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CD Antigens 2001

2002; Elsevier BV; Volume: 15; Issue: 1 Linguagem: Inglês

10.1038/modpathol.3880492

1530-0285

David Y. Mason, Pascale André, Armand Bensussan, Christopher D. Buckley, Curt I. Civin, Edward A. Clark, Masja de Haas, Sanna M. Goyert, M. Hadam, Derek N.J. Hart, Václav Hořejšı́, Stefan Meuer, James H. Morrissey, Reinhard Schwartz‐Albiez, Stephen Shaw, David Simmons, Mariagrazia Uguccioni, C. Ellen van der Schoot, Éric Vivier, Heddy Zola,

Glycosylation and Glycoproteins Research

The process of categorizing the antigenic molecules and epitopes associated with human white cells, via the collaborative study of monoclonal antibodies, dates back to the early 1980s, when the first HLDA (Human Leukocyte Differentiation Antigen) Workshop was held in Paris. This initial meeting listed only 15 agreed molecular entities, but it created an internationally agreed basis for the nomenclature of leukocyte molecules (the CD scheme) and also provided a forum for reporting studies on their function and practical relevance. A further six HLDA meetings have been held since the first Paris meeting. The most recent of these (HLDA7) took place last year in Harrogate, UK, and the proceedings of the meeting will be published later this year (Leucocyte Typing VII, Oxford University Press). It was apparent at the previous meeting, HLDA6, held in Kobe, Japan, in 1996, that the technique of detecting molecular entities by screening coded panels of monoclonal antibodies against human cells was becoming obsolescent. Antibodies to the most immunogenic molecules had already been produced, and fewer laboratories than in the early days were prepared to devote resources to raising new antibodies because the probability of finding novel reagents becomes ever less likely. In consequence, many antibodies in the 6th Workshop were reagents (submitted by laboratories that were not equipped to characterize them) that proved to be of known specificity. With these considerations in mind, the 7th Workshop adopted a different approach: instead of screening poorly characterized antibodies, reagents were selected (and actively solicited) for which at least some molecular data were already available. A substantial number of monoclonal antibodies reactive with leukocyte-associated molecules exist 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 that time, biochemical and molecular biological techniques for characterizing the targets of new antibodies have come to be widely used. Consequently, 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. Four new sections were introduced in the 7th HLDA Workshop to add to the traditional list from past meetings: namely, 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. The inclusion of erythroid molecules, although it may seem out of place in a “Leukocyte Workshop,” was justified by the number of molecules shared between white and red cells (e.g., cytokine receptors) that hint at unexplored functions of red cells. This more active approach to the identification of new CD specificities represented a break with tradition, but the results justified the new approach because a total of well over 80 new entities were added to the list of CD specificities. This compares favorably with previous Workshops (an average of less than 30 CD specificities per Workshop), and it also largely avoided 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 7th Workshop. Full details will be found in Leucocyte Typing VII, and molecular, functional, and other data can be found for many of these new specificities on the Website for “Protein Reviews on the Web” (www.ncbi.nlm.nih.gov/prow/).TABLE 1New CD DesignationsCD DesignationNameSectionLocus LinkCD15uSulphated CD15Carbohydrate structuresCD60aGD3Carbohydrate structuresCD60b9-O-acetyl-GD3Carbohydrate structuresCD60c7-O-acetyl-GD3Carbohydrate structuresCD75LactosaminesCarbohydrate structuresCD75sAlpha-2,6-sialylated lactosamines (formerly CDw75 and CDw76)Carbohydrate structuresCD85ILT/LIR family (see Table 2)Dendritic cellsCD110MPL, TPO RPlatelets4352CD111PRR1/Nectin1Myeloid cells5818CD112PRR2Myeloid cells5819CD133AC133Stem/progenitor cells8842CD156bTACE/ADAM17Adhesion structures6868CD158KIR family (see Table 2)NK cellsCD159aNKG2ANK cells3821CD160BY55T cells11126CD162RPEN5NK cells6404CD167aDiscoidin domain R (DDR1)Adhesion structures780CD168RHAMMAdhesion structures3161CD169SialoadhesinAdhesion structures6614CD170Siglec-5Adhesion structures8778CD171L1Adhesion structures3897CD172aSIRPαAdhesion structures8194CD173Blood group H type 2Carbohydrate structuresCD174Lewis yCarbohydrate structuresCD175TnCarbohydrate structuresCD175sSialyl-TnCarbohydrate structuresCD176TFCarbohydrate structuresCD177NB1Myeloid cellsCD178Fas ligandCytokine/chemokine receptors356CD179aVpre-BB cells7441CD179bLambda 5B cells3543CD180RP105B cells4064CD183CXCR3Cytokine/chemokine receptors2833CD184CXCR4Cytokine/chemokine receptors7852CD195CCR5Cytokine/chemokine receptors1234CDw197CCR7Cytokine/chemokine receptors1236CD200OX2Nonlineage molecules4345CD201EPC REndothelial cells10544CD202bTie2 (Tek)Endothelial cells7010CD203cNPP3/PDNP3Myeloid cells5169CD204Macrophage scavenger RMyeloid cells4481CD205DEC205Dendritic cells4065CD206Macrophage mannose RDendritic cells4360CD207LangerinDendritic cells50489CD208DC-LAMPDendritic cellsCD209DC-SIGNDendritic cells30385CDw210IL-10 RCytokine/chemokine receptors3587; 3588CD212IL-12 RCytokine/chemokine receptors3594CD213a1IL-13 R α 1Cytokine/chemokine receptors3597CD213a2IL-13 R α 2Cytokine/chemokine receptors3598CDw217IL-17 RCytokine/chemokine receptors23765CD220Insulin RNonlineage molecules3643CD221IGF1 RNonlineage molecules3480CD222Mannose-6-phosphate/IGF2 RNonlineage molecules3482CD223LAG-3Nonlineage molecules3902CD224γ-glutamyl transferaseNonlineage molecules2678CD225Leu13Nonlineage molecules8519CD226DNAM-1 (PTA1)T cells10666CD227MUC.1Nonlineage molecules4582CD228MelanotransferrinNonlineage molecules4241CD229Ly9Nonlineage molecules4063CD230Prion proteinNonlineage molecules5621CD231TALLA-1/A15Nonlineage molecules7102CD232VESP RNonlineage molecules10154CD233Band 3Erythroid cells6521CD234Fy-glycoprotein (DARC)Erythroid cells2532CD235aGlycophorin AErythroid cells2993CD235bGlycophorin BErythroid cells2994CD235abGlycophorin A/B crossreactive mabsErythroid cellsCD236Glycophorin C/DErythroid cellsCD236RGlycophorin CErythroid cells2995CD238KellErythroid cells3792CD239B-CAMErythroid cells4059CD240CERh30CEErythroid cells6006CD240DRh30DErythroid cells6007CD240DCERh30D/CE cross-reactive mabsErythroid cellsCD241RhAgErythroid cells6005CD242ICAM-4Erythroid cells3386CD243MDR-1Stem/progenitor cellsCD2442B4NK cells51744CD245p220/240T cellsCD246Anaplastic lymphoma kinaseT cells238CD247ζ chainT cells919 Open table in a new tab TABLE 2New CD Nomenclature for ILT/LIR and KIR MoleculesCD DesignationNameThe ILT/LIR family CD85aILT5/LIR3 CD85bILT8 CD85cLIR8 CD85dILT4/LIR2, MIR10 CD85eILT6/LIR4 CD85fILT11 CD85gILT7 CD85hILT1/LIR7 CD85iLIR6 CD85jILT2/LIR1, MIR7 CD85kILT3/LIR5 CD85lILT9 CD85mILT10The KIR family CD158zKIR3DL7/KIRC1 CD158b1 and CD158b2KIR2DL2/p58.2 and KIR2DL3/p58.3 CD158aKIR2DL1/p58.1 CD158cKIR2DS6/KIRX CD158dKIR2DL4 CD158e1 and CD158e2KIR3DL1/p70 and KIR3DS1/p70 CD158fKIR2DL5 CD158gKIR2DS5 CD158hKIR2DS1/p50.1 CD158iKIR2DS4/p50.3 CD158jKIR2DS2/p50.2 CD158kKIR3DL2/p140For further details of this classification, based on the position of the genes on chromosome 19q;13.4 from centromeric to telomeric loci, see André et al. (1André P Biassoni R Colonna M Cosman D Lanier LL Long EO New nomenclature for MHC receptors.Nat Immunol. 2001; 2: 66110.1038/90589Crossref PubMed Scopus (83) Google Scholar). Open table in a new tab For further details of this classification, based on the position of the genes on chromosome 19q;13.4 from centromeric to telomeric loci, see André et al. (1André P Biassoni R Colonna M Cosman D Lanier LL Long EO New nomenclature for MHC receptors.Nat Immunol. 2001; 2: 66110.1038/90589Crossref PubMed Scopus (83) Google Scholar). Plans are well advanced for the 8th Workshop, to be organized in Adelaide in 2004 under the aegis of Prof. H. Zola (see www.hlda8.org). It is sometimes assumed that the catalog of surface molecules associated with human hemopoietic cells is now essentially complete, but there is abundant evidence in the literature for novel surface molecules that would 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 by 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 3D protein structure, and for analyzing protein–protein interactions. It may be added that cloning of gene sequences often reveals multiple members of new or existing molecular families (e.g., the Toll-like receptors) and may identify surface receptors that bind more than one ligand or vice versa (e.g., the TALL-1 and APRIL ligands for TACI and BCMA). Furthermore, a number of leukocyte-associated markers have been cloned from mice and other species, and almost all will have human homologues. The 8th Workshop will provide a forum for a range of antibody-based studies relating to this accumulating corpus of genomic and proteomic data.TABLE 3Examples of Possible Future CD SpecificitiesMoleculeMolecule SizeCell TypesCommentsReference no.Identified after antibody production AM-3K antigen70 and 120 kDaMacrophages(2Zeng L Takeya M Takahashi K AM-3K, a novel monoclonal antibody specific for tissue macrophages and its application to pathological investigation.J Pathol. 1996; 178: 207-21410.1002/(SICI)1096-9896(199602)178:2 3.0.CO;2-GCrossref PubMed Scopus (37) Google Scholar) BDCA-2, BDCA-3, and BDCA-4 antigensDendritic cellsIdentifies subsets of dendritic cells(3Dzionek A Fuchs A Schmidt P Cremer S Zysk M Miltenyi S BDCA-2, BDCA-3, and BDCA-4: three markers for distinct subsets of dendritic cells in human peripheral blood.J Immunol. 2000; 165: 6037-604610.4049/jimmunol.165.11.6037Crossref PubMed Scopus (1065) Google Scholar) BENE17 kDaEndothelium“Raft-associated” member of MAL family; interacts with caveolin-1(4de Marco MC Kremer L Albar JP Martinez-Menarguez JA Ballesta J Garcia-Lopez MA BENE, a novel raft-associated protein of the MAL proteolipid family, interacts with caveolin-1 in human endothelial-like ECV304 cells.J Biol Chem. 2001; 276: 23009-2301710.1074/jbc.M009739200Abstract Full Text Full Text PDF PubMed Scopus (38) Google Scholar) CMRF-44?Dendritic cellsDifferentiated/activated(5Hock BD Starling GC Daniel PB Hart DN Characterization of CMRF-44, a novel monoclonal antibody to an activation antigen expressed by the allostimulatory cells within peripheral blood, including dendritic cells.Immunology. 1994; 83 (PMCID 1415076; 7875738): 573-581PubMed Google Scholar, 6Hock BD Fearnley DB Boyce A McLellan AD Sorg RV Summers KL Human dendritic cells express a 95 kDa activation/differentiation antigen defined by CMRF-56.Tissue Antigens. 1999; 53: 320-33410.1034/j.1399-0039.1999.530402.xCrossref PubMed Scopus (53) Google Scholar) CMRF-5695 kDaDendritic cellsDifferentiated/activated H47 antigen100 kDa (non red.) 120 kDa (red.)T cells & most NK and B cells and monocytes? Involved in T-cell activation(7Hirohashi N Nakao M Kubo K Yamada A Shichijo S Hara A Sagawa K A novel antigen (H47 Ag) on human lymphocytes involved in T cell activation.Cell Immunol. 1993; 152: 371-38210.1006/cimm.1993.1298Crossref PubMed Scopus (11) Google Scholar) Hal-1200 kDa (100 kDa)T cells, EBV-transformed B cells, myelo-monocytic cells, anaplastic large cell lymphoma? New lymphoma marker(8Asanuma H Takahashi S Ishikawa M Kamiguchi K Sato N Poppema S A monoclonal antibody, 3G12, reacts with a novel surface molecule, Hal-1, with high expression in CD30-positive anaplastic large cell lymphomas.Br J Haematol. 1999; 106: 55-6310.1046/j.1365-2141.1999.01520.xCrossref PubMed Scopus (8) Google Scholar) LAK1 and LAK2 antigens120 kDa and 110 + 140 kDa, respectivelyLGL and LAK cells(9Zocchi MR Poggi A Mariani S Gianazza E Rugarli C Identification of a new surface molecule expressed by human LGL and LAK cells production of a specific monoclonal antibody and comparison with other NK/LAK markers.Cell Immunol. 1989; 124: 144-15710.1016/0008-8749(89)90118-4Crossref PubMed Scopus (12) Google Scholar) NKp8080-kDa dimerNK cells and CD56-positive T cellsNovel member of the killer cell lectin-like receptor gene family, encoded by KLRF1 gene; triggers NK cell cytotoxicity(10Vitale M Falco M Castriconi R Parolini S Zambello R Semenzato G Identification of NKp80, a novel triggering molecule expressed by human NK cells.Eur J Immunol. 2001; 31: 233-24210.1002/1521-4141(200101)31:1 3.0.CO;2-4Crossref PubMed Scopus (162) Google Scholar, 11Roda-Navarro P Arce I Renedo M Montgomery K Kucherlapati R Fernandez-Ruiz E Human KLRF1, a novel member of the killer cell lectin-like receptor gene family: molecular characterization, genomic structure, physical mapping to the NK gene complex and expression analysis.Eur J Immunol. 2000; 30: 568-57610.1002/1521-4141(200002)30:2 3.0.CO;2-YCrossref PubMed Scopus (44) Google Scholar) VAP-1 (vascular adhesion protein)90 kDaEndotheliumMediates lymphocyte–endothelial adhesion; has monoamine oxidase activity(12Bono P Salmi M Smith DJ Jalkanen S Cloning and characterization of mouse vascular adhesion protein-1 reveals a novel molecule with enzymatic activity.J Immunol. 1998; 160 (9605161): 5563-5571PubMed Google Scholar, 13Salmi M Jalkanen S A 90-kilodalton endothelial cell molecule mediating lymphocyte binding in humans.Science. 1992; 257: 1407-140910.1126/science.1529341Crossref PubMed Scopus (266) Google Scholar) Wue-1 antigen94 kDaPlasma cellsStimulates growth of plasma cells(14Greiner A Neumann M Stingl S Wassink S Marx A Riechert F Characterization of Wue-1, a novel monoclonal antibody that stimulates the growth of plasmacytoma cell lines.Virchows Arch. 2000; 437: 372-37910.1007/s004280000258Crossref PubMed Scopus (10) Google Scholar)Identified by gene cloning B-cell maturation factor184 aaB cellsTNFR family member; receptor for TALL-1 and APRIL(15Madry C Laabi Y Callebaut I Roussel J Hatzoglou A Le Coniat M The characterization of murine BCMA gene defines it as a new member of the tumor necrosis factor receptor superfamily.Int Immunol. 1998; 10: 1693-170210.1093/intimm/10.11.1693Crossref PubMed Scopus (116) Google Scholar, 16Shu HB Johnson H B cell maturation protein is a receptor for the tumor necrosis factor family member TALL-1.Proc Natl Acad Sci U S A. 2000; 97: 9156-916110.1073/pnas.160213497Crossref PubMed Scopus (139) Google Scholar) B7-H2302 aaDendritic cellsNew member of B7 family; binds ICOS on activated T cells(17Wang S Zhu G Chapoval AI Dong H Tamada K Ni J Costimulation of T cells by B7-H2, a B7-like molecule that binds ICOS.Blood. 2000; 96 (11023515): 2808-2813Crossref PubMed Google Scholar) CLEC-1280 aaDendritic cellsNovel C-type lectin-like receptor with cytoplasmic tyrosine-based motif(18Colonna M Samaridis J Angman L Molecular characterization of two novel C-type lectin-like receptors, one of which is selectively expressed in human dendritic cells.Eur J Immunol. 2000; 30: 697-70410.1002/1521-4141(200002)30:2 3.0.CO;2-MCrossref PubMed Scopus (186) Google Scholar) CMRF-35A CMRF-35H224 aa 300aaNK cells, neutrophils, monocytes, dendritic cells, and subset of T lymphocytesNovel Ig superfamily receptors; CMRF-35H contains 3 cytoplasmic tyrosine based motifs(19Jackson DG Hart DN Starling G Bell JI Molecular cloning of a novel member of the immunoglobulin gene superfamily homologous to the polymeric immunoglobulin receptor.Eur J Immunol. 1992; 22: 1157-116310.1002/eji.1830220508Crossref PubMed Scopus (51) Google Scholar, 20Green BJ Clark GJ Hart DN The CMRF-35 mAb recognizes a second leukocyte membrane molecule with a domain similar to the poly Ig receptor.Int Immunol. 1998; 10: 891-89910.1093/intimm/10.7.891Crossref PubMed Scopus (52) Google Scholar) CS1NK cellsNovel receptor belonging to CD2 subset of Ig superfamily(21Boles KS Mathew PA Molecular cloning of CS1, a novel human natural killer cell receptor belonging to the CD2 subset of the immunoglobulin superfamily.Immunogenetics. 2001; 52: 302-30710.1007/s002510000274Crossref PubMed Scopus (71) Google Scholar) DC-STAMP470 aaDendritic cellsNovel protein containing seven putative transmembrane domains.(22Hartgers FC Vissers JL Looman MW van Zoelen C Huffine C Figdor CG DC-STAMP, a novel multimembrane-spanning molecule preferentially expressed by dendritic cells.Eur J Immunol. 2000; 30: 3585-359010.1002/1521-4141(200012)30:12 3.0.CO;2-YCrossref PubMed Scopus (93) Google Scholar) EMR3652 aaMainly leukocyte restricted. Highest levels on neutrophils, monocytes, and macrophagesNovel EGF-TM7 molecule; interacts with a surface ligand on myeloid cells(23Stacey M Lin HH Hilyard KL Gordon S McKnight AJ Human epidermal growth factor (EGF) module-containing mucin-like hormone receptor 3 is a new member of the EGF-TM7 family that recognizes a ligand on human macrophages and activated neutrophils.J Biol Chem. 2001; 276: 18863-1887010.1074/jbc.M101147200Abstract Full Text Full Text PDF PubMed Scopus (86) Google Scholar) Flt-1 (VEGFR-1)Endothelial cells, monocytes(24Sawano A Iwai S Sakurai Y Ito M Shitara K Nakahata T Flt-1, vascular endothelial growth factor receptor 1, is a novel cell surface marker for the lineage of monocyte-macrophages in humans.Blood. 2001; 97: 785-79110.1182/blood.V97.3.785Crossref PubMed Scopus (412) Google Scholar) GPRv53390 aaLeukocytesIdentified by gene cloning; G-protein–coupled histamine receptor(25Oda T Morikawa N Saito Y Masuho Y Matsumoto S Molecular cloning and characterization of a novel type of histamine receptor preferentially expressed in leukocytes.J Biol Chem. 2000; 275: 36781-3678610.1074/jbc.M006480200Abstract Full Text Full Text PDF PubMed Scopus (584) Google Scholar) IRTA1 and IRTA2Subpopulations of B cellsHomologous to the Fc and inhibitory receptor families(26Hatzivassiliou G Miller I Takizawa J Palanisamy N Rao PH Iida S IRTA1 and IRTA2, novel immunoglobulin superfamily receptors expressed in B cells and involved in chromosome 1q21 abnormalities in B cell malignancy.Immunity. 2001; 14: 277-28910.1016/S1074-7613(01)00109-1Abstract Full Text Full Text PDF PubMed Scopus (159) Google Scholar) M1601453 aaMacrophagesNew member of scavenger receptor cysteine-rich superfamily(27Gronlund J Vitved L Lausen M Skjodt K Holmskov U Cloning of a novel scavenger receptor cysteine-rich type I transmembrane molecule (M160) expressed by human macrophages.J Immunol. 2000; 165: 6406-641510.4049/jimmunol.165.11.6406Crossref PubMed Scopus (48) Google Scholar) MARCO (macrophage receptor with collagenous structure)520 aaMacrophagesClass A scavenger receptor; involved in bacterial clearance in vivo(28Elomaa O Sankala M Pikkarainen T Bergmann U Tuuttila A Raatikainen-Ahokas A Structure of the human macrophage MARCO receptor and characterization of its bacteria-binding region.J Biol Chem. 1998; 273: 4530-453810.1074/jbc.273.8.4530Abstract Full Text Full Text PDF PubMed Scopus (120) Google Scholar, 29van der Laan LJ Dopp EA Haworth R Pikkarainen T Kangas M Elomaa O Regulation and functional involvement of macrophage scavenger receptor MARCO in clearance of bacteria in vivo.J Immunol. 1999; 162 (9916718): 939-947PubMed Google Scholar) TACI293 aaB cellsTNFR family member; receptor for TALL-1 and APRIL(30Xia XZ Treanor J Senaldi G Khare SD Boone T Kelley M TACI is a TRAF-interacting receptor for TALL-1, a tumor necrosis factor family member involved in B cell regulation.J Exp Med. 2000; 192: 137-14310.1084/jem.192.1.137Crossref PubMed Scopus (220) Google Scholar) TREM-1 and TREM-2 (triggering receptors expressed on myeloid cells)Neutrophils and subset of monocytes (TREM-1) and macrophages (TREM-2)Novel Ig superfamily receptors; TREM-1 triggers neutrophil secretion (e.g., IL-8) and degranulation; TREM-2 activates macrophages, and both associate with DAP12(31Bouchon A Dietrich J Colonna M Cutting edge: inflammatory responses can be triggered by TREM-1, a novel receptor expressed on neutrophils and monocytes.J Immunol. 2000; 164: 4991-499510.4049/jimmunol.164.10.4991Crossref PubMed Scopus (891) Google Scholar, 32Daws MR Lanier LL Seaman WE Ryan JC Cloning and characterization of a novel mouse myeloid DAP12-associated receptor family.Eur J Immunol. 2001; 31: 783-79110.1002/1521-4141(200103)31:3 3.0.CO;2-UCrossref PubMed Scopus (148) Google Scholar) Open table in a new tab As in the 7th Workshop, in which four new sections were added, it may be possible to include neuronal cells in the 8th Workshop. Many neuronal cells express cell surface proteins found on leukocytes and vice versa (e.g., CD56, CD100, CD168, 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 may reflect shared biological processes. It may also be noted that other molecules such as the mucins, thought to be primarily associated with epithelial cells, are now being described on leukocytes. Finally, it remains to be established how the 8th and subsequent HLDA Workshops should deal with lineage- or stage-restricted leukocyte molecules that are localized within the cell cytoplasm (or nucleus). Given the importance of many of these molecules in signaling pathways initiated via known surface CD molecules, their identification and study is an inevitable extension of the work of the first seven HLDA Workshops. Whether or not a new “intracellular CD” categorization scheme is devised for such molecules, they are of interest for many laboratories studying human hematopoietic cells, and their investigation will be among the aims of the next Workshop.