CD antigens 2001

CD antigens 2001 Abstract: This paper reviews the Seventh Human Leucocyte Differentiation Antigen (HLDA7) workshop. Due to the limitations of “blind” antibody screening, which had been evident at the previous meeting in 1996, participants at HLDA7 adopted a more selective approach to the choice of antibodies by identifying new CD specificities. This resulted in the addition of more than 80 new CD specificities. Plans for the eighth and subsequent workshops are also previewed. J. Leukoc. Biol. 70: 685– 690; 2001. Key Words: HLDA workshops z leukocyte molecules THE SEVENTH HLDA WORKSHOP Aims and approaches The Limitations of “Blind” Antibody Screening It was apparent at HLDA6 (Kobe, Japan, 1996) that the technique of detecting molecular entities by screening coded panels of monoclonal antibodies against human cells was obsolete. Antibodies to the most immunogenic molecules had already been produced, and fewer laboratories than in the earlier days of this research were prepared to devote resources to raising new antibodies, because the probability of finding novel reagents had become increasingly less likely. As a consequence, many antibodies at the sixth workshop were reagents (submitted by laboratories that were not equipped to characterize them) that proved to be of known specificity. Selection of Antibodies THE TRADITION OF HLDA WORKSHOPS The process of categorizing the antigenic molecules and epitopes associated with human white blood cells via the collaborative study of monoclonal antibodies dates back to the early 1980s, when the first Human Leucocyte Differentiation Antigen (HLDA) workshop was held in Paris. This initial meeting agreed on and listed only 15 of these molecular entities, but it also created a basis for an international nomenclature of leukocyte molecules (the CD scheme) and provided a forum for reporting studies on the function and practical relevance of these molecules. Six more HLDA meetings have been held since then, the most recent of which (“HLDA7”) convened last year in Harrogate, United Kingdom. The published proceedings of HLDA7 will be available later this year [1]. With these considerations in mind, the seventh workshop adopted a different approach: instead of screening poorly characterized antibodies, participants selected (and actively solicited) reagents for which at least some molecular data were already available. There are a substantial number of monoclonal antibodies reactive with leukocyte-associated molecules that do not meet the traditional criterion for establishing a new CD specificity (i.e., the existence of at least two independent antibodies of the same specificity). This rule dates from the first HLDA workshop two decades ago; since then, biochemical and molecular biological techniques for characterizing the targets of new antibodies have come to be widely used. Consequently, Correspondence: Prof. David Y. Mason, Haematology Department, John Radcliffe Hospital, Oxford OX3 9DU, U.K. E-mail: [email protected] Received August 2, 2001; accepted August 4, 2001. Journal of Leukocyte Biology Volume 70, November 2001 685 Downloaded from https://academic.oup.com/jleukbio/article/70/5/685/7092964 by guest on 01 April 2023 David Mason,* Pascale André,† Armand Bensussan,‡ Chris Buckley,§ Curt Civin,i Edward Clark,# Masja de Haas,** Sanna Goyert,†† Martin Hadam,‡‡ Derek Hart,§§ Václav Hǒrejšı́,ii Stefan Meuer,## James Morrissey,*** Reinhard Schwartz-Albiez,††† Stephen Shaw,‡‡‡ David Simmons,§§§ Mariagrazia Uguccioni,iii Ellen van der Schoot,** Eric Vivier,† and Heddy Zola### *Haematology Department, John Radcliffe Hospital, Oxford, §Division of Immunity and Infection, MRC Centre for Immune Regulation, Birmingham, and §§§Celltech R&D Ltd., Great Abington, Cambridge, United Kingdom; †Centre d’Immunologie, INSERM-CNRS de Marseille Luminy, Marseille, and ‡INSERM Institut National de la Santé et de la Recherche Medicale, Creteil, France; iJohns Hopkins Comprehensive Cancer Center, Baltimore, Maryland; # Department of Microbiology, University of Washington, Seattle; **Central Laboratory of the Netherlands, Department of Experimental Immunohematology, Amsterdam, The Netherlands; ††Laboratory of Molecular Hematology/Division of Molecular Medicine, Cornell University Medical College, Manhasset, New York; ‡‡ Kinderklinik-Medizinische Hochschule, Hannover, and ##Institut für Immunologie, Ruprecht-Karls Universität and ††† German Cancer Research Centre, Tumor Immunology, Heidelberg, Germany; §§Mater Medical Research Institute, Mater Hospital, South Brisbane, and ###Child Health Research Institute, Women’s & Children’s Hospital, North Adelaide, SA, Australia; iiInstitute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic; ***University of Illinois College of Medicine, Urbana; ‡‡‡National Institute of Health, Bethesda, Maryland; and iiiInstitute for Research in Biomedicine, Bellinzona, Switzerland TABLE 1. CD designation 686 Name Section Sulfated CD15 GD3 9-O-acetyl-GD3 7-O-acetyl-GD3 Lactosamines a-2,6-Sialylated lactosamines (formerly CDw75 and CDw76) ILT/LIR family (see Table 2) MPL, TPO R PRR1/Nectin1 PRR2 AC133 TACE/ADAM17 KIR family (see Table 2) NKG2A BY55 PEN5 Discoidin domain R (DDR1) RHAMM Sialoadhesin Siglec-5 L1 SIRP a Blood group H type 2 Lewis y Tn Sialyl-Tn TF NB1 Fas ligand Vpre-B l-5 RP105 CXCR3 CXCR4 CCR5 CCR7 OX2 EPC R Tie2 (Tek) NPP3/PDNP3 Macrophage scavenger R DEC205 Macrophage mannose R Langerin DC-LAMP DC-SIGN IL-10 R IL-12 R IL-13 R a1 IL-13 R a2 IL-17 R Insulin R IGF1 R Mannose-6-phosphate/IGF2 R LAG-3 g-Glutamyl transferase Leu-13 DNAM-1 (PTA1) MUC.1 Melanotransferrin Ly9 Prion protein TALLA-1/A15 VESP R Band 3 Fy-glycoprotein (DARC) Carbohydrate structures Carbohydrate structures Carbohydrate structures Carbohydrate structures Carbohydrate structures Carbohydrate structures Dendritic cells Platelets Myeloid cells Myeloid cells Stem/progenitor cells Adhesion structures NK cells NK cells T cells NK cells Adhesion structures Adhesion structures Adhesion structures Adhesion structures Adhesion structures Adhesion structures Carbohydrate structures Carbohydrate structures Carbohydrate structures Carbohydrate structures Carbohydrate structures Myeloid cells Cytokine/chemokine receptors B cells B cells B cells Cytokine/chemokine receptors Cytokine/chemokine receptors Cytokine/chemokine receptors Cytokine/chemokine receptors Non-lineage molecules Endothelial cells Endothelial cells Myeloid cells Myeloid cells Dendritic cells Dendritic cells Dendritic cells Dendritic cells Dendritic cells Cytokine/chemokine receptors Cytokine/chemokine receptors Cytokine/chemokine receptors Cytokine/chemokine receptors Cytokine/chemokine receptors Non-lineage molecules Non-lineage molecules Non-lineage molecules Non-lineage molecules Non-lineage molecules Non-lineage molecules T cells Non-lineage molecules Non-lineage molecules Non-lineage molecules Non-lineage molecules Non-lineage molecules Non-lineage molecules Erythroid cells Erythroid cells Journal of Leukocyte Biology Volume 70, November 2001 Locus link 4352 5818 5819 8842 6868 3821 11126 6404 780 3161 6614 8778 3897 8194 356 7441 3543 4064 2833 7852 1234 1236 4345 10544 7010 5169 4481 4065 4360 50489 30385 3587; 3588 3594 3597 3598 23765 3643 3480 3482 3902 2678 8519 10666 4582 4241 4063 5621 7102 10154 6521 2532 http://www.jleukbio.org Downloaded from https://academic.oup.com/jleukbio/article/70/5/685/7092964 by guest on 01 April 2023 CD15u CD60a CD60b CD60c CD75 CD75s CD85 CD110 CD111 CD112 CD133 CD156b CD158 CD159a CD160 CD162R CD167a CD168 CD169 CD170 CD171 CD172a CD173 CD174 CD175 CD175s CD176 CD177 CD178 CD179a CD179b CD180 CD183 CD184 CD195 CDw197 CD200 CD201 CD202b CD203c CD204 CD205 CD206 CD207 CD208 CD209 CDw210 CD212 CD213a1 CD213a2 CDw217 CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD231 CD232 CD233 CD234 New CD Designations TABLE 1. CD designation Name Section Glycophorin A Glycophorin B Glycophorin A/B cross-reactive mAbs Glycophorin C/D Glycophorin C Kell B-CAM Rh30CE Rh30D Rh30D/CE crossreactive mAbs RhAg ICAM-4 MDR-1 2B4 p220/240 Anaplastic lymphoma kinase Zeta chain it is now considered appropriate to establish a CD designation for a molecule if its gene has been cloned and at least one specific monoclonal antibody has been studied in the workshop. New Workshop Sections Four new workshop sections were introduced at HLDA7, adding to the traditional list from previous meetings; those new sections included dendritic cells, stem/progenitor cells, erythroid cells, and carbohydrate structures. Although it has been recognized for many years that monoclonal antibodies reactive with human leukocytes can be specific for carbohydrate epitopes (e.g., the carbohydrate CD category CD15 was identified at the first workshop), they had not received specific attention in any workshop before HLDA7. Although the inclusion of erythroid molecules might seem out of place in a leukocyte workshop, it was justified by the number of molecules shared between white and red blood cells (e.g., cytokine receptors) that hint at unexplored functions of red cells. The yield of new CD specificities in the seventh HLDA workshop The more active approach to the identification of new CD specificities represents a break with tradition, but the results have justified the new approach, because well over 80 new entities have been added to the list. This compares favorably with previous workshops (which added an average of ,30 CD specificities per workshop), and, to a large extent, avoids the laborious screening in multiple laboratories of antibodies that prove to be directed against known CD molecules. Tables 1 and 2 list the new specificities established at the seventh workshop. Full details will be found in the forthcoming proceedings publication [1]. Molecular, functional, and other data can be found for many of these new specificities at the “Protein Reviews on the Web” (PROW) web site (http:// www.ncbi.nlm.nih.gov/prow/). Locus link Erythroid cells Erythroid cells Erythroid cells Erythroid cells Erythroid cells Erythroid cells Erythroid cells Erythroid cells Erythroid cells Erythroid cells Erythroid cells Erythroid cells Stem/progenitor cells NK cells T cells T cells T cells 2993 2994 2995 3792 4059 6006 6007 6005 3386 51744 238 919 THE EIGHTH WORKSHOP Plans for the eighth workshop are progressing well. The meeting will convene in Adelaide, Australia, in 2004 under the aegis of Prof. H. Zola (see http://www.hlda8.org). It is sometimes assumed that the catalog of surface molecules associated with human hemopoietic cells is now essentially complete, but TABLE 2. New CD Nomenclature for ILT/LIR and KIR Molecules CD designation Name The ILT/LIR family CD85a CD85b CD85c CD85d CD85e CD85f CD85g CD85h CD85i CD85j CD85k CD85l CD85m The KIR family CD158z CD158b1 and CD158b2 CD158a CD158c CD158d CD158e1 and CD158e2 CD158f CD158g CD158h CD158i CD158j CD158k ILT5/LIR3 ILT8 LIR8 ILT4/LIR2, MIR10 ILT6/LIR4 ILT11 ILT7 ILT1/LIR7 LIR6 ILT2/LIR1, MIR7 ILT3/LIR5 ILT9 ILT10 KIR3DL7/KIRC1 KIR2DL2/p58.2 and KIR2DL3/p58.3 KIR2DL1/p58.1 KIR2DS6/KIRX KIR2DL4 KIR3DL1/p70 and KIR3DS1/p70 KIR2DL5 KIR2DS5 KIR2DS1/p50.1 KIR2DS4/p50.3 KIR2DS2/p50.2 KIR3DL2/p140 For further details of this classification, based on the position of the genes on chromosome 19q;13.4 from centromeric to telomeric loci, see ref. 2. Mason et al. Seventh HLDA Workshop 687 Downloaded from https://academic.oup.com/jleukbio/article/70/5/685/7092964 by guest on 01 April 2023 CD235a CD235b CD235ab CD236 CD236R CD238 CD239 CD240CE CD240D CD240DCE CD241 CD242 CD243 CD244 CD245 CD246 CD247 (Continued) TABLE 3. Moleculea Identified after antibody production AM-3K antigen BDCA-2, BDCA-3, and BDCA-4 antigens BENE CMRF-44 CMRF-56 H47 antigen Hal-1 Cell typesb Molecular size 70 and 120 kDa Macrophages Dendritic cells 17 kDa Endothelium ? 95 kDa 100 kDa (non red.) and 120 kDa (reduced) 200 kDa (100 kDa) Dendritic cells Dendritic cells T cells and most NK, B cells and monocytes 5 6 7 8 Novel member of the killer cell lectin-like receptor gene family, encoded by KLRF1 gene. Triggers NK cell cytotoxicity. Mediates lymphocyteendothelial adhesion. Has monoamine oxidase activity Stimulates growth of plasma cells 11,12 TNFR family member. Receptor for TALL-1 and APRIL New member of B7 family. Binds ICOS on activated T cells Novel C-type lectin-like receptor with cytoplasmic tyrosine-based motif Novel Ig superfamily receptors. CMRF-35H Contains 3 cytoplasmic tyrosine-based motifs Novel receptor belonging to CD2 subset of Ig superfamily Novel protein containing seven putative transmembrane domains. Novel EGF-TM7 molecule. Interacts with a surface ligand on myeloid cells 16,17 90 kDa Endothelium Wue-1 antigen 94 kDa Plasma cells 184 aa B cells B7-H2 302 aa Dendritic cells CLEC-1 280 aa Dendritic cells CMRF-35A 224 aa CMRF-35H 300 aa NK cells, neutrophils, monocytes, dendritic cells and subset of T lymphocytes NK cells DC-STAMP 470 aa Dendritic cells EMR3 652 aa Flt-1 (VEGFR-1) GPRv53 390 aa Mainly leucocyte restricted. Highest levels on neutrophils, monocytes, and macrophages Endothelial cells, monocytes Leucocytes Subpopulations of B cells M160 1,453 aa Macrophages MARCO 520 aa Macrophages 688 3 4 NK cells and CD56-positive T cells VAP-1 IRTA1 and IRTA2 Identifies subsets of dendritic cells “Raft-associated” member of MAL family. Interacts with caveolin-1 Differentiated/activated Differentiated/activated ? Involved in T cell activation ? New lymphoma marker NKp80 CS1 Reference(s) T cells, EBV-transformed B cells, myelomonocytic cells, anaplastic large cell lymphoma LGL and LAK cells 120 kDa and 110 1 140 kDa, respectively 80-kDa dimer Identified via gene cloning BCMA Commentsc Journal of Leukocyte Biology Volume 70, November 2001 9 10 Identified by gene cloning. G-protein-coupled histamine receptor Homologous to the Fc and inhibitory receptor families New member of scavenger receptor cysteine-rich superfamily Class A scavenger receptor. Involved in bacterial clearance in vivo. 13,14 15 18 19 20,21 22 23 24 25 26 27 28 29,30 http://www.jleukbio.org Downloaded from https://academic.oup.com/jleukbio/article/70/5/685/7092964 by guest on 01 April 2023 LAK1 and LAK2 antigens Examples of Possible Future CD Specificities TABLE 3. Moleculea TACI TREM-1 and TREM-2 Cell typesb Molecular size 293 aa (Continued) Commentsc B cells TNFR family member. Receptor for TALL-1 and APRIL Novel Ig superfamily receptors. TREM-1 triggers neutrophil secretion (e.g., IL-8) and degranulation. TREM-2 activates macrophages. Both associate with DAP12. Neutrophils and subset of monocytes (TREM-1) and macrophages (TREM-2) Reference(s) 31 32,33 there is abundant evidence in the literature for novel surface molecules that merit study at the next workshop and that could provide the basis for new CD designations. Table 3 comprises a list of potential new molecules reported after the production of monoclonal antibodies and also a more extensive list of surface molecules identified via gene cloning. In most instances, no antibodies are available against the putative new leukocyte/endothelial markers in this latter group. Specific and well-characterized reagents, whether monoclonal or polyclonal, are needed not only for detecting these new “virtual” molecules, but also for defining functional domains, for characterizing three-dimensional protein structure, and for analyzing protein-protein interactions. Cloning of gene sequences often reveals multiple members of new or existing molecular families (e.g., the Toll-like receptors) and might identify surface receptors that bind more than one ligand or vice versa (e.g., the TALL-1 and APRIL ligands for transmembrane activator and CAML interacting protein and BCMA). Furthermore, several leukocyte-associated markers have been cloned from mice and other species, and almost all will have human homologues. The eighth workshop will provide a forum for a range of antibodybased studies relating to this accumulating corpus of genomic and proteomic data. As in the seventh workshop in which four new sections were added, it might be possible to include neuronal cells in the eighth workshop. Many neuronal cells express cell surface proteins found on leukocytes and vice versa (e.g., CD56, CD100, CD168, and CD171). Furthermore, the guidance cues used by neuronal cells share similarities to those involved in leukocyte extravasation, so the expression of these molecules in common might reflect shared biological processes. It might also be noted that other molecules such as the mucins, thought to be primarily associated with epithelial cells, are now being described on leukocytes. 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