Monoclonal antibodies as a tool for phylogenetic studies of major histocompatibility antigens and ? 2-microglobulin

Teillaud, Jean‐Luc; Crevat, D.; Chardon, Patrick; Kalil, Jorge; Goujet‐Zalc, C.; Mahouy, G.; Vaiman, M.; Fellous, Marc; Piou, Donald

doi:10.1007/bf00364261

Cited by 47 publications

(12 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…mAb w6/32 (IgG2a) defines a monomorphic determinant on human HLA-A, -B, and -C molecules (21) and crossreacts in a nonpolymorphic fashion with bovine class I MHC molecules (22). mAb B1.1G6 (IgG2a) reacts with human and bovine P2-microglobulin (23,24). mAb BT3/8 (IgG2a) recognizes a cell surface molecule that is expressed on all cell lines infected with Theileria and on some normal bovine leukocytes (25).…”

Section: Methodsmentioning

confidence: 99%

Bovine cytotoxic T-cell clones specific for cells infected with the protozoan parasite Theileria parva: parasite strain specificity and class I major histocompatibility complex restriction.

Goddeeris¹,

Morrison²,

Teale³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

We present information on the specificity of three bovine cytotoxic T-cell clones reactive with lymphoblasts infected with the protozoan parasite Theileriaparva. The clones were derived from peripheral blood mononuclear cells of an animal immunized with T. parva (Muguga stock), after five stimulations in vitro with an autologous parasitized cell line. The three clones belonged to the BoT8+ subset of T cells, which is similar to the human CD8' T-cell subset. On the basis of analysis on a panel of infected target cells originating from cattle of different major histocompatibility complex (MHC) phenotypes, killing by all three clones was found to be restricted to targets bearing the class I MHC specificity KN1O4, which is defined by alloantiserum KNA104 and monoclonal antibody IL-A4. This class I MHC restriction was confirmed by blocking of target cell lysis with these antibodies and monoclonal antibody w6/32, which reacts with a nonpolymorphic determinant on bovine class I MHC molecules. The three clones were parasite strain specific, in that they did not kill cells of the appropriate MHC type infected with T. parva (Marikebuni stock). These findings, taken together with previous observations that immunization of cattle with T. parva (Muguga) does not provide protection against challenge with T. parva (Marikebuni), suggest that the cytotoxic T cells recognize a cell surface antigen that may be important in induction ofimmunity to the parasite.

show abstract

Section: Methodsmentioning

confidence: 99%

Bovine cytotoxic T-cell clones specific for cells infected with the protozoan parasite Theileria parva: parasite strain specificity and class I major histocompatibility complex restriction.

Goddeeris¹,

Morrison²,

Teale³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…In immunological studies, urinary β 2 -m cross-reacted with colostral β 2 -m, but not with human urinary β 2 -m. An investigation using monoclonal antibody against human β 2 -m revealed that a half of the antibodies did not react with bovine β 2 -m [28]. These findings indicate that bovine β 2 -m is not homologous to those of human β 2 -m in the epitope structure.…”

Section: Purification Of Bovine Urinary β 2 -M: Sds-page Patterns Ofmentioning

confidence: 87%

Purification of Bovine Urinary .BETA.2-Microglobulin and Its Biochemical Characteristics.

Hoshi

Nagai

Nakajima

et al. 2000

The Journal of Veterinary Medical Science

View full text Add to dashboard Cite

ABSTRACT. In this study, bovine β 2 -m was purified from urine by ion-exchange chromatography and gel chromatography, and the characteristics were compared with those of colostral β 2 -m by the immunological reactivity, isoelectric points, peptide map, and amino acid sequence. The characteristics of purified urinary β 2 -m were consistent with those of the colostral β 2 -m. The urinary and colostral β 2 -m possessed the same polypeptide chain consisting of 98 amino acids, and its molecular weight is 11.8 kDa. Furthermore, four isoforms of β 2 -m were found. The isoelectric points were different from each other. KEY WORDS: amino acid sequence, bovine β 2 -microglobulin, isoform, peptide map, purification.J. Vet. Med. Sci. 62(8): 867-874, 2000 β 2 -microglobulin (β 2 -m) is a single polypeptide chain of 100 amino acids (molecular weight = 11.800), which is found in body fluids and on the surfaces of all nucleated cells [7]. It is also the light chain of the class I major histocompatibility antigens. Based on amino acid sequences, β 2 -m is homologous to the α 3 -domains of the heavy chain for the class I histocompatibility antigens and to the immunoglobulin constant domains [21,23].Human β 2 -m is used for evaluation of kidney function, because β 2 -m is eliminated by renal glomerular filtration and subsequently reabsorbed almost completely into the proximal tubule cells, where it is metabolised [12]. Elevated serum levels of human β 2 -m reflect glomerular dysfunction, and its increased concentration in urine reflects proximal tubule disorder [31]. Recently, it has been found that the concentration of serum β 2 -m increased in association with various tumours [20]. Immunological studies have reported that β 2 -m may be involved in antigenic recognition of T-lymphocytes [4,26]. In hemodialysis, it was found that β 2 -m plays the role of an amyloid forming protein, and is one of the causes of kidney amyloidosis in long time hemodialysis treatment. In other species, a relationship between β 2 -m and kidney function, and between its protein and the immunological system including various tumors, have been reported, but few clinical studies are reported. β 2 -m was first isolated from urine of patients with chronic cadmium poisoning [2]. It was later isolated from the urine of various animals (e.g. rat, rabbit, and guinea pig) with renal dysfunction [3,5,17]. In ruminant (bovine and goat) β 2 -m was isolated from milk [8,10]. The isolation of bovine β 2 -m was carried out first by Gloves and Greenberg from colostrum [8]. In a previous study, we demonstrated that a low molecular protein increased in the urine of bovine with renal dysfunction, however, we did not identify this protein [15]. Thus, in this study, we attempted to isolate bovine β 2 -m from urine, and compare it with the biochemical characteristics of β 2 -m from colostrum in order to confirm that this protein is not a metabolite of β 2 -m. MATERIALS AND METHODS Animals:Five healthy female Holstein cows were used in this experiment. Three of them were use...

show abstract

“…We also tested the effects of 2 anti-p2m mAb, M18 [28] and BBMl [29], and found that these mAb fully blocked [3H]dThd incorporation by whole PBL cultivated with the several CD3 mAb we tested (Table 1). However, we observed no blocking effects when whole PBL were cultivated with mitogenic pairs of CD2 mAb, including GT2 + T l l l (Table 1).…”

Section: Anti-pgn Mab Fured To Ac Inhibit T Cell Activation Via Cd3mentioning

confidence: 96%

“…Anti-HLA class I mAb directed against the heavy chain were W6132 (IgG,) [26], B10.8 (IgG3) [27], B10.22 (IgG3) [27] and B1.23.2 (IgG2,). Anti-p2-microglobulin (P2m) mAb were M18 (IgG,,) [28] and BBMl (IgGZb) [29]. In some experiments we used Fab or F(ab'), fragments of W6/32 mAb prepared, respectively, with a papain or pepsin digestion of purified mAb, and recovered by high performance liquid chromatography (HPLC) as described [30].…”

Section: Mabmentioning

confidence: 99%

The required interaction between monocytes and peripheral blood T lymphocytes (T‐PBL) upon activation via CD2 or CD3. Role of HLA class I molecules from accessory cells and the differential response of T‐PBL subsets

et al. 1988

View full text Add to dashboard Cite

Previously, we have shown that paraformaldehyde-fixed monocytes are able to fully complement, in terms of [3H]dThd incorporation, a primary stimulus delivered to purified T cells by monoclonal antibodies (mAb) reacting with CD3 or CD2 molecules. Here, we show that depending on the stimulus used (CD3 mAb or different pairs of CD2 mAb) HLA class I molecules from monocytes are directly involved in complementary signals provided to T cells. This was evidenced by the following observations: (a) mAb reacting with the heavy or light chain of class I molecules, or their Fab fragments, completely blocked proliferation of peripheral blood lymphocytes (PBL) activated by CD3 mAb; (b) mAb against the heavy chain of HLA class I but not against beta 2-microglobulin partially blocked (approximately equal to 50%) PBL activation by the CD2 "GT2 + T111" mAb pair but did not block activation by CD2 "D66 + T111" mAb; (c) this pattern of inhibition was observed when anti-class I mAb were used in the soluble phase or when they were bound to monocytes subsequently fixed with paraformaldehyde and cultivated with purified autologous T cells; (d) fixed monocytes are able to restore interleukin (IL) 2 receptor expression on purified T cells stimulated by CD3 mAb or CD2 "GT2 + T111", contrary to anti-HLA class I mAb-pretreated monocytes. The inhibitory effects of anti-HLA class I mAb bound to monocytes were not found to be reversed by recombinant IL2 or recombinant IL1. We assume that HLA class I would be involved in two or more signals delivered to T cells by monocytes, the requirement in those signals depending on the initial stimulus applied to T cells.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

Monoclonal antibodies as a tool for phylogenetic studies of major histocompatibility antigens and ? 2-microglobulin

Cited by 47 publications

References 14 publications

Bovine cytotoxic T-cell clones specific for cells infected with the protozoan parasite Theileria parva: parasite strain specificity and class I major histocompatibility complex restriction.

Bovine cytotoxic T-cell clones specific for cells infected with the protozoan parasite Theileria parva: parasite strain specificity and class I major histocompatibility complex restriction.

Purification of Bovine Urinary .BETA.2-Microglobulin and Its Biochemical Characteristics.

The required interaction between monocytes and peripheral blood T lymphocytes (T‐PBL) upon activation via CD2 or CD3. Role of HLA class I molecules from accessory cells and the differential response of T‐PBL subsets

Contact Info

Product

Resources

About