Immunohistological analysis of antibodies against ABH and other glycoconjugates in normal human pyloric and duodenal mucosae

Pendu, Jacques Le; Cabellec, Marie-Thérèse Le; Bara, Jacques

doi:10.1016/s1246-7820(97)80009-2

Cited by 8 publications

(7 citation statements)

References 3 publications

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“…We observed that those antibodies reactive with either E. coli LMG8223 or E. coli LFMFP861 were those that have the broadest reactivity to A or B epitopes. Thus, E. coli LMG8223 showed positive reactions with anti-A antibodies #21 (42.5%) and #7 (68%), which have very strong, and broad A reactivity, but not with antibodies #3, or #5 (<1%), which have more restricted anti-A specificity ( Le Pendu et al, 1997 ). Similarly, E. coli LFMFP861 showed strong positive reaction with anti-B antibody #49 (14.3%), which has a broad reactivity with a group of B-like molecules, but showed low or no reaction with antibodies #38 (3.9%), #39 (2.7%), #40 (<1%), and #43 (3.9%), known to be more restricted anti-B ( Le Pendu et al, 1997 ).…”

Section: Resultsmentioning

confidence: 99%

“…A series of anti-HBGAs antibodies was used. Anti-A antibodies #3, #5, #7, #21 and anti-B antibodies #38, #39, #40, #43, #49 have been described previously ( Le Pendu et al, 1997 ). The anti-H type 3/4 Mbr1 was obtained from Enzo Life Sciences; the anti-H 19-0LE, an anti-H type 2 that shows some cross-reactivity with Le y , the anti-Le a 7-LE, the anti-Le b 2-25LE, and the anti-Le y 12-4LE were obtained from Dr. J. Bara (CNRS, Villejuif, France).…”

Section: Methodsmentioning

confidence: 99%

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Binding to histo-blood group antigen-expressing bacteria protects human norovirus from acute heat stress

Breiman

Pendu

et al. 2015

Front. Microbiol.

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This study aims to investigate if histo-blood group antigen (HBGA) expressing bacteria have any protective role on human norovirus (NoV) from acute heat stress. Eleven bacterial strains were included, belonging to Escherichia coli, Enterobacter cloacae, Enterobacter aerogenes, Clostridium difficile, Bifidobacterium adolescentis, and B. longum. HBGA expression of the bacteria as well as binding of human NoV virus-like particles (VLPs, GI.1, and GII.4 strains) to the bacteria were detected by flow cytometry. NoV VLPs pre-incubated with HBGA expressing or non-HBGA expressing bacteria were heated and detected by both direct ELISA and porcine gastric mucin-binding assay. The NoV-binding abilities of the bacteria correlated well with their HBGA expression profiles. Two HBGA expressing E. coli (LMG8223 and LFMFP861, both GI.1 and GII.4 binders) and one non-HBGA expressing E. coli (ATCC8739, neither GI.1 nor GII.4 binder) were selected for the heat treatment test with NoV VLPs. Compared with the same cell numbers of non-HBGA expressing E. coli, the presence of HBGA-expressing E. coli could always maintain higher antigen integrity, as well as mucin-binding ability of NoV VLPs of both GI.1 and GII.4 after heat-treatment at 90°C for 2 min. These results indicate that HBGA-expressing bacteria may protect NoVs during the food processing treatments, thereby facilitating their transmission.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Binding to histo-blood group antigen-expressing bacteria protects human norovirus from acute heat stress

Breiman

Pendu

et al. 2015

Front. Microbiol.

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“…ND, not determined. , and ALe y (13). Their binding was detected as described above for antibody 10C5.…”

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confidence: 99%

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

135

120

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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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“…Antibody-dependent assays were blocked with 5% nonfat dry milk (Régilait, Saint-Martin-Belle-Roche, France) diluted in PBS, while lectin assays were blocked with Synblock (AbD Serotec, Oxford, United Kingdom). The A antigen was detected using mouse monoclonal anti-A antibody (2A21), and the B antigen was detected using a specific mouse monoclonal antibody (B49) (81). H type 2 expression was determined using the horseradish peroxidase (HRP)-conjugated lectin UEA-I at 2 g/ml (Sigma-Aldrich, St. Louis, MO).…”

Section: Methodsmentioning

confidence: 99%

Host-Specific Glycans Are Correlated with Susceptibility to Infection by Lagoviruses, but Not with Their Virulence

Lopes

Breiman

Lora

et al. 2018

J Virol

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The rabbit hemorrhagic disease virus (RHDV) and the European brown hare syndrome virus (EBHSV) are two lagoviruses from the family that cause fatal diseases in two leporid genera, and , respectively. In the last few years, several examples of host jumps of lagoviruses among leporids were recorded. In addition, a new pathogenic genotype of RHDV emerged and many non-pathogenic strains of lagoviruses have been described. The molecular mechanisms behind host shifts and the emergence of virulence are unknown. Since RHDV uses glycans of the histo-blood group antigen type as attachment factors to initiate infection, we studied if glycan specificities of the new pathogenic RHDV genotype, non-pathogenic lagoviruses and EBHSV potentially play a role in determining host range and virulence of lagoviruses. We observed binding to A, B or H antigens of the histo-blood group family for all strains known to primarily infect European rabbits (), that have recently been classified as GI strains. Yet, we could not explain the emergence of virulence since similar glycan specificities were found between several pathogenic and non-pathogenic strains. By contrast, EBHSV, recently classified as GII.1, bound to terminal β-linked N-acetylglucosamine residues of O-glycans. Expression of these attachment factors in the upper respiratory and digestive tracts in three lagomorph species ( and ) showed species-specific patterns regarding the susceptibility to infection by these viruses, indicating that species-specific glycan expression is likely a major contributor to lagoviruses host specificity and range. Lagoviruses constitute a genus of the family, comprising highly pathogenic viruses, RHDV and EBHSV, which infect rabbits and hares, respectively. Recently, non-pathogenic strains were discovered and new pathogenic strains have emerged. In addition, host jumps between lagomorphs are observed. The mechanisms responsible for the emergence of pathogenicity and host-species range are unknown. Previous studies showed that RHDV strains attach to glycans expressed in the upper respiratory and digestive tracts of rabbits, the likely doors of virus entry. Here we studied the glycan-binding properties of novel pathogenic and non-pathogenic strains looking for a link between glycan-binding and virulence or between glycan specificity and host range. We found that glycan binding did not correlate with virulence. However, expression of glycan motifs in the upper respiratory and digestive tracts of lagomorphs revealed species-specific patterns associated with the host range of the virus strains, suggesting that glycan diversity contributes to lagoviruses' host range.

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Immunohistological analysis of antibodies against ABH and other glycoconjugates in normal human pyloric and duodenal mucosae

Cited by 8 publications

References 3 publications

Binding to histo-blood group antigen-expressing bacteria protects human norovirus from acute heat stress

Binding to histo-blood group antigen-expressing bacteria protects human norovirus from acute heat stress

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

Host-Specific Glycans Are Correlated with Susceptibility to Infection by Lagoviruses, but Not with Their Virulence

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