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B Venkataram V Prasad - One of the best experts on this subject based on the ideXlab platform.

  • cell attachment protein vp8 of a Human Rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Sue E Crawford, Rita Czako, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, Mary K Estes, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the attachment of Human Rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of cells through interactions with specific cellular glycans. Animal Rotaviruses bind to glycans with terminal sialic acid, whereas Human Rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain Human Rotavirus strains bind to and infect cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific Human Rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the attachment protein of Human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans1,2,3,4. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells8, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

  • Cell attachment protein VP8* of a Human Rotavirus specifically interacts with A-type histo-blood group antigen
    Nature, 2012
    Co-Authors: Sue E Crawford, Rita Czako, David F Smith, Jacques Le Pendu, Mary K Estes, Nicolas W. Cortes-penfield, B Venkataram V Prasad
    Abstract:

    As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that 'sialidase-sensitive' animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas 'sialidase-insensitive' Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori and noroviruses. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world's population.

Liya Hu - One of the best experts on this subject based on the ideXlab platform.

  • cell attachment protein vp8 of a Human Rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Sue E Crawford, Rita Czako, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, Mary K Estes, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the attachment of Human Rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of cells through interactions with specific cellular glycans. Animal Rotaviruses bind to glycans with terminal sialic acid, whereas Human Rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain Human Rotavirus strains bind to and infect cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific Human Rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the attachment protein of Human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans1,2,3,4. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells8, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

Mary K Estes - One of the best experts on this subject based on the ideXlab platform.

  • milk oligosaccharides inhibit Human Rotavirus infectivity in ma104 cells
    Journal of Nutrition, 2017
    Co-Authors: Daniel R Laucirica, Mary K Estes, Vassilis Triantis, Ruud J W Schoemaker, Sasirekha Ramani
    Abstract:

    Background: Oligosaccharides in milk act as soluble decoy receptors and prevent pathogen adhesion to the infant gut. Milk oligosaccharides reduce infectivity of a porcine Rotavirus strain; however, the effects on Human Rotaviruses are less well understood.Objective: In this study, we determined the effect of specific and abundant milk oligosaccharides on the infectivity of 2 globally dominant Human Rotavirus strains.Methods: Four milk oligosaccharides-2'-fucosyllactose (2'FL), 3'-sialyllactose (3'SL), 6'-sialyllactose (6'SL), and galacto-oligosaccharides-were tested for their effects on the infectivity of Human Rotaviruses G1P[8] and G2P[4] through fluorescent focus assays on African green monkey kidney epithelial cells (MA104 cells). Oligosaccharides were added at different time points in the infectivity assays. Infections in the absence of oligosaccharides served as controls.Results: When compared with infections in the absence of glycans, all oligosaccharides substantially reduced the infectivity of both Human Rotavirus strains in vitro; however, virus strain-specific differences in effects were observed. Compared with control infections, the maximum reduction in G1P[8] infectivity was seen with 2'FL when added after the onset of infection (62% reduction, P < 0.01), whereas the maximum reduction in G2P[4] infectivity was seen with the mixture of 3'SL + 6'SL when added during infection (73% reduction, P < 0.01). The mixture of 3'SL + 6'SL at the same ratio as is present in breast milk was more potent in reducing G2P[4] infectivity (73% reduction, P < 0.01) than when compared with 3'SL (47% reduction) or 6'SL (40% reduction) individually. For all oligosaccharides the reduction in infectivity was mediated by an effect on the virus and not on the cells.Conclusions: Milk oligosaccharides reduce the infectivity of Human Rotaviruses in MA104 cells, primarily through an effect on the virus. Although breastfed infants are directly protected, the addition of specific oligosaccharides to infant formula may confer these benefits to formula-fed infants.

  • cell attachment protein vp8 of a Human Rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Sue E Crawford, Rita Czako, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, Mary K Estes, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the attachment of Human Rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of cells through interactions with specific cellular glycans. Animal Rotaviruses bind to glycans with terminal sialic acid, whereas Human Rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain Human Rotavirus strains bind to and infect cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific Human Rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the attachment protein of Human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans1,2,3,4. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells8, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

  • Cell attachment protein VP8* of a Human Rotavirus specifically interacts with A-type histo-blood group antigen
    Nature, 2012
    Co-Authors: Sue E Crawford, Rita Czako, David F Smith, Jacques Le Pendu, Mary K Estes, Nicolas W. Cortes-penfield, B Venkataram V Prasad
    Abstract:

    As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that 'sialidase-sensitive' animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas 'sialidase-insensitive' Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori and noroviruses. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world's population.

Sue E Crawford - One of the best experts on this subject based on the ideXlab platform.

  • cell attachment protein vp8 of a Human Rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Sue E Crawford, Rita Czako, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, Mary K Estes, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the attachment of Human Rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of cells through interactions with specific cellular glycans. Animal Rotaviruses bind to glycans with terminal sialic acid, whereas Human Rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain Human Rotavirus strains bind to and infect cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific Human Rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the attachment protein of Human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans1,2,3,4. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells8, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

  • Cell attachment protein VP8* of a Human Rotavirus specifically interacts with A-type histo-blood group antigen
    Nature, 2012
    Co-Authors: Sue E Crawford, Rita Czako, David F Smith, Jacques Le Pendu, Mary K Estes, Nicolas W. Cortes-penfield, B Venkataram V Prasad
    Abstract:

    As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that 'sialidase-sensitive' animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas 'sialidase-insensitive' Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori and noroviruses. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world's population.

Rita Czako - One of the best experts on this subject based on the ideXlab platform.

  • cell attachment protein vp8 of a Human Rotavirus specifically interacts with a type histo blood group antigen
    Nature, 2012
    Co-Authors: Liya Hu, Sue E Crawford, Rita Czako, Nicolas W Cortespenfield, David F Smith, Jacques Le Pendu, Mary K Estes, B Venkataram V Prasad
    Abstract:

    This crystallographic study shows the attachment of Human Rotavirus VP8* to histo blood group A antigen, and suggests how changes within the structure of VP8* could allow switching from sialylated to non-sialylated glycan receptor. Rotaviruses are the major pathogens of infantile gastroenteritis. They attach to the surfaces of cells through interactions with specific cellular glycans. Animal Rotaviruses bind to glycans with terminal sialic acid, whereas Human Rotavirus strains are sialidase insensitive. Venkataram Prasad and colleagues now show that certain Human Rotavirus strains bind to and infect cells through A-type histo-blood group antigen (HBGA), suggesting that susceptibility to specific Human Rotavirus strains might be influenced by different blood-group antigens, a phenomenon reported in Helicobacter pylori and norovirus infection. Crystallographic studies show how HBGA binds to the attachment protein of Human norovirus (VP8), and suggest how subtle changes in the structure of VP8 might allow receptor switching. As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans1,2,3,4. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that ‘sialidase-sensitive’ animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas ‘sialidase-insensitive’ Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies1,3,6,7, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells8, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori9 and noroviruses10. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world’s population.

  • Cell attachment protein VP8* of a Human Rotavirus specifically interacts with A-type histo-blood group antigen
    Nature, 2012
    Co-Authors: Sue E Crawford, Rita Czako, David F Smith, Jacques Le Pendu, Mary K Estes, Nicolas W. Cortes-penfield, B Venkataram V Prasad
    Abstract:

    As with many other viruses, the initial cell attachment of Rotaviruses, which are the major causative agent of infantile gastroenteritis, is mediated by interactions with specific cellular glycans. The distally located VP8* domain of the Rotavirus spike protein VP4 (ref. 5) mediates such interactions. The existing paradigm is that 'sialidase-sensitive' animal Rotavirus strains bind to glycans with terminal sialic acid (Sia), whereas 'sialidase-insensitive' Human Rotavirus strains bind to glycans with internal Sia such as GM1 (ref. 3). Although the involvement of Sia in the animal strains is firmly supported by crystallographic studies, it is not yet known how VP8* of Human Rotaviruses interacts with Sia and whether their cell attachment necessarily involves sialoglycans. Here we show that VP8* of a Human Rotavirus strain specifically recognizes A-type histo-blood group antigen (HBGA) using a glycan array screen comprised of 511 glycans, and that virus infectivity in HT-29 cells is abrogated by anti-A-type antibodies as well as significantly enhanced in Chinese hamster ovary cells genetically modified to express the A-type HBGA, providing a novel paradigm for initial cell attachment of Human Rotavirus. HBGAs are genetically determined glycoconjugates present in mucosal secretions, epithelia and on red blood cells, and are recognized as susceptibility and cell attachment factors for gastric pathogens like Helicobacter pylori and noroviruses. Our crystallographic studies show that the A-type HBGA binds to the Human Rotavirus VP8* at the same location as the Sia in the VP8* of animal Rotavirus, and suggest how subtle changes within the same structural framework allow for such receptor switching. These results raise the possibility that host susceptibility to specific Human Rotavirus strains and pathogenesis are influenced by genetically controlled expression of different HBGAs among the world's population.