Genetics of ABO, H, Lewis, X and Related Antigens

Oriol, Rafaël; Pendu, Jacques Le; Mollicone, Rosella

doi:10.1159/000461485

Cited by 49 publications

(59 citation statements)

References 25 publications

(34 reference statements)

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“…Addition of a fucose in ␣1,2 to the galactose residue of the precursors yields the H antigens. The A and B antigens can then be formed by addition of either an N-acetylgalactosamine or a galactose in ␣1,3 linkage to the galactose of the H antigens (20). The results presented above clearly show that native RHDV and VLPs recognize the A and H type 2 blood group antigens.…”

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confidence: 73%

Binding of Rabbit Hemorrhagic Disease Virus to Antigens of the ABH Histo-Blood Group Family

Ruvoën-Clouet

Ganière

André‐Fontaine

et al. 2000

J Virol

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The ability of rabbit hemorrhagic disease virus to agglutinate human erythrocytes and to attach to rabbit epithelial cells of the upper respiratory and digestive tracts was shown to depend on the presence of ABH blood group antigens. Indeed, agglutination was inhibited by saliva from secretor individuals but not from nonsecretors, the latter being devoid of H antigen. In addition, erythrocytes of the rare Bombay phenotype, which completely lack ABH antigens, were not agglutinated. Native viral particles from extracts of infected rabbit liver as well as virus-like particles from the recombinant virus capsid protein specifically bound to synthetic A and H type 2 blood group oligosaccharides. Both types of particles could attach to adult rabbit epithelial cells of the upper respiratory and digestive tracts. This binding paralleled that of anti-H type 2 blood group reagents and was inhibited by the H type 2-specific lectin UEA-I and polyacrylamide-conjugated H type 2 trisaccharide. Young rabbit tissues were almost devoid of A and H type 2 antigens, and only very weak binding of virus particles could be obtained on these tissues. Rabbit hemorragic disease virus (RHDV) is a noncultivablecalicivirus that infects rabbits and causes epidemics of an acute fatal hepatitis. The disease is characterized by high morbidity and mortality rates for adult animals. Death is the result of a widespread circulation dysfunction associated with disseminated intravascular coagulation and necrotizing hepatitis lesions (14, 24). Large quantities of virus particles are found in several organs, especially the liver, which is considered the major site of virus replication (6,14,19,27). The viral genome consists of a single-stranded RNA of nearly 7.5 kb, packaged in a small icosahedral capsid (3, 15). The capsid protein has an estimated molecular mass of 60 kDa (VP60) (16), and expression of the corresponding cDNA in insect cells infected with a recombinant baculovirus yields a protein that spontaneously assembles into virus-like particles (VLPs). These VLPs are both antigenically and morphologically similar to native RHDV particles (11,23). Yet very little is known about the pathogenesis of naturally occurring RHDV infections, and identification of the cellular receptor(s) used by the virus to establish infection would lead to a better understanding of the pathogenesis of RHDV.RHDV is known to agglutinate human erythrocytes (2, 25), and previous studies demonstrated that its hemagglutinin receptor on human red blood cells corresponds to a developmental antigen which is not expressed on fetal cells and is mainly carried by polyglycosylceramides (26). The glycolipid nature of the receptor on human red blood cells suggests that the carbohydrate moiety could be recognized by the virus capsid protein. Carbohydrate antigens of the histo-blood group family are developmental antigens that can be shared among various mammal species, and the presence of some of these antigens has been detected on epithelial cells of the rabbit digestive tract (1,17,21...

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confidence: 73%

Binding of Rabbit Hemorrhagic Disease Virus to Antigens of the ABH Histo-Blood Group Family

Ruvoën-Clouet

Ganière

André‐Fontaine

et al. 2000

J Virol

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132

120

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“…The expression of HBGAs on RBCs is a recent evolutionary event, being present only in humans and anthropoid apes (23). However, pigs express A and H antigens on their tissues (26) and also have a gene homolog to the human FUT2 gene, the gene expressing GDP-L-fucose:␤-D-galactoside ␣-1-2-L-fucosyltransferase (30).…”

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confidence: 99%

Binding Patterns of Human Norovirus-Like Particles to Buccal and Intestinal Tissues of Gnotobiotic Pigs in Relation to A/H Histo-Blood Group Antigen Expression

Cheetham

Souza

McGregor

et al. 2007

J Virol

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Histo-blood group antigen (HBGA) phenotypes have been associated with susceptibility to human noroviruses (HuNoVs). Our aims were: (i) to determine the patterns of A/H HBGA expression in buccal and intestinal tissues of gnotobiotic (Gn) pigs; (ii) to determine if virus-like particles (VLPs) of HuNoV genogroup I (GI) and GII bind to A- or H-type tissues; (iii) to compare A/H expression and VLP binding patterns and confirm their binding specificities by blocking assays; (iv) to develop a hemagglutination inhibition test using buccal cells from live pigs to determine the Gn pig's A/H phenotype and to match viral strains with previously determined HuNoV VLP binding specificities; and (v) to determine the A/H phenotypes and compare these data to the infection outcomes of a previous study of 65 Gn pigs inoculated with HuNoV GII/4 strain HS66 and expressing A and/or H or neither antigen on their buccal and intestinal tissues (S. Cheetham, M. Souza, T. Meulia, S. Grimes, M. G. Han, and L. J. Saif, J. Virol. 80:10372-10381, 2006). We found that the HuNoV GI/GII VLPs of different clusters bound to tissues from four pigs tested (two A+ and two H+). The GI/1 and GII/4 VLPs bound extensively to duodenal and buccal tissues from either A+ or H+ pigs, but surprisingly, GII/1 and GII/3 VLPs bound minimally to the duodenum of an A+ pig. The VLP binding was partially inhibited by A-, H1-, or H2-specific monoclonal antibodies, but was completely blocked by porcine mucin. Comparing the A/H phenotypes of 65 HS66-inoculated Gn pigs from our previous study, we found that significantly more A+ and H+ pigs (51%) than non-A+ and non-H+ pigs (12.5%) shed virus. From the 22 convalescent pigs, significantly more A+ or H+ pigs (66%) than non-A+ or H+ pigs (25%) seroconverted.

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“…The genetic relationship occurs between the Lewis blood group system and the structures of HMO found in an individuals' milk (8,9). The genetic background of the Lewis blood group system has been thoroughly reviewed (12) and is depicted in Fig. 3.…”

Section: Applications Of Hmo Analysis Determination Of Genetic Basis mentioning

confidence: 99%

“…The fucose residues may be attached to HMO depending on the expression of both the Lewis gene (fucosyltransferase 3 -FUT3) and the secretor gene (fucosyltransferase 2 -FUT2). Fucose residues may be α1-2 linked to galactose residues when Fut2 is active, while fucose residues may be α1-4 linked when Fut3 is active (11,12). In individuals where the expression of FUT2 occurs in epithelial cells, (α1-2)fucose is secreted into fluids such as saliva, tear, and milk.…”

Section: Applications Of Hmo Analysis Determination Of Genetic Basis mentioning

confidence: 99%

“…Fucoses may be variably linked to a galactose. An α1-2 linked fucose is produced when fucosyltransferase 2 (FUT2) is active.. Alternately, fucose residues may be α1-4 linked when fucosyltransferase 3 (FUT3) is active (11,12). Although human milk oligosaccharides are the third most abundant component of human milk, they have no direct nutritional values.…”

Section: Introductionmentioning

confidence: 99%

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