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Blood Group Antigens As Receptors for Bacteria and Parasites

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Blood Group Antigens As Receptors for Bacteria and Parasites Review: blood group antigens as receptors for bacteria and parasites C. LOMAS-FRANCIS Abbreviations: Gal = galactose; Glc = glucose; NeuAc lectins.4 Lectins are a class of proteins of nonimmune = N-acetylneuraminic acid; GlcNAc = N-acetylglu- origin that can combine with sugars rapidly, selective- cosamine; GalNAc = N-acetylgalactosamine; FUC = ly, and, since binding is noncovalent, reversibly. Lectins fucose; Cer = ceramide. are not confined to plants but are widespread through- out nature, and frequently appear on surfaces of cells, An important phase in the initiation of diseases caused where they are strategically positioned to combine by bacterid and parasites is the adhesion of the infectious with complementary sugars on neighboring cells. agent to tissues of the mammalian host. Adhesion is Lectins are exquisitely specific; they can distinguish mediated by specificligand-receptor interactions. Host between different monosaccharides and specifically cell receptors include a number of structures carrying bind to oligosaccharides, detecting subtle differences blood group antigens. A selection of such receptors and in complex carbohydrate structures. the attaching microorganisms, mostly bacteria, are listed Bacterial attachment to epithelial cells and to RBCs in Table 1 and will be reviewed in this article. results from the interaction of host cell receptors with bacterial surface structures known as fimbriae or pili.5 Table 1. Receptors for bacteria and parasites These submicroscopic hair-like appendages are 5 to 10 Receptors Bacteria and parasites nanometers in diameter and several hundreds of Ii Mycoplasmapneumuniae nanometers long. They protrude from the surface of P1, P, andPk P-fimbriated Escherichia coli the bacteria and serve as bacterial-binding factors by AnWj Haemophilus influenzae producing lectin-like adhesins or hemagglutinins. Dra 075X-adhesin of Escherichia coli Fimbriae-bearing surface lectins are not restricted to E. FY Plasmodium vivax Plasmodium knowlest coli. A particular strain of bacteria may produce more Glycophorin A, R, C, D PIasmodium falciparum than one fimbrial type at the same time; each fimbrial N-acetylneuraminic acid type is usually on a different bacterium. Fimbriae may be characterized by the hemagglutinin produced. The The adhesive capacity of bacteria was first described common type 1 fimbriae bind the sugar mannose and by Duguid et al. These workers demonstrated that are therefore termed “mannose sensitive,” since many strains of Escherichia (E.) coli, an organism caus- hemagglutination is inhibited by mannose.* Various ing intestinal and extraintestinal infections, adhered to “mannose resistant” adhesins have been identified on cells from the epithelial lining of tissues and to red E. coli strains: P fimbriae of pyelonephritogenic E. coli blood cells (RBCs). The presence of the bacteria caused bind the disaccharide Gala(1-4)Gal, which is found in red cell clumping, commonly referred to as hemagglu- human blood group P glycosphingolipids (thus the tination. Hemagglutination is specific and, depending term P fimbriae) and antigens of the globoside collec- on the bacterial strain, can be inhibited by specific sug- tion.6.7 Other mannose-resistant fimbriae make up a ars, including the monosaccharidemannose. heterogeneous group and are termed X-adhesins: these Sugars play a vital role in cell-to-cellrecognition and include S fimbriae, which recognize sialylgalactosides cell-to-celladhesion, and glycoconjugates are found on (NeuAca[2-31Galß[1-3]GalNAc)of glycophorinA and the surface of most cells. Receptor recognition and may be important in the pathogenesis of neonatal interaction is mediated by carbohydrate2,3 and meningitis.* E. coli-075X strains produce an X-adhesin IMMUNOHEMATOLOGY, VOLUME 10, NUMBER 3, 1994 75 C. LOMAS-FRANCIS that is referred to as the Dr hemagglutinin, since ognized by the cold autoantibodies anti-Gd and anti-FI Dr(a+) RBCs but not Dr(a-) RBCs are agglutinated by (Table 2); anti-I is an autoantibody directed against the this adhesin.8 backbone structure of the receptor.7,10 König et al.10 found that 53 percent of 192 patients Mycoplasma pneumoniae and Ii with recent M. pneumoniae infection had co-existing Mycoplasma (M.) pneumoniae infection has long anti-I and anti-FI/Gd in their serum. These patients had been associated with an increase in titer and thermal responded to the entire receptor structure, although in range of autoanti-I. The antibody was thought to be pro- the same study 22 percent of the sera contained only duced in response to an M. pneumoniae antigen and to anti-I. be cross-reactive with an RBC antigen, presumably I related. Loomes et al.9 suggested that these autoanti- Haemophilus inauenzae and AnWj bodies occurred as a result of the interaction of I antigen Haemophilus (H.) influenzae is found in the throat with M. pneumoniae and of the presentation of this of most healthy people, but can cause respiratory tract altered "self" antigen to the immune system. infections. This organism is a major cause of bacterial The attachment of radiolabeled RBCs to M. pneumo- meningitis in young children. Fimbriated strains of H. niae cultures was inhibited by oligosaccharides, glyco- influenzae will agglutinate RBCs, and the fimbriae pro- proteins, and glycolipids containing chains of the mote bacterial adherence to nasopharyngeal cells. branched I or linear i antigen structures, provided that In 1986, van Alphen and his colleagues" showed NeuAc (sialic acid) was present in a terminal position. that the high-incidence antigen AnWj (called Anton at Linear oligosaccharide chains containing repeating N- that time) is the RBC receptor for H. influenzae. This acetyllactosamine residues (GAPß[ 1-41 GlcNAc) give rise work was extended in later publications. AnWj is pre- to i antigen; I antigen results from repeated branching sent on RBCs of most people, but is lacking or marked- of this chain by addition of more Galß(1-4)GlcNAc units ly suppressed on RBCs of the Lu(a-b-) phenotype (Table 2). It was concluded that the structure caused by In(Lu), a rare dominant gene independent of NeuAca(2-3)Galß(1-4)GlcNAc is recognized by, and the Lu locus. AnWj is also absent from cord RBCs and acts as a receptor for, M pneumoniae. The receptor is RBCs from those rare people with anti-AnWj in their made immunogenic by the binding of the bacteria. The serum or with the inherited AnWj- phenotype.12 complete structures that were identified as receptors for Although AnWj antigen is the structure on RBCs M. pneumoniae are identical to the RBC antigens rec- bound by H. influenzae, the establishment of infection 3) Gd antigen Galß(1-4)GlcNAc/Glc 6) 76 IMMUNOHEMATOLOGY, VOLUME 10, NUMBER 3, 1994 RBC antigens: bacterial and parasitic receptors requires binding to epithelial cells of the respiratory disposes females to UTIs. The presence of differentfim- tract. Initially, van Alphen et al.11 concluded that the brial types is correlated with different types of UTIs: P epithelial cell receptor and the RBC receptor for H. and S fimbriae are correlated with pyelonephritis, Dr influenzae fimbriae are expressed independently. 13 hemagglutinins with cystitis, and type 1 fimbriae (the This conclusion was based on the observation that H. common type) with lower UTIs.18 influenzae adhered to buccal epithelial cells, but not to RBCs from healthy neonates, nor to RBCs from an P-fimbriated E. coli AnWj- person with anti-AnWj. Recent studies showed P-fimbriated E. coli were so named when it was that the failure of H influenzae to bind to these RBCs found that they would hemagglutinate all RBCs except was caused by suppression of the red cell receptor, tem- those of the p phenotype, a null phenotype lacking all porarily in the case of cord cells and transiently in P system antigens,6 and antigens of the globoside col- AnWj- persons having and-AnWj in their serum, rather lection. P fimbriae bind to host cell surfaces through than by genetic events. The finding of an Arab-Israeli recognition of the disaccharide Gala(1-4)Gal present in family with three AnWj- siblings demonstrated that the the oligosaccharides attached to membrane glycolipids AnWj- phenotype may be an inherited characteristic.14 of the host cell. Testing of AnWj- and AnWj+ members of this family Serologically, we recognize these Gala(1-4)Gal- showed concomitant inheritance of the epithelial and containing glycosphingolipids as P1, antigen, P antigen RBC receptors, proving joint inheritance of the genetic (globoside), and Pk antigen (Table 3). On P1 and Pk gly- information for both receptors.15 However, despite this cosphingolipids, Gala(1-4)Gal is in a terminal position, common genetic background, the two receptors must while in globoside (P antigen), Gala(1-4)Gal is in an be different, since anti-AnWj inhibited only hemaggluti- internal position. E coli can combine with glycosphin- nation of AnWj+ RBCs and not adherence to buccal golipids that have the disaccharide in a terminal position epithelium. Evidence shows that the receptor is likely or when the disaccharide is part of the inner structure to be sugar, and lipids are unlikely to be involved. of the molecule. Therefore, E coli have a choice of P, P1, AnWj, and thus the receptor for H. influenzae, may and Pkantigens as attachment sites. Indeed, E. coli may be associated with the erythrocyte CD44 glycoprotein. prefer the internal version of the disaccharide, because Parsons et al. 16 described a child with a novel form of of the greater conformational stability of the receptor in dyserythropoietic anemia whose RBCs were AnWj-; this position. A subtype of P fimbriae, encoded by the these RBCs had a marked deficiency of the erythrocyte pap-2 gene cluster, uses LKE antigen (stage-specific membrane CD44 glycoprotein. embryonic antigen 4, SSEA-4) as its receptor.18 This complex binding site, an internal portion of the E. coli and urinary tract infections molecule, is composed of Galp(1-3)GalNAcß(1-3) The establishment of ascending urinary tract infec- Gala(1-4)Gal.
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