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Binding of Rabbit Hemorrhagic Disease Virus to Antigens of the ABH Histo-Blood Group Family
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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.
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“while RHDV and human noroviruses bind histo-blood group antigens – complex carbohydrates linked to glycoproteins or glycolipids on the surface of erythrocytes and mucosal epithelial cells [40–42].”
From Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures (2017) · cites this paper as [42]
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Research works printed but not linked: 27
- 10.1002/bms.1200060603 · DOI
- 10.20506/rst.10.2.561 · DOI
- 10.1099/0022-1317-78-2-291 · DOI
- 10.1021/bi00290a024 · DOI
- 10.1016/S0166-0934(98)00030-5 · DOI
- Guittré C. Ruvoën-Clouet N. Barraud L. Cherel Y. Baginski I. Prave M. Ganière J. P. Trépo C. Cova L. Early stages of rabbit haemorrhagic disease virus infection monitored by polymerase chain infection.Zentbl. Vetmed Reihe B 43 1996 109 118
- Hanchun Y. Xu W. Y. Du N. Hemagglutination characteristics of rabbit haemorrhagic disease virus 1991 67 Proceedings of the International Symposium on Rabbit Haemorrhagic Disease. Beijing People's Republic of China. Chinese Association of Animal and Veterinary Sciences Beijing China.
- 10.1073/pnas.91.13.5843 · DOI
- 10.1074/jbc.270.9.4640 · DOI
- 10.1128/JVI.72.5.4492-4497.1998 · DOI
- 10.1128/jvi.68.10.6794-6798.1994 · DOI
- Le Pendu J. Cartron J. P. Lemieux R. U. Oriol R. The presence of at least two different H blood group-related β-d-gal α-2-l-fucosyltransferases in human serum and genetics of blood group H substances.Am. J. Hum. Genet. 37 1985 749 760
- 10.1016/S1246-7820(97)80009-2 · DOI
- 10.20506/rst.10.2.560 · DOI
- 10.1016/0042-6822(91)90436-F · DOI
- 10.1016/0042-6822(91)90437-G · DOI
- 10.1023/A:1018545922728 · DOI
- Morisse J. P. Le Gall G. Boilletot E. Hepatitis of viral origin in leporidae. Introduction and aetiological hypotheses.Rev. Sci. Tech. Off. Int. Epizoot. 10 1991 283 297
- 10.1016/0378-1135(92)90065-2 · DOI
- 10.1111/j.1423-0410.1986.tb01946.x · DOI
- Oriol R. Mollicone R. Coullin P. Dalix A. M. Candelier J. J. Genetic regulation of the expression of ABH and Lewis antigens in tissues.APMIS 100 1992 28 38
- 10.1016/0021-9975(92)90008-I · DOI
- 10.1007/BF01718245 · DOI
- 10.1111/j.1439-0450.1992.tb01192.x · DOI
- Pu B. Q. Qian N. J. Cui S. J. HA and HI tests for the detection of antibody titers to so called “haemorrhagic pneumonia” in rabbits.Chin. J. Vet. Med. 11 1985 16 17
- 10.1016/0923-2516(96)80587-5 · DOI
- 10.1007/BF00142046 · DOI
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BackgroundInfluentialYu, Y., Mishra, S., Song, X.-Z., Lasanajak, Y., Bradley, K. C., Tappert, M. M., Air, G., Steinhauer, D., Halder, S., Cotmore, S., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.425819 · Cited by 95
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BackgroundZakhour, M., Ruvoen-Clouet, N., Charpilienne, A., Langpap, B., Poncet, D., Peters, T., Bovin, N., & Pendu, J. L. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000504 · Cited by 79
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BackgroundDonohue, D. S., Ielasi, F., Goossens, K. V. Y., & Willaert, R. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07676.x · Cited by 53
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“[16, 17].”
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BackgroundVirus-Like Particles, a Versatile Subunit Vaccine Platform
Donaldson, B., Al-Barwani, F., Young, V., Scullion, S., Ward, V., & Young, S. (2014) · Subunit Vaccine Delivery · doi:10.1007/978-1-4939-1417-3_9 · Cited by 33
“RHDV VLPs retain the ability of its native virus to bind carbohydrate moieties, providing a useful mechanism for modifi cation and vaccine enhancement (Ruvoen-Clouet et al.”
BackgroundNeave, M. J., Hall, R. N., Huang, N., McColl, K. A., Kerr, P. J., Hoehn, M., Taylor, J. M., & Strive, T. (2018) · Viruses · doi:10.3390/v10090512 · Cited by 39
“These include (i) a developmental antigen that functions as the cellular receptor for the virus [30,53]; (ii) structural or functional changes to the liver, possibly due to dietary changes at weaning, that induce susceptibility [33,50]; or (iii) differences in innate immune responses between young and adult rabbits th…”
BackgroundImmunosuppression abrogates resistance of young rabbits to Rabbit Haemorrhagic Disease (RHD)
Marques, R. M., Teixeira, L., Águas, A. P., Ribeiro, J. C., Costa-e-Silva, A., & Ferreira, P. G. (2014) · Veterinary Research · doi:10.1186/1297-9716-45-14 · Cited by 30
“They also showed that hepatocytes, the main target of RHDV replication, do not express HBGA [7,8], which led them to suggest the existence of additional hepatic cellular receptor(s) for the virus [3].”
BackgroundInfluentialImmunity against Lagovirus europaeus and the Impact of the Immunological Studies on Vaccination
Müller, C., Hrynkiewicz, R., Bębnowska, D., Maldonado, J., Baratelli, M., Köllner, B., & Niedźwiedzka-Rystwej, P. (2021) · Vaccines · doi:10.3390/vaccines9030255 · Cited by 27
Zhu, J., Miao, Q., Tang, J., Wang, X., Dong, D., Liu, T., Qi, R., Yang, Z., & Liu, G. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007383 · Cited by 26
“RHDV has been shown to bind to oligosaccharides H type 2 and A type 2, which are histo-blood group antigens (HBGAs) expressed on the surfaces of cells lining the duodenal surface and trachea of rabbits, thereby presenting two possible viral entry points [5].”
BackgroundCompetition for membrane receptors: norovirus detachment via lectin attachment.
Parveen, N., Rydell, G., Larson, G., Hytönen, V., Zhdanov, V., Höök, F., & Block, S. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06036 · Cited by 24
Bruce, J., Twigg, L., & Gray, G. S. (2004) · doi:10.1071/wr02069 · Cited by 23
Intestinal mucin-type O -glycans: the major players in the host-bacteria-rotavirus interactions
Raev, S. A., Amimo, J. O., Saif, L. J., & Vlasova, A. N. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2197833 · Cited by 22
“The biodiversity of mucosal O-glycans may play an evolutionary important role in protection against pathogens known to interact with certain glycans such as HBGAs resulting in lower susceptibility of mammals.(54)”
BackgroundLiver disease in young rabbits infected by calicivirus through nasal and oral routes.
Ferreira, P. G., Costa-e-Silva, A., & Águas, A. P. (2006) · Research in Veterinary Science · doi:10.1016/j.rvsc.2006.02.001 · Cited by 22
Immune Response Modulation by Caliciviruses
Peñaflor-Téllez, Y., Trujillo-Uscanga, A., Escobar-Almazán, J. A., & Gutiérrez-Escolano, A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02334 · Cited by 21
“Many noroviruses, neboviruses, and lagoviruses require saccharides in histo-blood group antigens (HBGAs) [reviewed in (13) and (14), whereas vesiviruses and murine norovirus (MNV) use sialic acid (15, 16)].”
BackgroundBovine Nebovirus Interacts with a Wide Spectrum of Histo-Blood Group Antigens
Cho, E.-H., Soliman, M., Alfajaro, M. M., Kim, J.-Y., Seo, J., Park, J.-G., Kim, D.-S., Baek, Y.-B., Kang, M.-I., Park, S.-I., et al. (2018) · Journal of Virology · doi:10.1128/jvi.02160-17 · Cited by 21
Fernández, E., Toledo, J., Méndez, L., González, N., Parra, F., Martín-Alonso, J., Limonta, M., Sánchez, K., Cabrales, A., Estrada, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056417 · Cited by 21
“The stability noticed for other calicivirus-like particles at acidic pH has been attributed in part to the capacity in vivo of some of these viruses to attach to the host gastrointestinal tract [50–52].”
BackgroundAbrantes, J., & Lopes, A. M. (2021) · Microorganisms · doi:10.3390/microorganisms9050972 · Cited by 32
“This culminated in the identification of ABH blood group antigens as attachment factors used by RHDV to initiate infection [37].”
BackgroundRademacher, C., & Peters, T. (2008) · Topics in current chemistry · doi:10.1007/128_2007_19 · Cited by 22
Parkes, J., Glentworth, B., & Sullivan, G. (2008) · doi:10.1071/wr08008 · Cited by 19
“2002) and so the cohort born the previous spring would have passed through one epizootic when theywere old enough to have lost their innate resistance toRHDV (Morrisse et al. 1991; Ruvoën-Clouet et al. 2000; Robinson et al. 2002) and any measurable maternal antibodies (Cooke et al.”
BackgroundThe Molecular Virology of Enteric Viruses
Buesa, J., & Rodríguez-Díaz, J. (2016) · Viruses in Foods · doi:10.1007/978-3-319-30723-7_3 · Cited by 18
“It was previously determined that RHDV attaches to H type 2 HBGAs present on rabbit epithelial cells (Ruvöen-Clouet et al. 2000 ).”
BackgroundBuehler, M., Jesse, S. T., Kück, H., Lange, B., Koenig, P., Jo, W. K., Osterhaus, A. D. M. E., & Beineke, A. (2020) · BMC Veterinary Research · doi:10.1186/s12917-020-02386-4 · Cited by 19
Lopes, A. M., Breiman, A., Lora, M., Moullac‐Vaidye, B. L., Galanina, O. E., Nyström, K., Marchandeau, S., Gall-Reculé, G. L., Strive, T., Neimanis, A. S., et al. (2017) · Journal of Virology · doi:10.1128/jvi.01759-17 · Cited by 21
Self-citationZhu, J., Miao, Q., Tan, Y., Guo, H., Liu, T., Wang, B., Chen, Z., Li, C., & Liu, G. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.780924 · Cited by 17
“Indirect strategies that have been used in studying RHDV, including the identification of the histo-blood group antigen H type 2, A type 2, and B type 2 oligosaccharides as attachment factors (28, 29).”
MethodKhodayar-Pardo, P., Martínez-Costa, C., Carmona-Vicente, N., & Buesa, J. (2014) · The Pediatric Infectious Disease Journal · doi:10.1097/inf.0000000000000207 · Cited by 17
“1) to exclusively infect secretor individuals was the starting point for the hypothesis regarding HBGAs as receptors for caliciviruses stated by Ruvoen-Clouet in 2000.(32) This binding affinity was subsequently confirmed by assays with synthetic oligosaccharides.”
BackgroundFouchet, D., Pendu, J. L., Guitton, J., Guiserix, M., Marchandeau, S., & Pontier, D. (2009) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2008.11.021 · Cited by 17
Schwensow, N., Detering, H., Pederson, S., Mazzoni, C. J., Sinclair, R. G., Peacock, D. E., Kovaliski, J., Cooke, B. D., Fickel, J., & Sommer, S. (2017) · Molecular Ecology · doi:10.1111/mec.14228 · Cited by 19
The role of maternal antibodies in the emergence of severe disease as a result of fragmentation
Fouchet, D., Marchandeau, S., Bahi-Jaber, N., & Pontier, D. (2007) · Journal of the Royal Society Interface · doi:10.1098/rsif.2006.0189 · Cited by 16
“Newborns are resistant to these diseases because they lack the receptors on which the virus binds to infect the cells (Ruvoën-Clouet et al. 2000).”
BackgroundViruses for Landscape-Scale Therapy: Biological Control of Rabbits in Australia
Kerr, P. J., Hall, R. N., & Strive, T. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-1012-1_1 · Cited by 19
Cooke, B. (2008) · doi:10.1007/978-3-540-72446-9_21 · Cited by 15
“For example, Ruvoen-Clouet et al. (2000) found that entry of RHDV into rabbit cells involves ABH antigens, a mechanism in common with other caliciviruses including those affecting humans (Huang et al. 2003) and similarly, Lalani et al. (1999) reported that chemokine receptors on cells are probably the entry point for…”
Richardson, B., Phillips, S., Hayes, R. A., Sindhe, S., & Cooke, B. (2007) · doi:10.1071/wr06117 · Cited by 14
Urakova, N., Hall, R. N., Strive, T., & Frese, M. (2018) · Journal of Wildlife Diseases · doi:10.7589/2018-03-067 · Cited by 9
Marchandeau, S., Letty, J., Bertagnoli, S., Peralta, B., Boucraut-Baralon, C., & Reitz, F. (2004) · The Veterinary Record · doi:10.1136/vr.155.19.589 · Cited by 13
Parkes, J., Heyward, R. P., Henning, J., & Motha, M. (2004) · New Zealand Veterinary Journal · doi:10.1080/00480169.2004.36410 · Cited by 13
“A possible explanation is that an immune response was initiated in the mucosa of the alimentary tract of these animals after a large challenge of non-replicating virus was obtained from eating infected rabbits (Ruvoen-Clouet et al 2002 ).”
BackgroundChen, M., Song, Y.-H., Fan, Z., Jiang, P., Hu, B., Xue, J.-B., Wei, H., & Wang, F. (2014) · Virus Research · doi:10.1016/j.virusres.2014.01.004 · Cited by 12
Alternative attachment factors and internalization pathways for GIII.2 bovine noroviruses.
Mauroy, A., Gillet, L., Mathijs, E., Vanderplasschen, A., & Thiry, E. (2011) · Journal of General Virology · doi:10.1099/vir.0.030072-0 · Cited by 11
Song, Y., Wang, F., Fan, Z., Hu, B., Liu, X., Wei, H., Xue, J., Xu, W., & Qiu, R. (2015) · Journal of General Virology · doi:10.1099/jgv.0.000355 · Cited by 10
Genetic basis of host resistance to norovirus infection
Kindberg, E., & Svensson, L. (2009) · doi:10.2217/fvl.09.14 · Cited by 10
Molecular Virology of Enteric Viruses (with Emphasis on Caliciviruses)
Javier, B., & Rodríguez-Díaz, J. (2006) · Viruses in Foods · doi:10.1007/0-387-29251-9_3 · Cited by 10
“It was previously known that RHDV attaches to H type 2 histo-blood group oligosaccharide present on rabbit epithelial cells (Ruvöen-Clouet et al., 2000).”
BackgroundSong, Y., Fan, Z., Zuo, Y., Wei, H., Hu, B., Chen, M., Qiu, R., Xue, J., & Wang, F. (2017) · Archives of Virology · doi:10.1007/s00705-017-3509-8 · Cited by 10
“Caliciviruses, including noroviruses and RHDV, exploit host-cell histo-blood group antigens (HBGAs) for attachment, which results in the initiation of their replication cycle [12, 16, 18].”
Conley, M., Emmott, E., Orton, R., Taylor, D., Carneiro, D. G., Murata, K., Goodfellow, I. G., Hansman, G. S., & Bhella, D. (2017) · Journal of General Virology · doi:10.1099/jgv.0.000658 · Cited by 8
Nyström, K., Abrantes, J., Lopes, A. M., Moullac‐Vaidye, B. L., Marchandeau, S., Rocher, J., Ruvoën‐Clouet, N., Esteves, P. J., & LePendu, J. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004759 · Cited by 9
“To this aim the transfected cells were incubated for 30 min at 4°C with a 10 μg/ mL suspension of virus-like particles from a G2 RHDV strain prepared as described previously [27].”
BackgroundMethod
Metadata
- Authors
- Ruvoën-Clouet, N., Ganière, J. P., André-Fontaine, G., Blanchard, D., & Le Pendu, J.
- Affiliations
- <!--label omitted: 1-->Unité de Pathologie Infectieuse, Ecole Nationale Vétérinaire, 44307 Nantes cedex 03,1
- Oniris (FR)
- <!--label omitted: 2-->Etablissement de Transfusion Sanguine, Pays de la Loire, 44011 Nantes cedex 01,2 and
- <!--label omitted: 3-->INSERM U419, Institut de Biologie, 44093 Nantes,3 France
- Venue
- Journal of Virology
- Publisher
- American Society for Microbiology
- Published
- 2000-12-15
- Volume
- 74
- Issue
- 24
- Pages
- 11950-11954
- ISSN
- 0022-538X (ISSN-L)
- 1098-5514
- PMC
- PMC112478
- OpenAlex
- W2083189047
- Cited by
- 160
- References
- 0
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 7 · 2023: 4 · 2022: 1 · 2021: 6 · 2020: 10 · 2019: 3 · 2018: 6 · 2017: 6 · 2016: 8 · 2015: 11 · 2014: 15 · 2013: 9 · 2012: 6
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Virology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Blood groups and transfusion
- Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- rabbit hemorrhagic disease virus, ABH blood group antigens, H antigen, A antigen, viral attachment, hemagglutination, secretor status, Bombay phenotype, virus-like particles, recombinant capsid protein, UEA-I lectin, upper respiratory tract, gastrointestinal tract
- MeSH terms
- ABO Blood-Group System, Adult, Animals, Erythrocytes, Humans, Rabbits, Receptors, Virus, Hemorrhagic Disease Virus, Rabbit
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