Monoclonal Anti-Hla-B27 Antibody (B27m1): Production and Lack of Detectable Typing Difference Between Patients With Ankylosing Spondylitis, Reiter's Syndrome, and Normal Controls

Grumet, F. Carl; Fendly, BrianM.; Engleman, E G

doi:10.1016/s0140-6736(81)90358-5

Cited by 74 publications

(20 citation statements)

References 15 publications

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“…This is in accord with an examination of HLA and BF data by Migone et a1 (16). In this regard, we note that the first mouse monoclonal anti-B27 antibody described by Grumet et a1 (17) was also unable to split B27 into disease-associated and healthy variants.…”

supporting

confidence: 91%

HLA‐B27 haplotypes in family studies of ankylosing spondylitis

Lochead¹,

Chalmers²,

Marshall³

et al. 1983

Arthritis & Rheumatism

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Although HLA-B27 carries a high relative risk for development of ankylosing spondylitis (AS), most B27 positive individuals do not have spondylitis. One interpretation of this observation is that there may be 2 types of B27, 1 which carries the risk factor and 1 which does not. If this were the case, then with the help of markers closely linked to HLA-B, it might be possible to detect differences between the B27 haplotypes in AS patients and those in healthy probands. We studied 197 members of 18 families with known AS and 110 members of 19 families in which HLA-B27 was present without any known inflammatory spinal disease. HLA antigens A, B, and C and alleles of complement components C2, C4, and Factor B and glyoxalase-1 were determined in all cases. Detailed haplotypes were assigned and their associations with development of the disease were examined. We were unable to identify any distinct HLA-B27 haplotype associated with AS; 2 common haplotypes and several miscellaneous ones were found in both groups. Thinking that the development of AS might be influenced by the other, non-B27 haplotype, we analyzed this and found that there was no detectable influence. The data do not contradict the notion that B27 in whites is a single entity and is itself the susceptibility factor predisposing to the development of ankylosing spondylitis.

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supporting

confidence: 91%

HLA‐B27 haplotypes in family studies of ankylosing spondylitis

Lochead¹,

Chalmers²,

Marshall³

et al. 1983

Arthritis & Rheumatism

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“…Attempts to perform immunochemical studies with the one available murine anti-HLA-B27 monoclonal antibody, B27ml (16) When HLA-B27 molecules were studied using 2-D gel, extensive charge heterogeneity was noted in the 45,000-dalton heavy chain. This degree of charge heterogeneity was very similar to that noted when detergent-solubilized H-2D, K, and L molecules were analyzed by the same technique (20,21).…”

Section: Discussionmentioning

confidence: 99%

Structural Identity of Human Histocompatibility Leukocyte Antigen-B27 Molecules from Patients with Ankylosing Spondylitis and Normal Individuals

Karr¹,

Hahn²,

Schwartz³

1982

J. Clin. Invest.

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A B S T R A C T Although the association between human histocompatibility leukocyte antigen (HLA) B27 and ankylosing spondylitis is the prototype of HLAdisease association, the mechanism underlying these associations has not been determined. We have investigated the possibility that the B27 molecules from patients with ankylosing spondylitis are different from those of normals, and only the "different" molecules predispose the individual to disease. Biosynthetically radiolabeled HLA-B27 molecules from patients with ankylosing spondylitis and normal individuals were compared by two-dimensional gel electrophoresis and tryptic peptide mapping with high pressure liquid chromatography. Extensive charge heterogeneity in the 45,000-dalton heavy chain was detected when B27 molecules were analyzed by two-dimensional gel electrophoresis; the charge heterogeneity was reduced, but not eliminated, when the B27 molecules were treated with neuraminidase to remove sialic acid residues before analysis. No structural difference in the B27 molecules from an ankylosing spondylitis patient and a normal individual were detected by two-dimensional gel electrophoresis. Analysis of [3H]leucine-labeled and[3H]arginine-labeled tryptic peptides and chymotryptic peptides of the trypsin insoluble material by reverse-phase high pressure liquid chromatography revealed identity of the B27 molecules from ankylosing spondylitis patients and normal individuals. These studies indicate that development of akylosing spondylitis in only some B27 positive individuals is not at-

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“…Hybridomas producing the following Abs: A1(IgG2a), anti-Ly-49A (27); MK-D6(IgG2a), anti-IA d (28); 11-4.1(IgG2a), anti-H-2K k (29); 14-4-4S(IgG2a) anti-IE k (30); BBM.1(IgG2b), anti-human ␤ 2 -microglobulin (31); B27 M1(IgG2a), anti-HLA-B7,27 (32) (34,35); and 2.4G2(rat IgG2b) anti-mouse Fc-␥ receptor (36); were obtained from American Type Culture Collection (Manassas, VA), except A1, which was obtained from Dr. James Allison (University of California, Berkeley, CA). Abs were prepared by ammonium sulfate precipitation and PBS dialysis of tissue culture supernatants obtained from hybridomas grown in protein-free hybridoma medium.…”

Section: Hybridomas and Absmentioning

confidence: 99%

Ly-49P Activates NK-Mediated Lysis by Recognizing H-2Dd 1

Silver

Gong

Chang

et al. 2000

The Journal of Immunology

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Little is known regarding the ligand specificity of Ly-49 activating receptor subfamily members expressed by NK cells. A new Ly-49 activating receptor related to Ly-49A in its extracellular domain, designated Ly-49P, was recently cloned from 129 strain mice. We independently cloned an apparent allele of Ly-49P expressed by nonobese diabetic and nonobese diabetes-resistant mouse strain NK cells. We found it to be reactive with the A1 Ab thought to recognize a polymorphic epitope expressed only by the Ly-49A inhibitory receptor of the C57BL/6 strain. Rat RNK-16 cells transfected with Ly-49P mediated reverse Ab-dependent cellular cytotoxicity of FcR-positive target cells, indicating that Ly-49P can activate NK-mediated lysis. We determined that RNK-16 lysis of Con A blasts induced by Ly-49P was MHC dependent, resulting in efficient lysis of H-2Dd-bearing targets. We found that the Dd α1/α2 domain is required for Ly-49P-mediated RNK-16 activation, as determined by exon shuffling and transfection. Thus, Ly-49P is the second activating Ly-49 receptor demonstrated to induce NK cytotoxicity by recognizing a class I MHC molecule.

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Monoclonal Anti-Hla-B27 Antibody (B27m1): Production and Lack of Detectable Typing Difference Between Patients With Ankylosing Spondylitis, Reiter's Syndrome, and Normal Controls

Cited by 74 publications

References 15 publications

HLA‐B27 haplotypes in family studies of ankylosing spondylitis

HLA‐B27 haplotypes in family studies of ankylosing spondylitis

Structural Identity of Human Histocompatibility Leukocyte Antigen-B27 Molecules from Patients with Ankylosing Spondylitis and Normal Individuals

Ly-49P Activates NK-Mediated Lysis by Recognizing H-2Dd 1

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