title: Structural and functional diversity of blood group antigens.
abstract: Biochemical and molecular genetic studies have revealed that blood group antigens are present on cell surface molecules of wide structural diversity, including carbohydrate epitopes on glycoproteins and/or glycolipids, and peptide antigens on proteins inserted within the membrane via single or multi-pass transmembrane domains, or via glycosylphosphatidylinositol linkages. These studies have also shown that some blood group antigens are carried by complexes consisting of several membrane components which may be lacking or severely deficient in rare blood group 'null' phenotypes. In addition, although all blood group antigens are serologically detectable on red blood cells (RBCs), most of them are also expressed in non-erythroid tissues, raising further questions on their physiological function under normal and pathological conditions. In addition to their structural diversity, blood group antigens also possess wide functional diversity, and can be schematically subdivided into five classes: i) transporters and channels; ii) receptors for ligands, viruses, bacteria and parasites; iii) adhesion molecules; iv) enzymes; and v) structural proteins. The purpose of this review is to summarize recent findings on these molecules, and in particular to illustrate the existing structure-function relationships.
authors.affiliation: INSERM U76, INTS, Paris, France. cartron@idf.inserm.fr
authors.forename: J P
authors.initials: JP
authors.lastname: Cartron
authors.forename: Y
authors.initials: Y
authors.lastname: Colin
mesh_terms: D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry / Q000502:physiology; D000953:Antigens, Protozoan; D001789:Blood Group Antigens / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000276:immunology / Q000502:physiology*; D001798:Blood Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000502:physiology*; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000502:physiology; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000502:physiology; D002877:Chromosomes, Human / Q000235:genetics; D004798:Enzymes / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000502:physiology; D004910:Erythrocyte Membrane / Q000737:chemistry / Q000276:immunology; D004912:Erythrocytes / Q000201:enzymology / Q000382:microbiology / Q000469:parasitology / Q000821:virology; D005796:Genes; D006801:Humans; D016023:Integrins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000502:physiology; D007473:Ion Channels / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000502:physiology; D008958:Models, Molecular; D009928:Organ Specificity; D011487:Protein Conformation; D015800:Protozoan Proteins; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000502:physiology; D015728:Receptors, HIV / Q000502:physiology; D012204:Rh-Hr Blood-Group System / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000502:physiology; D013045:Species Specificity; D013329:Structure-Activity Relationship
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D000953:Antigens, Protozoan; D001789:Blood Group Antigens; D001798:Blood Proteins; D002352:Carrier Proteins; D015815:Cell Adhesion Molecules; C066001:Duffy antigen binding protein, Plasmodium; D004798:Enzymes; D016023:Integrins; D007473:Ion Channels; D015800:Protozoan Proteins; D011956:Receptors, Cell Surface; D015728:Receptors, HIV; D012204:Rh-Hr Blood-Group System