Histo-blood group antigens: A common niche for norovirus and rotavirus

Expert Reviews in Molecular Medicine

Volumn 16, Issue , 2014, Pages

  Tan, Ming ^a   Jiang, Xi ^a  

^a UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1,3 FUCOSYLTRANSFERASE; BLOOD GROUP A ANTIGEN; BLOOD GROUP ANTIGEN; BLOOD GROUP B ANTIGEN; BLOOD GROUP O ANTIGEN; FUCOSYLTRANSFERASE; HISTO BLOOD GROUP ANTIGEN; SECRETOR ANTIGEN; UNCLASSIFIED DRUG;

ACUTE GASTROENTERITIS; ANTIGEN FUNCTION; ANTIGEN RECOGNITION; BLOOD GROUP ABO SYSTEM; CENTRAL BINDING POCKET; CRYSTAL STRUCTURE; EXPLORATORY RESEARCH; FUT2 GENE; FUT3 GENE; GENETIC CONSERVATION; GENETIC POLYMORPHISM; GENETIC VARIABILITY; HELICOBACTER INFECTION; HELICOBACTER PYLORI; HGBA GENE; HOST PATHOGEN INTERACTION; HUMAN; MOLECULAR EPIDEMIOLOGY; MOLECULAR EVOLUTION; NONHUMAN; NOROVIRUS; NOROVIRUS INFECTION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN STRUCTURE; REVIEW; ROTAVIRUS; VIRAL GASTROENTERITIS; VIRUS CAPSID; VIRUS CELL INTERACTION; VIRUS CLASSIFICATION; VIRUS TRANSMISSION; ANIMAL; CALICIVIRUS INFECTION; GASTROENTERITIS; GENETICS; METABOLISM; PHYSIOLOGY; ROTAVIRUS INFECTION; VIROLOGY; VIRUS ATTACHMENT;

ANIMALS; BLOOD GROUP ANTIGENS; CALICIVIRIDAE INFECTIONS; EVOLUTION, MOLECULAR; GASTROENTERITIS; HOST-PATHOGEN INTERACTIONS; HUMANS; NOROVIRUS; POLYMORPHISM, GENETIC; ROTAVIRUS; ROTAVIRUS INFECTIONS; VIRUS ATTACHMENT;

EID: 84915803056     PISSN: 14623994     EISSN: None     Source Type: Journal    
DOI: 10.1017/erm.2014.2     Document Type: Review

References (107)

1. Marionneau, S. et al. (2001) ABH and Lewis histoblood group antigens, a model for the meaning of oligosaccharide diversity in the face of a changing world. Biochimie 83, 565-573
2. Tan, M. and Jiang, X. (2005) Norovirus and its histoblood group antigen receptors: an answer to a historical puzzle. Trends in Microbiology 13, 285-293
3. Tan, M. and Jiang, X. (2007) Norovirus-host interaction: implications for disease control and prevention. Expert Reviews in Molecular Medicine 9, 1-22
4. Tan, M. and Jiang, X. (2010) Norovirus gastroenteritis, carbohydrate receptors, and animal models. PLoS Pathogens 6, e1000983
5. Tan, M. and Jiang, X. (2010) Virus-host interaction and cellular receptors of caliciviruses. In Caliciruses (Hansman G., Jiang X. and Green K., eds), pp. 111-130, Caister Academic Press, Norwich
6. Hutson, A.M., Atmar, R.L. and Estes, M.K. (2004) Norovirus disease: changing epidemiology and host susceptibility factors. Trends in Microbiology 12, 279-287
7. Hutson, A.M. et al. (2002) Norwalk virus infection and disease is associated with ABO histo-blood group type. The Journal of Infectious Diseases 185, 1335-1337
8. Lindesmith, L. et al. (2003) Human susceptibility and resistance to Norwalk virus infection. Nature Medicine 9, 548-553
9. Frenck, R. et al. (2012) Predicting susceptibility to norovirus GII.4 by use of a challenge model involving humans. The Journal of Infectious Diseases 206, 1386-1393
10. Tan, M. et al. (2008) Outbreak studies of a GII-3 and a GII-4 norovirus revealed an association between HBGA phenotypes and viral infection. Journal of Medical Virology 80, 1296-1301
11. Bu,W. et al. (2008) Structural basis for the receptor binding specificity of Norwalk virus. Journal of Virology 82, 5340-5347
12. Cao, S. et al. (2007) Structural basis for the recognition of blood group trisaccharides by norovirus. Journal of Virology 81, 5949-5957
13. Chen, Y. et al. (2011) Crystallography of a lewisbinding norovirus, elucidation of strain-specificity to the polymorphic human histo-blood group antigens. PLoS Pathogens 7, e1002152
14. Choi, J.M. et al. (2008) Atomic resolution structural characterization of recognition of histo-blood group antigens by Norwalk virus. Proceedings of the National Academy of Sciences of the United States of America 105, 9175-9180
15. Hansman, G.S. et al. (2011) Crystal structures of GII.10 and GII.12 norovirus protruding domains in complex with histo-blood group antigens reveal details for a potential site of vulnerability. Journal of Virology 85, 6687-6701
16. Shanker, S. et al. (2011) Structural analysis of histoblood group antigen binding specificity in a norovirus GII.4 epidemic variant: implications for epochal evolution. Journal of Virology 85, 8635-8645
17. Kubota, T. et al. (2012) Structural basis for the recognition of Lewis antigens by genogroup I norovirus. Journal of Virology 86, 11138-11150
18. Bertolotti-Ciarlet, A. et al. (2002) Structural requirements for the assembly of Norwalk viruslike particles. Journal of Virology 76, 4044-4055
19. Zarate, S. et al. (2003) Interaction of rotaviruses with Hsc70 during cell entry is mediated by VP5. Journal of Virology 77, 7254-7260
20. Lopez, S. and Arias, C.F. (2004) Multistep entry of rotavirus into cells: a Versaillesque dance. Trends in Microbiology 12, 271-278
21. Lopez, S. and Arias, C.F. (2006) Early steps in rotavirus cell entry. Current Topics in Microbiology and Immunology 309, 39-66
22. Guo, C.T. et al. (1999) Ganglioside GM(1a) on the cell surface is involved in the infection by human rotavirus KUN and MO strains. Journal of Biochemistry (Tokyo) 126, 683-688
23. Delorme, C. et al. (2001) Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope. Journal of Virology 75, 2276-2287
24. Isa, P. et al. (2004) Rotavirus RRV associates with lipid membrane microdomains during cell entry. Virology 322, 370-381
25. Coulson, B.S., Londrigan, S.L. and Lee, D.J. (1997) Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells. Proceedings of the National Academy of Sciences of the United States of America 94, 5389-5394
26. Hewish, M.J., Takada, Y. and Coulson, B.S. (2000) Integrins alpha2beta1 and alpha4beta1 can mediate SA11 rotavirus attachment and entry into cells. Journal of Virology 74, 228-236
27. Graham, K.L. et al. (2003) Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry. Journal of Virology 77, 9969-9978
28. Hu, L. et al. (2012) Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen. Nature 485, 256-259
29. Huang, P. et al. (2012) Spike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner. Journal of Virology 86, 4833-4843
30. Liu, Y. et al. (2012) Rotavirus VP8*: phylogeny, host range, and interaction with histo-blood group antigens. Journal of Virology 86, 9899-9910
31. Aspholm-Hurtig, M. et al. (2004) Functional adaptation of BabA, the H. pylori ABO blood group antigen binding adhesin. Science (New York, NY) 305, 519-522
32. Aspholm, M. et al. (2006) SabA is the H. pylori hemagglutinin and is polymorphic in binding to sialylated glycans. PLoS Pathogens 2, e110
33. Bok, K. and Green, K.Y. (2012) Norovirus gastroenteritis in immunocompromised patients. New England Journal of Medicine 367, 2126-2132
34. Rayani, A. et al. (2007) Rotavirus infections in paediatric oncology patients: a matched-pairs analysis. Scandinavian Journal of Gastroenterology 42, 81-87
35. Tan, M., Hegde, R.S. and Jiang, X. (2004) The P domain of norovirus capsid protein forms dimer and binds to histo-blood group antigen receptors. Journal of Virology 78, 6233-6242
36. Tan, M. et al. (2003) Mutations within the P2 domain of norovirus capsid affect binding to human histo-blood group antigens: evidence for a binding pocket. Journal ofVirology 77, 12562-12571
37. Prasad, B.V. et al. (1999) X-ray crystallographic structure of the Norwalk virus capsid. Science 286, 287-290
38. Jiang, X. et al. (1992) Expression, self-assembly, and antigenicity of the Norwalk virus capsid protein. Journal of Virology 66, 6527-6532
39. Huang, P. et al. (2003) Noroviruses bind to human ABO, Lewis, and secretor histo-blood group antigens: identification of 4 distinct strain-specific patterns. The Journal of Infectious Diseases 188, 19-31
40. Huang, P. et al. (2005) Norovirus and histo-blood group antigens: demonstration of a wide spectrum of strain specificities and classification of two major binding groups among multiple binding patterns. Journal of Virology 79, 6714-6722
41. Harrington, P.R. et al. (2004) Norovirus capture with histo-blood group antigens reveals novel virus-ligand interactions. Journal of Virology 78, 3035-3045
42. Lindesmith, L.C. et al. (2008) Mechanisms of GII.4 norovirus persistence in human populations. PLoS Medicine 5, e31
43. Tan, M. et al. (2011) Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles. Virology 410, 345-352
44. Tan, M. and Jiang, X. (2005) The p domain of norovirus capsid protein forms a subviral particle that binds to histo-blood group antigen receptors. Journal of Virology 79, 14017-14030
45. Tan, M. and Jiang, X. (2012) Norovirus P particle, a subviral nanoparticle for vaccine development against norovirus, rotavirus and influenza virus. Nanomedicine 7, 1-9
46. Tan, M. et al. (2011) Norovirus P Particle as a Platform for Antigen Presentation. Procedia in Vaccinology 4, 19-26
47. Tan, M. and Jiang, X. (2012) Norovirus P particle: a subviral nanoparticle for vaccine development against norovirus, rotavirus and influenza virus. Nanomedicine (Lond) 7, 889-897
48. Tan, M. et al. (2008) Elucidation of strain-specific interaction of a GII-4 norovirus with HBGA receptors by site-directed mutagenesis study. Virology 379, 324-334
49. Tan, M. et al. (2009) Conservation of carbohydrate binding interfaces: evidence of human HBGA selection in norovirus evolution. PLoSONE 4, e5058
50. Dai, Y.C. et al. (2012) Evaluation of anti-norovirus IgY from egg yolk of chickens immunized with norovirus P particles. Journal of Virological Methods 186, 126-131
51. Dai, Y.C. et al. (2013) A dual chicken IgY against rotavirus and norovirus. Antiviral Research 97, 293-300
52. Aad, G. et al. (2013) Measurement of Z boson production in Pb-Pb collisions at sqrt[s-{NN}] = 2.76TeV with the ATLAS detector. Physical Review Letters 110, 022301
53. Greenberg, H.B. et al. (1981) Proteins of Norwalk virus. Journal of Virology 37, 994-999
54. Hardy, M.E. et al. (1995) Specific proteolytic cleavage of recombinant Norwalk virus capsid protein. Journal of Virology 69, 1693-1698
55. Tan, M., Meller, J. and Jiang, X. (2006) C-terminal arginine cluster is essential for receptor binding of expert reviews http://www.expertreviews.org/ in molecular medicine norovirus capsid protein. Journal of Virology 80, 7322-7331
56. Settembre, E.C. et al. (2011) Atomic model of an infectious rotavirus particle. The EMBO Journal 30, 408-416
57. Trask, S.D., Ogden, K.M. and Patton, J.T. (2012) Interactions among capsid proteins orchestrate rotavirus particle functions. Current Opinion in Virology 2, 373-379
58. Ruggeri, F.M. and Greenberg, H.B. (1991) Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture. Journal of Virology 65, 2211-2219
59. Pesavento, J.B. et al. (2005) pH-induced conformational change of the rotavirus VP4 spike: implications for cell entry and antibody neutralization. Journal of Virology 79, 8572-8580
60. Fiore, L., Greenberg, H.B. and Mackow, E.R. (1991) The VP8 fragment of VP4 is the rhesus rotavirus hemagglutinin. Virology 181, 553-563
61. Patton, J.T., Hua, J. and Mansell, E.A. (1993) Location of intrachain disulfide bonds in the VP5* and VP8* trypsin cleavage fragments of the rhesus rotavirus spike protein VP4. Journal of Virology 67, 4848-4855
62. Padilla-Noriega, L. et al. (1995) Identification of two independent neutralization domains on the VP4 trypsin cleavage products VP5* and VP8* of human rotavirus ST3. Virology 206, 148-154
63. Arias, C.F. et al. (2002) Molecular biology of rotavirus cell entry. Archives of Medical Research 33, 356-361
64. Monnier,N. et al. (2006) High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain. Journal of Virology 80, 1513-1523
65. Zheng, D.P. et al. (2006) Norovirus classification and proposed strain nomenclature. Virology 346, 312-323
66. Esona, M.D. et al. (2010) Reassortant group A rotavirus from straw-colored fruit bat (Eidolon helvum). Emerging Infectious Diseases 16, 1844-1852
67. Khamrin, P. et al. (2006) Emergence of human G9 rotavirus with an exceptionally high frequency in children admitted to hospital with diarrhea in Chiang Mai, Thailand. Journal of Medical Virology 78, 273-280
68. Le Pendu, J. (2004) Histo-blood group antigen and human milk oligosaccharides: genetic polymorphism and risk of infectious diseases. Advances in Experimental Medicine and Biology 554, 135-143
69. Ravn, V. and Dabelsteen, E. (2000) Tissue distribution of histo-blood group antigens. APMIS 108, 1-28
70. Hutson, A.M. et al. (2003) Norwalk virus-like particle hemagglutination by binding to h histobloodgroupantigens. Journal ofVirology77,405-415
71. Hutson, A.M. et al. (2005) Norwalk virus infection associates with secretor status genotyped from sera. Journal of Medical Virology 77, 116-120
72. Rockx, B.H. et al. (2005) Association of histo-blood group antigens and susceptibility to norovirus infections. The Journal of Infectious Diseases 191, 749-754
73. Duizr, E. et al. (2004) Laboratory efforts to cultivate noroviruses. The Journal of General Virology 85(Pt 1), 79-87
74. Lindesmith, L. et al. (2005) Cellular and humoral immunity following Snow Mountain virus challenge. Journal of Virology 79, 2900-2909
75. Ruvoen-Clouet, N. et al. (2000) Binding of rabbit hemorrhagic disease virus to antigens of the ABH histo-blood group family. Journal of Virology 74, 11950-11954
76. Nystrom, K. et al. (2011) Histo-blood group antigens act as attachment factors of rabbit hemorrhagic disease virus infection in a virus strain-dependent manner. PLoS Pathogens 7, e1002188
77. Farkas, T. et al. (2010) Genetic diversity and histoblood group antigen interactions of rhesus enteric caliciviruses. Journal of Virology 84, 8617-8625
78. Taube, S. et al. (2012) Murine noroviruses bind glycolipid and glycoprotein attachment receptors in a strain-dependent manner. Journal of Virology 86, 5584-5593
79. Stuart, A.D. and Brown, T.D. (2007) Alpha2,6- linked sialic acid acts as a receptor for Feline calicivirus. The Journal of General Virology 88(Pt 1), 177-186
80. Zakhour, M. et al. (2010) Bovine norovirus: carbohydrate ligand, environmental contamination, and potential cross-species transmission via oysters. Applied and Environmental Microbiology 76, 6404-6411
81. Ossiboff, R.J. and Parker, J.S. (2007) Identification of regions and residues in feline junctional adhesion molecule required for feline calicivirus binding and infection. Journal of Virology 81, 13608-13621
82. Liu, Y. et al. (2013) Poly-LacNAc as an Age-Specific Ligand for Rotavirus P[11] in neonates and infants. PLoS ONE [Electronic Resource] 8, e78113
83. Rotavirus surveillance - worldwide, 2009. MMWR Morbidity and Mortality Weekly Report 60, 514-516
84. Shirato, H. et al. (2008) Noroviruses distinguish between type 1 and type 2 histo-blood group antigens for binding. Journal of Virology 82, 10756-10767
85. Blanchard, H. et al. (2007) Insight into host cell carbohydrate- recognition by human and porcine rotavirus from crystal structures of the virion spike associated carbohydrate-binding domain (VP8*). Journal of Molecular Biology 367, 1215-1226
86. Dormitzer, P.R. et al. (2002) The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. The EMBO Journal 21, 885-897
87. Ablikim, M. et al. (2006) Observation of two new N* peaks in J/psi - >ppi n and ppi + n decays. Physical Review Letters 97, 062001
88. de Rougemont, A. et al. (2011) Qualitative and quantitative analysis of the binding of GII.4 norovirus variants onto human blood group antigens. Journal of Virology 85, 4057-4070
89. Bishop, J.R. and Gagneux, P. (2007) Evolution of carbohydrate antigens - microbial forces shaping host glycomes? Glycobiology 17, 23R-34R
90. Zakhour, M. et al. (2009) The alphaGal epitope of the histo-blood group antigen family is a ligand for bovine norovirus Newbury2 expected to prevent cross-species transmission. PLoS Pathogens 5, e1000504
91. Souza, M. et al. (2007) Cytokine and antibody responses in gnotobiotic pigs after infection with human norovirus genogroup II.4 (HS66 strain). Journal of Virology 81, 9183-9192
92. Souza, M. et al. (2008) Pathogenesis and immune responses in gnotobiotic calves after infection with the genogroup II.4-HS66 strain of human norovirus. Journal of Virology 82, 1777-1786
93. Tian, P. et al. (2010) Specificity and kinetics of norovirus binding to magnetic bead-conjugated histo-blood group antigens. Journal of Applied Microbiology 109, 1753-1762
94. Le Pendu, J. et al. (2006) Mendelian resistance to human norovirus infections. Seminars in Immunology 18, 375-86
95. de Rougemont, A. et al. (2011) Qualitative and quantitative analysis of the binding of GII.4 norovirus variants onto human blood group antigens. Journal of Virology 85, 4057-4070
96. Tan, M. and Jiang, X. (2011) Norovirus-host interaction: multi-selections by the human HBGAs. Trends in Microbiology 19, 382-388
97. Yang, Y. et al. (2010) Genetic and phenotypic characterization of GII-4 noroviruses that circulated during 1987 to 2008. Journal of Virology 84, 9595-9607
98. Lindesmith, L.C. et al. (2012) Immunogenetic mechanisms driving norovirus GII.4 antigenic variation. PLoS Pathogens 8, e1002705
99. Parra, G.I. et al. (2012) Multiple antigenic sites are involved in blocking the interaction of GII.4 norovirus capsid with ABH histo-blood group antigens. Journal of Virology 86, 7414-7426
100. Lindesmith, L.C. et al. (2012) Monoclonal antibodybased antigenic mapping of norovirus GII.4-2002. Journal of Virology 86, 873-883
101. Niv, Y. et al. (1996) Helicobacter pylori infection and blood groups. The American Journal of Gastroenterology 91, 101-104
102. May, S.J., Blackwell, C.C. and Weir, D.M. (1989) Lewis a blood group antigen of non-secretors: a receptor for candida blastospores. FEMS Microbiology Immunology 1, 407-409
103. Darwazeh, A.M. et al. (1990) The relationship between colonisation, secretor status and in-vitro adhesion of Candida albicans to buccal epithelial cells from diabetics. Journal of Medical Microbiology 33, 43-49
104. Burford-Mason, A.P., Weber, J.C. and Willoughby, J.M. (1988) Oral carriage of Candida albicans, ABO blood group and secretor status in healthy subjects. Journal of Medical and Veterinary Mycology: Bimonthly Publication of the International Society for Human and Animal Mycology 26, 49-56
105. Shin, E.-S. et al. (2003) The relationship between oral Candida carriage and the secretor status of blood group antigens in saliva. Oral Surgery, Oral Medicine, Oral Pathology, Oral Radiology, and Endodontics 96, 48-53
106. Bush, R.M. et al. (1999) Predicting the evolution of human influenza A. Science 286, 1921-1925
107. Ha, Y. et al. (2001) X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proceedings of the National Academy of Sciences of the United States of America 98, 11181-11186