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Y Jacques

Publications and source records attributed to Y Jacques.

At least 73 records · Page 4Linked to original sources
PubMed1991

Synergistic action of monoclonal antibodies directed at p55 and p75 chains of the human IL-2-receptor.

TU27, a mouse IgG1 mAb directed at the p75 chain of the human IL-2R, was analyzed for its ability to interact with IL-2 binding on isolated p75 chains (YT-2C2 cells) and high affinity p55/p75 receptors (human alloreactive T cell clone 4AS), to inhibit IL-2-induced proliferation (4AS cells) and to cooperate with an anti-p55 chain mAb (33B3.1) for inhibiting IL-2 binding and proliferation. TU27 and IL-2 bound to the isolated p75 chain expressed by YT-2C2 cells with respective dissociation constants (Kd) of 1.3 and 1 nM. They cross-inhibited each other for binding with inhibition constants (Ki) in agreement with their respective Kd values. The nature of the interaction was, however, not purely competitive and suggested nonidentical epitopes for the two ligands on the p75 chain. On 4AS cells, IL-2 bound with high affinity (Kd = 50 pM) and TU27 with an affinity similar to that found on YT-2C2 cells. The binding of TU27 and IL-2 were also mutually exclusive on 4AS cells. However, the mechanism of interaction of TU27 with IL-2 was complex since the inhibitory potency of the antibody depended on temperature, antibody preincubation and time of assay. Data obtained at 4 degrees C in the presence of suboptimal, tracer-like concentrations of IL-2 indicated that the intrinsic affinity of TU27 for the high affinity configuration was 15-fold lower than for the isolated p75 chain and argued in favor of the affinity-conversion model (as opposed to the preformed complex model) in which p55 and p75 are dissociated in the absence of IL-2. At 37 degrees C, TU27 inhibited IL-2 binding only on short time assays (6 min). Longer time (30 min) of IL-2 binding resulted in an almost complete disappearance of the effect of TU27, suggesting that internalization of the high affinity p55/p75/IL2 complex enables the cells to escape from the inhibitory effect of TU27. In the presence of the 33B3.1 mAb, the interaction of TU27 with IL-2 resembled the one observed on YT-2C2 cells, suggesting that 33B3.1 is able to inhibit the IL-2-induced association of p55 and p75. Both antibody were found to synergize on 4AS cells, as a result of a cooperative mechanism in which 33B3.1 blocks the formation of the high affinity complex hence allowing TU27 to bind with higher affinity, and TU27 blocks IL-2 binding to the p75 chain. Proliferation studies corroborated the binding experiments.(ABSTRACT TRUNCATED AT 400 WORDS)

Antibodies, Monoclonal↗
PubMed1991

Cluster-function relationship of rat-antimouse P55 IL-2 receptor monoclonal antibodies. In vitro studies of the CTL-L2 mouse cell line and in vivo studies in a delayed-type hypersensitivity model in mice.

Monoclonal antibodies directed against the P55 component of the interleukin 2 receptor (IL-2-R) have been used to prevent allograft rejection in various animal models, including primates and man. This study compares the functional effects of seven MoAbs directed against the mouse IL-2-R P55 chain both in vitro using the mouse CTL-L2 cell line and in vivo in a sheep red blood cell-induced delayed-type hypersensitivity model. Data from in vitro studies showed that a cluster of four MoAbs (cluster I: 5A2, 125, 135 [IgG2a] and AMT13 [IgG2b]) competed with IL-2 for binding to the P55 chain and caused an inhibition of IL-2-induced proliferation on CTL-L2. The respective dissociation constants (Kd) of the four MoAbs were 1.1, 1.4, 2.5, and 5.5 nM, and they all displayed a common maximal binding capacity of 2 x 10(5) sites per cell on CTL-L2. None of these MoAbs were found to fix rabbit complement. The three other MoAbs (2E4: IgG2a, 7D4: IgM, PC61: IgG1) with respective Kd of 0.8, 0.2, and 0.85 nM and maximal binding capacities of 2 x 10(5), 4 x 10(5) sites per cell did not interfere with IL-2 binding and did not affect the IL-2-induced proliferation of the murine cell line. All three MoAbs were found to define three separate epitopic clusters independent of cluster I. Among them, only 2E4 induced a strong complement-mediated cytotoxicity. In vivo experiments showed that all MoAbs from cluster I were efficient in suppressing the DTH reaction and that the magnitude of their effect was consistent with their respective Kds. At a suboptimal dose of 1 microgram per day, the DTH inhibition indices were 40%, 43%, 23%, and 9% for 5A2, 125, 135, and AMT13, respectively. The 2E4 MoAb was found to be as efficient as cluster I MoAbs in suppressing DTH (53% inhibition at 1 microgram/day) while 7D4 and PC61 induced only a moderate inhibitory effect (37% inhibition for each MoAb given at 10 micrograms/day, compared with 70% inhibition for cluster I MoAbs). Taken together, our results indicate that blocking the IL-2/IL-2-R interaction without complement fixation is sufficient per se to attenuate the DTH reaction, and conversely that strong complement-mediated cytotoxicity in the absence of a functional effect in the IL-2/IL-2-R interaction is also effective in this system. Finally, no synergistic effect between MoAbs belonging to different clusters was evidenced in the DTH model.

Animals↗
PubMed1991

Effect of anti-LFA1 (CD11a) monoclonal antibodies in acute rejection in human kidney transplantation.

A murine IgG1 monoclonal antibody, 25-3 (Immunotech, France), directed against the alpha chain (CD11a) of the human LFA1 molecule was used in the treatment of 7 histologically documented first acute rejection in first kidney transplantations under cyclosporine. Four patients (group I) received 20 mg/day for 2 days and 10 mg/day for 8 days of 25-3 MoAb. One developed Quincke's edema after the first injection of 25-3 and was immediately withdrawn from the study. In 2 patients, whose serum creatinine continued to increase, 25-3 MoAb was replaced by steroids, followed by ALG after 3 and 4 days of treatment, respectively. In the last case, rejection was reversed by 25-3 MoAb alone. As the clinical response of rejection to 25-3 was poor, another group of 3 patients (group II) was treated with 25-3 at a dose of 40 mg/day for 2 days, 20 mg/day for 2 days, and 10 mg/day for 6 days, but 25-3 was still unsuccessful in reversing acute rejection, and rescue treatment was initiated between days 5 and 8 in all cases. MoAb tolerance was excellent in 3 patients. With the exception of the one case of Quincke's edema, only minor side effects were noted in the last 3 recipients. 25-3 MoAb serum trough levels peaked between 1.5-3.5 micrograms/ml at day 3 in group I and between 2-9 micrograms/L at day 2 in group II. Surprisingly, only one patient, in group I, exhibited a borderline IgG immune response against 25-3. These findings suggest that the 25-3 anti-CD11a MoAb is ineffective in controlling the course of acute rejection in kidney transplantation. However as already reported for another anti-LFA1 or with an anti-CD4 MoAb in mouse, 25-3 would be the first example in humans of a MoAb that does not elicit a strong immune response against its own determinants. This property might have important applications if 25-3 can prevent rejection in a prophylactic protocol or block the immune response against other MoAbs.

Adult↗
PubMed1990

Biochemical study of a recombinant soluble interleukin-2 receptor. Evidence for a homodimeric structure.

A truncated soluble form of the human interleukin-2 receptor p55 chain (T-S-IL-2R) was expressed to high levels in RODENT (mammalian) cells and affinity-purified. Its biochemical behavior was analyzed by polyacrylamide gel electrophoresis (PAGE), gel filtration, and sucrose gradient centrifugation. It migrated as a single 40-kDa band on sodium dodecyl sulfate-PAGE (reducing or nonreducing conditions), whereas it ran as a 80-kDa component on native PAGE or as a 86-kDa component on gel filtration. The combination of gel filtration and density gradient sedimentation gave a Stokes radius of 4.0 nm and a sedimentation coefficient of 3.72 S. The deduced molecular mass was 67 kDa, and the fractional ratio was 1.516. These data therefore indicated that the T-S-IL-2R was secreted as an homodimer of two noncovalently associated 40-kDa subunits. Cross-linking experiments using bifunctional reagents enabled the materialization of the dimeric structure on sodium dodecyl sulfate-PAGE. Stoichiometric binding studies using two monoclonal antibodies (mAbs 33B3.1 and 11H2) reacting with separate epitopes on the p55 chain also strongly supported the dimeric structure. Indeed, there was one binding site for the 33B3.1 mAb (and Fab fragment) per T-S-IL-2R 40-kDa subunit, whereas the 11H2 mAb (or Fab fragment) could bind only half a site per subunit, a result which could only be explained when assuming more than one subunit for the native T-S-IL-2R. Soluble interleukin-2 receptor species were also purified from culture supernatants of either L cells transfected with the full-length p55 cDNA or a normal alloreactive T cell clone. Similar biochemical behavior and reactivities with the two mAbs were found. Finally, cell-surface p55 chains expressed either by pgL21 or 4AS cells bound the 33B3.1 and 11H2 mAbs in a 2:1 ratio, suggesting that the p55 chains are also associated as homodimers when imbedded in the membrane.

Animals↗
PubMed1990

Production of human interleukin for DA cells (HILDA)/leukemia inhibitory factor (LIF) by activated monocytes.

We demonstrate mRNA accumulation and production of HILDA/LIF by human activated Mo, monocyte-derived macrophages and myelomonocytic cell lines. Among the various stimuli tested, the synergistic combination of phorbol diester and VD3 was the most potent inducer of HILDA/LIF gene expression. The kinetics of mRNA accumulation on activated Mo showed a stimulation peak at 24 hr which declined thereafter. HILDA/LIF activity in culture supernatants was detected at 24 hr and reached a plateau at 72 hr of culture. In contrast to Mo, PBL did not accumulate HILDA/LIF mRNA upon culture with PDBu and VD3, whereas PHA and the combination of PDBu and A23187 induced HILDA/LIF mRNA accumulation and secretion in the culture supernatant. To exclude the possibility that HILDA/LIF was produced by contaminating PBL, highly enriched Mo preparations were used, which were devoid of T cells as assessed by the absence of TCR-beta chain mRNA transcripts. HILDA/LIF production by monocytic cells was further documented by the capacity of stimulated U937 cell conditioned medium to compete with 125I-labeled nHILDA/LIF for binding to its receptor on murine M1 cells. Under the synergistic effect of PDBu and VD3 stimulation, Mo-derived macrophages as well as HL-60 and U937 cell lines accumulated HILDA/LIF mRNA and produced this cytokine with identical kinetics as for Mo. Finally, we show that HILDA/LIF mRNA accumulation in U937 cells upon stimulation with PDBu, or the combination of PDBu and VD3, was inhibited in the presence of the protein synthesis inhibitor CHX. These results document for the first time that human Mo, when stimulated appropriately in vitro, can express the HILDA/LIF gene and its product, and that intermediate proteins must be newly synthesized in this process.

Cell Differentiation↗
PubMed1990

Randomized controlled trial of a monoclonal antibody against the interleukin-2 receptor (33B3.1) as compared with rabbit antithymocyte globulin for prophylaxis against rejection of renal allografts.

Interleukin-2 is a major growth factor for activated T lymphocytes, and antibodies reacting with the Tac-chain component of the interleukin-2 receptor can prevent allograft rejection in animals. Because Tac chains are expressed only on a small fraction of activated lymphocytes, monoclonal antibodies against the interleukin-2 receptor may offer a more specific means of immunosuppression than polyclonal antilymphocyte globulin in prophylaxis against graft rejection. Therefore, we compared the immunosuppressive effect of 33B3.1, a rat monoclonal antibody against the human Tac chain, with the effect of a rabbit polyclonal antithymocyte globulin in a randomized study of 100 recipients of first renal transplants. Injections of 33B3.1 (10 mg per day) were tolerated well, whereas major side effects in 15 of 47 patients (32 percent) receiving antithymocyte globulin required discontinuation of treatment before day 14. The incidence of rejection episodes was not statistically different in the two groups at days 14, 30, 60, and 90 after transplantation. Patient and graft survival was also equal in the two groups at one year (96 and 85 percent, respectively, in both groups), and graft function was similar. The total number of infectious episodes within the first three months was lower in the 33B3.1 group than in the antithymocyte group (47 vs. 72). The drop in peripheral-blood lymphocyte concentrations was significantly larger in the patients treated with antithymocyte globulin. The level of circulating Tac-chain-bearing lymphocytes remained below 1 percent during 33B3.1 treatment, as compared with 4 to 5 percent during antithymocyte-globulin treatment (P not significant). We conclude that 33B3.1 is as effective as antithymocyte globulin in the prevention of renal-transplant rejection, and its use results in fewer infections and side effects.

Adolescent↗
PubMed1990

Constitutive production of human interleukin for DA cells/leukemia inhibitory factor by human tumor cell lines derived from various tissues.

The cytokine HILDA (human IL for DA cells)/LIF (leukemia inhibitory factor), previously reported to trigger the proliferation of the DA1.a cell line was purified to homogeneity from the culture supernatant of the 5637 bladder carcinoma cell line by using a four step procedure, including cationic exchange chromatography at pH 6, Con A affinity chromatography, reverse phase HPLC, and gel filtration HPLC. The purified radiolabeled protein was analyzed in SDS-PAGE and a single band with a molecular mass of 43 kDa was revealed. The iodinated material was then tested in a radioreceptor assay using the M1 cell line as a second target cell line. The binding of the natural 125I hormone was abrogated in a dose dependent and specific fashion by either natural and rHILDA. The limit of signal detection of displacement for the radiolabeled ligand by unlabeled sample was found to be 0.05 ng/ml. The proliferative DA1.a assay and the M1 radioreceptor assay were used to analyze the HILDA content of 17 human tumor cell line culture supernatants, and 12 among them were spontaneously secreting a detectable level of LIF. The secreted amount of HILDA was largely enhanced by treating the cell line with 30 to 80 nM PMA; in these conditions a 10 to 20x increase in the detected amount was observed. The specificity of the detected signal was reinforced by analyzing the mRNA expression of HILDA in the tumor cell lines. The secreting cell lines were found to express various forms of LIF transcripts with a major specie at 3.8 kb.

Animals↗
PubMed1990

Anti-human interleukin 2 receptor monoclonal antibody isotypic switching: chimeric rat-human antibodies.

Univalent and bivalent (2Fab'-Fc) chimeric rat-human antibodies were constructed by chemical coupling (thioether bonds) of Fab' fragments from the 33B31 rat anti-human interleukin 2 receptor (alpha chain) monoclonal antibody to human IgG or Fc fragments. The purity of the chimeric antibodies obtained after purification was assessed by the sodium dodecyl sulfide-polyacrylamide gel electrophoresis method. The affinity of chimeric antibodies for the human interleukin 2 receptor was determined. The affinity of the 2Fab'-Fc was better (Kd = 0.87 nM) than that of the Fab'-IgG (Kd = 2.04 nM) or the Fab'-Fc chimera (Kd = 3.93 nM). Binding studies on a T-cell clone showed that the percentage of positive cells recognized by chimeric antibodies was comparable to that obtained with unmodified 33B3.1 IgG2a or its corresponding Fab' fragment. In addition, the inhibition of interleukin 2-induced cell proliferation and allogeneic proliferative response by chimeric antibodies was of the same magnitude as that obtained with the rat IgG2a anti-interleukin 2 receptor monoclonal antibody and Fab' fragments. This study shows the possibility of changing the isotype of monoclonal antibodies without important modification to their binding activity. These reagents may offer an alternative to unmodified monoclonal antibodies for therapeutic application.

Animals↗
PubMed1989

Characterization and NH2-terminal amino acid sequence of natural human interleukin for DA cells: leukemia inhibitory factor. Differentiation inhibitory activity secreted by a T lymphoma cell line.

Six human T lymphomas and an NK-like cell line were tested for their ability to produce HILDA, one of the two human growth promoting activities for the DA1.a cells. Among them, the HSB2 cell line turned out to be the only one secreting significant HILDA activity (200-400 units/ml) after activation with 50 nM phorbol myristate acetate. Subclones of the HSB2 cell line were obtained by limiting dilution experiments. One of them (2B3) was found to secrete 1,000-5,000 units/ml of HILDA after phorbol myristate acetate activation in the presence of 10% fetal calf serum and 200-500 units/ml in serum-free conditions. 2B3-HILDA was purified from serum-free conditioned medium by a four-step procedure including fast flow cationic exchange at pH 6, concanavalin A chromatography, reverse-phase high performance liquid chromatography and gel-filtration high performance liquid chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the purified radiolabeled cytokine revealed a single band of Mr 43,000, which co-electrophoresed with the biological activity. The NH2-terminal amino acid sequence of the first residues of the protein were determined and found to be similar to the equivalent residues deduced from the molecularly cloned cytokine. Isoelectric point determination revealed some charge heterogeneity of HILDA, which focused to pH 8.5-9 after neuraminidase treatment. Carbohydrate content of the cytokine was studied by deglycosylation experiments which showed that the O-linked oligosaccharides represented 2,000-3,000 and that the N-linked sugars account for half of the apparent molecular weight of HILDA.

Amino Acid Sequence↗
PubMed1989

Monoclonal anti-IL2-receptor in organ transplantation.

So far, only monoclonal antibodies directed at functional target molecules on lymphocyte surface membrane have been proven useful in preventing or reversing allograft rejection episodes. Antibodies directed against light chain (P55) of interleukin 2 (IL2) receptor and able to interfere with IL2 binding on the IL2-receptor in its high-affinity conformation (only expressed on activated T cells) are effective in various animal models and recently in a preventive protocol in human kidney graft recipients. Thus, IL2-receptor targeting emerges as a new therapeutic strategy involving only a small pool of progenitors committed against donor antigens. Furthermore, membranous or soluble forms of P55, as indicators of the presence of alloreactive clones in the graft or at the peripheral level, may offer new tools for monitoring the rejection process.

Animals↗
PubMed1989

Anti-interleukin 2 receptor monoclonal antibody in the treatment of ongoing acute rejection episodes of human kidney graft--a pilot study.

Monoclonal antibodies (MoAbs) against human interleukin 2 receptor (IL-2-R) have been shown to prevent early kidney rejection in animals and humans. We report here the effect of an anti-IL-2-R MoAb (33B3.1) inhibiting IL-2 binding high-affinity sites on activated lymphocytes in 10 declared acute rejection episodes of first cadaveric kidney grafts. Six patients were under cyclosporine treatment only at the time of diagnosis of the rejection. All rejection episodes but one were biopsy-proved cellular rejections. Treatment consisted of intravenous infusions of 33B3.1 at 20 mg/day x 2 days, followed by 10 mg/day for 8 additional days. In case of MoAb ineffectiveness at day 5, anti-IL-2-R MoAb was discontinued and a rescue treatment of corticosteroid boluses (CSb) was given. If not, in all cases corticosteroids (CS) were given (1 mg/kg) at the end of MoAb treatment (day 10) and tapered off thereafter. Two rejection episodes immediately responded to 33B3.1 treatment. During 33B3.1 treatment four other patients had only a stabilization of their blood creatinine concentration, which nevertheless returned to prerejection levels after day 10 when anti-IL-2-R was discontinued and CS administered at 1 mg/kg (no rescue treatment). The four remaining patients had an increase of their blood creatinin levels at day 5 despite 33B3.1 treatment, and their renal function only improved with CSb rescue treatment. One of these patients lost the graft despite rescue treatment, as well as a 9-day course of antithymocyte globulin. Trough levels of MoAb reached a plateau as early as day 2 (approximately 6 micrograms/ml). All patients developed antibodies (IgM and IgG) after day 14. In no instance could unresponsiveness be related to low circulating 33B3.1 trough levels or to early host anti-MoAb immune response (IgM or IgG). We conclude that 33B3.1, known to be effective in preventing early rejection, has only inconsistent and/or incomplete effects on the ongoing rejection process. Our data suggest that once IL-2-dependent clones are expanded in the rejected graft, interference with IL-2/IL-2-R signals does not block the effector mechanisms sustaining acute rejection.

Antibodies, Monoclonal↗
PubMed1989

Biodistribution of an anti-interleukin 2 receptor monoclonal antibody in rat recipients of a heart allograft, and its use as a rejection marker in gamma scintigraphy.

Anti-interleukin-2 receptor monoclonal antibodies have been shown to prevent allograft rejection. This paper reports on the biodistribution of a mouse MoAb directed at the 55 Kd alpha chain of rat interleukin-2 receptor (IL2-R) during allograft rejection. Only a low percentage (approximately 1%) of intact 125I-labeled MoAb was detected in the rejected graft, and irrelevant control IgG1 was found at a similar level. This suggests that most of the injected intact MoAb bound to graft tissue via its monomorphic Fc segment. In contrast, OX39 F(ab')2 fragments showed a preferential localization in the rejected allograft and did not bind to the LEW-to-LEW syngeneic heart graft. Irrelevant F(ab')2 did not concentrate in the allogeneic graft. Accordingly, F(ab')2 fragments from OX39 or irrelevant MoAb were used for gamma-scintigraphy on allograft recipients together with biodistribution studies. Results show that scintigraphy was able to detect allograft accumulation of 131I OX39 F(ab')2, whereas no imaging was obtained when OX39 F(ab')2 was used in the syngeneic combination or when irrelevant 131-IgG1 F(ab')2 was given to allograft recipients. This method, applied to the clinical situation, could be of interest for detection of early graft rejection episodes by immunoscintigraphy using reagents specific for activation determinants on lymphocyte membranes, such as anti-interleukin-2 receptor MoAb.

Animals↗
PubMed1989

Interleukin 2 receptor in rat heart allograft rejection.

Soluble interleukin 2 receptors (S-R-IL-2) of truncated Tac chain, produced in vitro during T lymphocyte activation, may represent an in vivo marker of an alloimmune reaction. We analyzed serum S-R-IL-2 production during acute heart allograft rejection and compared soluble and membranous Tac chain (blood lymphocytes and graft invading cells) regulation during rejection. Serum S-R-IL-2 was tested in an immunoradiometric assay, with a combination of two mouse IgG1 anti-IL2-R mAbs (ART18 and OX39). Membranous Tac chain was analyzed by immunochemistry in graft tissue, and by immunofluorescence on blood and spleen leukocytes. Four experimental groups were used: untreated allogeneic, untreated syngeneic, CsA-treated (10 mg/kg/day for 15 days) allogeneic and CsA-treated syngeneic graft recipients. In the untreated allogeneic group, S-R-IL-2, tested every day until rejection (9.14 +/- 1.6 days), increased as early as day 3 after transplantation, peaked at day 6, and plateaued thereafter. The allograft was infiltrated at day 5 by Tac chain-positive cells (10% of OX1 cells and 84% of OX19 cells). A small percentage of mononucleated cells was labeled in blood, but not in spleen, by ART18 and OX39 at day 7 only. In contrast, in untreated syngeneic and CsA-treated allogeneic combinations, there was no increase of baseline S-R-IL-2 level (P less than 0.001), and graft infiltrate did not contain IL-2-R positive cells. CsA treatment prolonged heart allograft survival (41.3 +/- 2.8 days). Baseline S-R-IL-2 levels during treatment were lower than those observed in untreated animals. In the CsA-treated allogeneic group, after CsA treatment interruption, S-R-IL-2 levels significantly increased, reaching a plateau at day 37. Results suggest that S-R-IL-2 measurement can be useful for clinical diagnosis of allograft rejection.

Animals↗
PubMed1989

Interleukin 2-like material in human epidermis: a ligand for the human interleukin 2-receptor 55 kD alpha chain.

The antirecombinant interleukin 2 (rec-IL-2) monoclonal antibody (moAb) 15.2 cross-reacts with a skin antigen located at the cell surface of human keratinocytes within the granular layer. This study extends the analysis of this IL-2-like material to its reactivity with eight antibodies raised against natural IL-2, rec-IL-2 or IL-2 peptides. Four among them were found to react with the granular epidermal layer as well as with a simian virus 40 (SV40) transformed human keratinocyte cell line. Each of these four antibodies gave similar labeling patterns, although with different intensities, and competitively inhibited each other. Analysis at the messenger RNA level in epidermal cells and SVK 14 also indicated that this material is very likely different from IL-2. From the knowledge, for some of these antibodies, of the amino-acid regions they recognize on the IL-2 molecule, it is inferred that the skin antigen shares with IL-2 at least two overlapping epitopes located in the 33-54 amino-acid region of IL-2, a region that has been shown to be involved in the binding of IL-2 to the IL-2-receptor (IL-2-R) 55 kD chain. Indeed, a purified recombinant soluble species of this IL-2-R is shown in this study to bind specifically to the IL-2-like skin material. As far as IL-2-R bearing cells are found in normal epidermis (Langerhans cells) and as important infiltrates of IL-2-R positive T lymphocytes are often encountered in cutaneous diseases, a potential role for this IL-2-like material in skin immunophysiopathology is suggested.

Antibodies, Monoclonal↗