Biomedical subjects

G Delespesse

Publications and source records attributed to G Delespesse.

At least 73 records · Page 4Linked to original sources

PubMed1987

In vitro production of IgE-binding factors by human mononuclear cells.

This study documents the production of IgE-binding factors (IgE-BFs) by unstimulated and by mitogen-activated human mononuclear cells. IgE-BFs were detected by a sensitive radioimmunoassay employing monoclonal antibodies to lymphocyte Fc epsilon R (MabER). IgE-BFs were found in the 24-hr CSN of unfractionated tonsillar lymphocytes and of their B-cell but not of their T-cell enriched fractions. When cultured for 1 week, PBMC spontaneously synthesized and released IgE-BFs in the CSN; this was significantly reduced by IgE (10 micrograms/ml). PWM, PHA and Con A significantly increased the production of IgE-BFs by PBMC, and this was not influenced by IgE. The production of IgE-BFs in response to mitogens required interactions between T and non-T cells, and IgE-BFs seemed to be derived mainly from non-T cells. However, low levels of IgE-BFs could be detected in the CSN of highly purified T cells cultured for 1 week in the presence of PHA. The production of IgE-BFs by non-T cells was T-cell dependent and it was mediated by soluble factors released from mitogen-activated T cells. T-cell factors increased the secretion of IgE-BFs by: the macrophage cell line U937, adherent cells, and adherent cell-depleted B-cell preparations. It is concluded that the majority of IgE-BFs produced by cultured human mononuclear cells are derived from B cells and monocytes, and that their production is regulated by T lymphocytes.

B-Lymphocytes↗

PubMed1987

Purification and partial biochemical characterization of IgE-binding factors secreted by a human B lymphoblastoid cell line.

IgE-binding factors (IgE-BFs) were purified from the culture supernatant of RPMI-8866 cells, a human lymphoblastoid B-cell line expressing IgE receptors. The material, purified by affinity-chromatography on immunoadsorbents coupled to IgE or to monoclonal antibody against IgE receptor, was comprised of two major components with apparent molecular weight (MW) of 25,000-27,000 and 12,000, as determined by SDS-PAGE and silver staining. Only the 25,000-27,000 MW molecules were identified as IgE-BFs, as demonstrated by their reactivity with MabER in the Western blot and the immunoprecipitation assays, and their ability to inhibit rosette formation of U937 cells with IgE- but not with IgG-coated erythrocytes. IgE-BFs were purified to homogeneity by combining affinity-chromatography and either DEAE-ion exchange or reverse-phase chromatography on an HPLC system. Chromatofocusing analysis demonstrated the microheterogeneity of IgE-BFs that were comprised of molecules with isoelectric points ranging from 5.0 to 4.4. IgE-BFs were sensitive to treatment with O-glycosidase but not with N-glycanase. These molecules were resistant to heat and to pH ranging from 2 to 9; their immunoreactivity was lost after treatment with trypsin and pepsin. Papain digestion of purified IgE-BFs generated 14,000-16,000 MW molecules that were still binding to IgE and to MabER.

B-Lymphocytes↗

PubMed1986

Production and characterization of a monoclonal antibody to biotin.

Monoclonal antibodies to biotin have been prepared by using biotin linked to keyhole limpet haemocyanin (KLH) as the antigen. Spleen cells obtained from mice immunized with biotin-KLH were fused with the myeloma cell line NS-1. The resulting hybridomas were screened for the production of antibodies to biotin using an enzyme-linked immunosorbent assay. Clones producing antibodies to biotin were isolated by limiting dilution methods. Four cell lines, each derived originally from a different fusion, were chosen for the production of monoclonal antibodies. The monoclonal antibodies obtained have been characterized with respect to their ability to interact with biotin, biotin-bovine serum albumin, biotin-KLH and biocytin as well as to inhibit biotin-dependent enzymes. They have been used to produce cellular biotin deficiency in vitro for studies of biotin function.

Animals↗

PubMed1986

Production and characterization of rabbit anti-idiotypic antibodies specific to mouse monoclonal anti-human IgE and reacting with IgE-binding factors and lymphocyte receptors for IgE.

A mouse monoclonal antibody specific to human IgE (mAb 75) was employed to immunize a rabbit to obtain anti-idiotypes (aId) bearing the internal image of human IgE determinants and reacting with IgE-binding factors (IgE-BF) and/or lymphocyte receptors for IgE (Fc epsilon R). mAb 75 was selected on the basis of inhibition assays where the binding of mAb 75 to radiolabeled IgE was blocked by IgE-BF. The latter were produced by a lymphoblastoid cell line (RPMI 8866) expressing Fc epsilon R. Sequential samples of rabbit serum, collected during the immunization period, were extensively absorbed on mouse and human Ig-Sepharose 4B. The IgG fractions of the rabbit serum displayed the following activities: (a) they reacted with 125I-labeled mAb 75 but not with other labeled mouse Ig including mAb-aIgE, (b) this binding was inhibited in a dose-dependent fashion by human IgE but not by other human Ig classes nor by heat-inactivated IgE, (c) they reacted with a polyclonal rabbit anti-human IgE and (d) they blocked the binding of 125I-labeled IgE to mAb 75. It was concluded that the rabbit IgG contained aId (RaId) bearing the internal image of heat labile determinants of human IgE. The rosetting of IgE-coated bovine erythrocytes with Fc epsilon R-bearing cells was inhibited by preincubating the receptor-bearing cells with IgG RaId or its F(ab')2 but not with normal rabbit IgG. The ability of RaId to react with IgE-BF as well as with Fc epsilon R was also shown in inhibition experiments where IgE-BF and solubilized Fc epsilon R blocked the binding of mAb 75 to RaId. Finally, Western blot analysis of human colostrum, known to contain IgE-BF, indicated that radioiodinated RaId and IgE identified the same 12-16-kDa molecules corresponding to IgE-BF. It is concluded that RaId expresses the internal image of a heat-labile determinant of IgE which is involved in the binding of IgE to IgE-BF and Fc epsilon R. An alternative interpretation is that RaId reacts with an idiotypic determinant of mAb 75 which is shared by IgE-BF and Fc epsilon R.

Animals↗

PubMed1986

IgE receptors on human lymphocytes. I. Identification of the molecules binding to monoclonal anti-Fc epsilon receptor antibodies.

The present study indicates that the surface molecules from Fc epsilon receptor-bearing human lymphoblastoid cells binding to monoclonal antibodies to Fc epsilon receptor (mAbER) are identical to those binding to IgE. mAbER identify three components in the Nonidet-P40 cell lysate of surface-iodinated RPMI 8866 cells with approximately 65-95 kDa, 45 kDa and 37 kDa as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions and autoradiography. The same pattern is observed under nonreducing conditions, except for the low mol. wt component which displays an apparent molecular mass 31 kDa. When the labeled and solubilized membranes are adsorbed on IgE-Sepharose the 45-kDa component is always found in the eluate, whereas the 65-95-kDa component is occasionally detected and the low mol. wt component is rarely found. The binding of these molecules to IgE-Sepharose is inhibited by soluble IgE, mAbER but not by an unrelated mAb; reciprocally, the binding to mAbER-Sepharose is prevented by mAbER and to some extent by IgE. To improve the stability of IgE-Fc epsilon R complexes, biotinylated IgE was cross-linked on surface iodinated intact cells, which were then solubilized and adsorbed on avidin-Sepharose. Under these conditions, it was clearly shown that IgE binds to the same three surface molecules as mAbER. The isoelectric point of the high mol. wt component ranged from 4.2 to 4.4 as compared to 5.1-5.2 for the 45-kDa and the 37-kDa components. The observation in the Western blot assay that both the 65-95-kDa and the 45-kDa molecules react with 9 different mAbER indicates that these molecules have a polypeptide sequence in common.

Antibodies, Monoclonal↗

PubMed1986

IgE receptors on human lymphocytes. II. Detection of cells bearing IgE receptors in unstimulated mononuclear cells by means of a monoclonal antibody.

A monoclonal antibody (mAb) specific for lymphocyte IgE receptors (ER) was employed in a rosette assay for the detection of cells bearing IgE receptors (Fc epsilon R). The specificity of the assay was documented by inhibition studies with soluble immunoglobulins (Ig) and anti-Ig antibodies. Moreover, similar results were obtained by employing the F(ab')2 fragment of mAbER instead of intact molecule. Circulating mononuclear cells isolated from normal or allergic adults and from umbilical cord blood contained approximately 8% of Fc epsilon R-bearing cells with values ranging from 0.3 to 17%. Tonsillar lymphocytes contained about 30% of Fc epsilon R+ cells. After the removal of adherent cells, there was a small but significant reduction of the proportion of Fc epsilon R+ cells. When mononuclear cells were separated into T and B cell fractions by two-cycle rosetting with 2-aminoethylisothiouronium bromide hydrobromide-treated sheep red blood cells, most of the Fc epsilon R+ cells were in the B cell fraction; however, a small proportion of Fc epsilon R+ was also found in the enriched T cells and double-labeling experiments confirmed that these cells were indeed T lymphocytes. Fc epsilon R+ cells were purified by rosetting with mAbER-coated erythrocytes and their phenotype was compared to that of Fc epsilon R- cells; Fc epsilon R+ cells contained about 90% of B cells (B1+) together with a small proportion of OKT3+, Leu 7+ and Mo2+ cells. The bulk of T cells, macrophages and natural killer (NK) cells was found in the Fc epsilon R- cells which contained fewer B cells than the fraction of Fc epsilon R+ cells. These data thus indicated that the great majority of Fc epsilon R-bearing cells are B cells but that a small proportion of NK cells, macrophages and T lymphocytes also express Fc epsilon R. Upon incubation at 37 degrees C, B cells lost their Fc epsilon R and this phenomenon was selectively inhibited by IgE; however, purified T cells seemed to express more Fc epsilon R after overnight incubation at 37 degrees C and this was not influenced by IgE. It is finally shown that the expression of Fc epsilon R is cyclic and that Fc epsilon R-bearing B cells do not represent a functionally distinct subpopulation of B lymphocytes.

Adult↗

PubMed1986

Presence of IgE suppressor factors in human colostrum.

In spite of intensive investigations, the ability of breast feeding to delay and to attenuate atopic diseases in children remains debatable. This study documents a mechanism whereby breast feeding might interfere with the synthesis of IgE by breast-fed infants. Indeed, we show that colostrum contains IgE-binding factors (IgE-BF) capable of suppressing the in vitro synthesis of human IgE. Colostrum obtained from 15 donors was successively depleted of lipids and casein, filtered through Amicon XM50 membrane (mol. mass cut-off 50 kDa) and lyophilized. IgE-BF was demonstrated in such preparations by two different approaches, i.e. a classical rosette inhibition assay and Western blot analysis. In the first instance, lyophilized preparations of colostrum inhibited the binding of IgE-coated bovine erythrocytes to IgE recovered on the surface of RPMI 8866 lymphoblastoid cells. The rosette-inhibiting activity could be absorbed on IgE- but not on IgG-Sepharose 4B and it could be recovered in the eluate of IgE-Sepharose 4B. The molecular mass of IgE-BF was comprised between 10 to 20 kDa as estimated by gel filtration through a calibrated Sephadex G-75 column. After fractionation on 12% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transfer to nitrocellulose membrane, colostrum displayed one band of 14 kDa and reacted with radiolabeled IgE but not with IgG nor IgM. This 14-kDa band could be removed by absorbing colostrum with IgE- but not with IgG-Sepharose 4B. Most importantly, the colostrum IgE-BF suppressed the spontaneous in vitro synthesis of IgE by B lymphocytes derived from allergic donors without altering the production of IgM.

Colostrum↗

PubMed1986

IgE receptors on human lymphocytes. III. Expression of IgE receptors on mitogen-stimulated human mononuclear cells.

Human peripheral blood mononuclear cells (PBMC) were tested for the expression of Fc epsilon-receptor (Fc epsilon R) after stimulation with various mitogens in the absence of IgE. Fc epsilon R were found on virtually all the cells from 19 Epstein-Barr virus-transformed B cell lines including those derived from cord blood, from one agamma-globulinemic patient and VDS-0 pre-B cells. Hence, the data clearly indicate that Fc epsilon R may be expressed on very immature B cells. PBMC cultures stimulated with either pokeweed mitogen (PWM), phytohemagglutinin (PHA) or concanavalin A displayed an early increase of their content in Fc epsilon R-bearing cells followed by a decrease to levels below those of control cultures. After fractionation of the PWM-stimulated cultures into T and B cell-enriched preparations, most of the Fc epsilon R+ cells were in the in the B cell fractions and the same low levels of Fc epsilon R+ cells were found in the T cell fractions isolated from the PWM-stimulated and from the control cultures. Double-labeling experiments, employing biotinylated F(ab')2 monoclonal antibody to FcR and either fluorescein isothiocyanate-conjugated B1 or Mo2 monoclonal antibodies, indicated that PWM mainly exerted its effect on B cells and on monocytes. This effect was T cell dependent and it was mediated by soluble factors of T cell origin. At the peak of the PHA or concanavalin A response, most of the Fc epsilon R-bearing cells were found in the B cell fraction but the T cells isolated from mitogen-stimulated cultures contained significant more Fc epsilon R+ cells than those from the control cultures, suggesting that T cell mitogens had increased the expression of Fc epsilon R on some T cells. This view was supported by the finding of a higher proportion of Fc epsilon R+ cells in PHA-stimulated than in control cultures of highly purified T cells with a maximum response at the end of the culture period. Double-labeling experiments at the peak (day 2) of the peripheral blood mononuclear cell response indicated that the expression of Fc epsilon R was increased on B cells (B1+) and on monocytes (Mo2+). By using the same approach at the peak of the T cell response (day 7), it was found that T cells isolated from PHA-stimulated cultures expressed more Fc epsilon R than those isolated from control cultures.(ABSTRACT TRUNCATED AT 400 WORDS)

Cell Line↗

PubMed1986

Evaluation of the functional maturity of newborn T8+ suppressor cells and the resistance of newborn lymphocytes to suppression.

Concanavalin A (Con A) was used to study the suppressor function of human umbilical cord blood T cells. The suppressor activity and the phenotype of Con A-activated adult and cord T cells were compared using allogeneic adult mononuclear cell (MNC) response to pokeweed mitogen (PWM), phytohemagglutinin (PHA), and alloantigen as indicator culture systems. It was found that Con A-activated adult suppressor T cells were predominantly T8+ cells and suppressed PWM-induced IgG production by adult lymphocytes, as well as PHA- and alloantigen-induced proliferation of allogeneic adult MNC. Con A-activated cord T cells, however, exhibited no significant suppression in any of the three indicator systems. Furthermore, using Con A-activated adult T8+ cells as a source of suppression, the proliferative response of cord lymphocytes to PHA and alloantigen were as susceptible to suppression as those of adult lymphocytes. These results, together with previous findings that PWM-induced cord suppressor T cells were predominantly T4+ cell-mediated suppression, suggest that fetus/newborn lymphocytes achieved their selective inhibition on adult lymphocytes through the T4+ suppressor cell circuit.

Adult↗

PubMed1986

Human cord blood suppressor T lymphocytes. II. Characterization of inducer of suppressor cells.

Previously, we reported an antigen nonspecific inducer of T suppressor cell factor (TisF) produced by cord blood mononuclear cells (MNC) in 48-hr, two-way mixed lymphocyte cultures (MLC). The target of this factor was a radiosensitive, T4+ (T8-) adult suppressor T cell subset. The cellular origin of this TisF was examined in the present study. IgG production by pokeweed mitogen (PWM)-stimulated adult MNC was used as an assay for TisF activity. It was found that TisF-producing cells formed rosettes with sheep erythrocytes (E+) and were independent of adherent cells (AC) in the production of TisF. They were resistant to irradiation (2500 rads) and phenotypic characterization with T cell reactive monoclonal antibodies indicated that they resided in the T8- (T4+) population. Furthermore, both TQ1- and TQ1+ cells were required for the production of TisF activity and such activity could not be reconstituted by supernatants from TQ1- MLC and TQ1+ MLC. These results indicate that the production of TisF is dependent upon interactions between radioresistant E+, T8-, TQ1- and radioresistant E+, T8-, TQ1+ cells.

Antibodies, Monoclonal↗

PubMed1986

Production and characterization of mouse monoclonal antibodies to allergenic epitopes on LolpI (Rye I).

This study describes the production and characterization of mouse monoclonal antibodies (Mab) to LolpI (Rye I), the major allergen of rye-grass pollen. Hybridoma cell lines were screened for the secretion of Mab, the binding of which to labelled LolpI could be inhibited by pooled human sera containing IgE and IgG anti-LolpI antibodies. Twenty monoclonal hybridoma cell lines were expanded, and their product was purified and characterized. Each Mab bound to LolpI but not to unrelated antigens. Cross-inhibition studies allowed the grouping of these 20 Mab into five families differing by their epitope specificity. One representative Mab of each family was tested for its ability to inhibit human IgE/IgG anti-Lolp-I from 15 allergic donors as well as for its inhibition by affinity-purified anti-LolpI antibodies isolated from 14 donors. The results indicated that each family of Mab was specific for an epitope that was identical or close to that recognized by some human anti-LolpI antibodies. It is further shown that human IgE/IgG anti-LolpI are heterogeneous with some patients reacting preferentially with one or two epitopes defined by the Mab LolpI, and others reacting with epitopes different from those identified by the Mab LolpI.

Allergens↗

PubMed1986

Presence of antigenic determinants common to Fc IgE receptors on human macrophages, T and B lymphocytes and IgE-binding factors.

The present study indicates that two Mab specific to Fc epsilon R (MabER) on human B lymphocytes also react with Fc epsilon R on macrophage and T-cell lines. More importantly, it is also shown that MabER cross-react with IgE-BFs derived from B, T and macrophage cell lines. This conclusion is supported by the following observations: the binding of MabER to Fc epsilon R-bearing cells is blocked by the CSN of T, B and macrophage Fc epsilon R-bearing cell lines, known to contain IgE-BFs as shown by their inhibition of rosette formation between IgE-coated erythrocytes and Fc epsilon R-bearing cells; the material purified from the CSN of each Fc epsilon R(+) cell lines by affinity chromatography on MabER-Affi-gel blocks the rosetting of U937 cells with IgE but not with IgG-coated erythrocytes; the same affinity-purified material inhibits the binding of 125I-IgE to a selected anti-IgE Mab (Mab 75); and the CSN of Fc epsilon R(+) cells but not of Fc epsilon R(-) cells reacts in a solid-phase sandwich radioimmunoassay with two MabER (135-176), and their reactivity is significantly retained on IgE-Affi-gel from which it may be recovered by glycine elution. This RIA is not influenced by any class of Ig, including IgE, employed at a final concentration of 100 micrograms/ml. Human serum also reacts in the RIA, and parallel dilution curves are obtained with different CSN and human sera. The RIA proved to be a reproducible and sensitive method to quantify human IgE-BFs. The expression of the same antigenic determinants on Fc epsilon R from T, B and macrophages as well as on the IgE-BFs secreted by these cells indicates structural homology between IgE receptors and IgE-FBs and suggests that they are encoded by the same gene.

Antibodies, Monoclonal↗

PubMed1986

Anti-idiotypes to anti-Lolp I (Rye) antibodies in allergic and non-allergic individuals. Influence of immunotherapy.

Anti-idiotypes (aId) reacting with anti-Lol I (Lolp I; Rye I) antibodies were detected by their ability to bind to radioiodinated F(ab')2 anti-Lol I. Sera were tested after removal of anti-Lol I and anti-heavy and light chain activity by adsorption on Lol I-Sepharose 4B and normal human serum Sepharose 4B. The binding of aId to Id was inhibited by affinity purified anti-Lol I but not by certain unrelated immunoglobulins; in some sera this binding was also inhibited by Lol I. The levels of aId were measured in serial bleedings collected over a 1 year period from Lol I-sensitive patients, allergic donors not sensitive to Lol I and non-allergic persons. In Lol I-allergic patients the levels of aId were significantly influenced by seasonal exposure to pollen and by immunotherapy with extracts of grass pollen. Moreover, in 12 out of 16 cases, there was also a significant inverse relationship between changes in serum levels of aId and of IgG or IgE anti-Lol I. Most interestingly, aId were also detected in non-allergic individuals; in this case, the levels of aId were not influenced by the pollen season. The data suggest that Id-aId interactions may play a role in the regulation of anti-Lol I antibody production.

Allergens↗

PubMed1985

Demonstration of intracytoplasmic IgE in circulating lymphocytes of allergic individuals.

Cells containing intracytoplasmic IgE (IC IgE) were demonstrated in the peripheral blood mononuclear cells of atopic individuals by means of indirect immunofluorescence, employing mouse monoclonal anti-human IgE antibody. IC IgE-positive cells are low-density B cells as shown by centrifugation on discontinuous bovine serum albumin density gradient and by their reactivity with B1 monoclonal antibody specific to B lymphocytes, respectively. Further characterization of these cells by means of a rosette assay employing anti-Ig-coupled bovine erythrocytes indicated that these cells were surface IgE (sIgE) positive and sIgM negative. The data strongly suggest that activated IgE B cells are circulating in the blood of allergic individuals.

B-Lymphocytes↗

PubMed1985

Induction of IgA-specific suppressor activity in human T-lymphocyte cultures.

Cell-free supernatants of human circulating T-lymphocyte cultures incubated with secretory IgA (S-IgA) specifically suppressed both spontaneous IgA synthesis by B lymphocytes isolated from allergic individuals and pokeweek mitogen-induced IgA secretion by peripheral blood mononuclear cells. Cell-free supernatants of T-cell cultures incubated with IgE had no effect on IgA, IgG, or IgM synthesis. Hence, it is concluded that upon incubation with S-IgA, but not with another Ig class, T lymphocytes release IgA-specific suppressor factors.

Antibody Specificity↗

PubMed1985

Human cord blood suppressor T lymphocytes: I. Phenotype and target of the inducer of suppressor cell factor.

The present study examines the characteristics of the cord suppressor T cells and their targets. When an inducer of suppressor T cell factor (TisF) from culture supernatant of alloantigen-activated cord lymphocytes was used as a source of suppression, adult lymphocyte response to soluble antigen candidin, alloantigens, and pokeweed mitogen were all suppressed. These results suggest that TisF acts primarily on T cells in an antigen-nonspecific fashion. Furthermore, preculture T cell irradiation, but not T8+ cell depletion, of adult lymphocytes abrogated the suppressive effect of TisF on the PWM-stimulated IgG production, suggesting that the target of TisF belongs to the radiosensitive T8-(T4+) T cell subset. When different cord T cell subsets were tested for suppressor activity, only radiosensitive T4+ cells were capable of suppressing IgG production by adult lymphocytes. Neither preculture T8+ cell depletion nor irradiation of adult T cells affected the suppression. Taken together, these results suggest that the suppressor activity of cord T cells originated from an inducer of suppressor cells that activates radiosensitive T4+ suppressor effector cells through TisF. In turn, these effector cells act on either radioresistant T4+ helper T cells or B cells or both.

Adult↗

PubMed1985

In utero immunization of the fetus to tetanus by maternal vaccination during pregnancy.

We tested 36 pairs of umbilical cord blood and maternal sera collected at the time of delivery by radioimmunoassay and by Western blot analysis for IgG or IgM antitetanus antibodies (anti-TT). Twenty-one participants had received a recall injection of tetanus toxoid at various periods during pregnancy. Maternal vaccination in the last trimester of pregnancy was associated with the presence of IgM anti-TT in the cord blood sera; these were not detected in neonatal sera from mothers who were not vaccinated during pregnancy or who received the booster injection during the first two trimesters of gestation. The results could not be ascribed to artifacts such as the contamination of neonatal sera by maternal blood, the contamination of the anti-IgM antisera by antiidiotypes, or by the presence of neonatal IgM rheumatoid factor binding to immune complexes made of maternal IgG anti-TT and radiolabelled TT. Hence, it is concluded that maternal vaccination during the last trimester of pregnancy may induce in utero active immunization of the fetus.

Female↗

PubMed1985

Detection and characterization of monoclonal antibodies specific to IgE receptors on human lymphocytes by flow cytometry.

BALB/c mice were immunized with human lymphoblastoid cells (RPMI 8866 cells) expressing surface receptors for IgE (Fc epsilon R). Spleen cells from animals displaying high titres of anti-Fc epsilon R antibodies were fused with HGPRT-deficient NSI myeloma cells. Anti-Fc epsilon R antibodies were identified by a flow cytometric assay based on their ability to block the binding of IgE-coated fluorescent latex particles to Fc epsilon R-positive cells. Fourteen monoclonal hybridoma cell lines secreting antibody of the required specificity were amplified in tissue culture and then grown in the peritoneal cavity of BALB/c mice in order to obtain ascitic fluids with high antibody titres. The specificity of each monoclonal antibody (Mab) to lymphocyte Fc epsilon R was shown by the following observations: (i) the intact monoclonal antibody molecule or, in some cases, its F(ab')2 fragments blocked the binding of IgE to several Fc epsilon R(+) cell lines different from that employed for the initial immunization; (ii) the Mab bound directly to all the Fc epsilon R(+) cell lines tested, but not to several Fc epsilon R(-) cells as determined by indirect immunofluorescence; (iii) the binding of Mab to Fc epsilon R(+) cells was selectively blocked by IgE, but not by the other classes of Ig; and (iv) Mab had no effect on the binding of IgG to Fc gamma R on normal human peripheral blood mononuclear cells (PBMC).

Animals↗