

1998

Allergy

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Allergic immune responses are initiated and maintained by T cells that recognize peptidic fragments of allergens in the context of major histocompatibility complex (MHC) class II molecules. An anomaly of this model exists in the T-cell response to haptens. Haptens are nonpeptide antigens that alone are too small to provoke an immune response. Nevertheless, T-cell responses to haptenic allergens clearly occur and are critically involved in allergic immune responses to drugs such as penicillin. Although the mechanisms that generate T-cell epitopes from protein antigens are well understood, haptens create T-cell epitopes by alternative mechanisms. These may include binding of haptens directly to preformed MHC-peptide complexes on the cell surface, or indirect association with MHC molecules after conjugation with self cell surface or serum proteins that are then processed and presented as haptenated peptide antigens. Which of these unorthodox mechanisms of epitope generation is dominant in allergy to penicillin is unknown. This study aims to determine the nature of the epitopes recognized by amoxicillin-specific T cells from allergic donors, and to clarify whether T-cell responses to penicillin antibiotics are MHC-restricted and require haptenated self proteins to be processed before recognition. Human T-cell lines specific for amoxicillin were raised and used in assays with processing-disabled and MHC-class II-typed antigen-presenting cells to determine the MHC restriction and processing requirements of T cells recognizing amoxicillin. Fixation of antigen-presenting cells with paraformaldehyde, before or after pulsing with amoxicillin, established that T cells can recognize amoxicillin-containing epitopes with a similar efficiency irrespective of whether the antigenic conjugate has been internalized and processed. These results suggest that amoxicillin can bind directly to performed MHC-peptide complexes and need not necessarily involve the processing of haptenated self carrier proteins before recognition of the conjugate by amoxicillin-specific T cells.

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Interaction of Penicillin with HLA-A and -B antigens

Cited by 25 publications

References 12 publications

Inhibition of Platelet Aggregation by Monoclonal Antibody Reactive with β ₂ -Microglobulin Chain of HLA Complex

Inhibition of Platelet Aggregation by Monoclonal Antibody Reactive with β ₂ -Microglobulin Chain of HLA Complex

The outcome of cell mediated lympholysis is influenced by the antibiotics in the culture medium

Allergy to antibiotics: T‐cell recognition of amoxicillin is HLA‐DR restricted and does not require antigen processing

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Interaction of Penicillin with HLA-A and -B antigens

Cited by 25 publications

References 12 publications

Inhibition of Platelet Aggregation by Monoclonal Antibody Reactive with β 2 -Microglobulin Chain of HLA Complex

Inhibition of Platelet Aggregation by Monoclonal Antibody Reactive with β 2 -Microglobulin Chain of HLA Complex

The outcome of cell mediated lympholysis is influenced by the antibiotics in the culture medium

Allergy to antibiotics: T‐cell recognition of amoxicillin is HLA‐DR restricted and does not require antigen processing

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Inhibition of Platelet Aggregation by Monoclonal Antibody Reactive with β ₂ -Microglobulin Chain of HLA Complex

Inhibition of Platelet Aggregation by Monoclonal Antibody Reactive with β ₂ -Microglobulin Chain of HLA Complex