RONALD IORIO

Summary

Affiliation: University of Massachusetts Medical School
Country: USA

Publications

  1. pmc Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor binding
    Elizabeth A Corey
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655 0122, USA
    J Virol 77:6913-22. 2003
  2. pmc Glycoprotein interactions in paramyxovirus fusion
    Ronald M Iorio
    Program in Immunology and Virology, University of Massachusetts Medical School, Worcester, MA 01655, USA and Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA, Tel 1 508 856 5257
    Future Virol 4:335-351. 2009
  3. pmc Paramyxoviruses: different receptors - different mechanisms of fusion
    Ronald M Iorio
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01655, USA
    Trends Microbiol 16:135-7. 2008
  4. pmc Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity
    R M Iorio
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655 0122, USA
    J Virol 75:1918-27. 2001
  5. pmc Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion
    Jianrong Li
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655 0122, USA
    J Virol 78:5299-310. 2004
  6. pmc Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
    Vanessa R Melanson
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Ave North, Worcester, MA 01655 0122, USA
    J Virol 78:13053-61. 2004
  7. pmc Decreased dependence on receptor recognition for the fusion promotion activity of L289A-mutated newcastle disease virus fusion protein correlates with a monoclonal antibody-detected conformational change
    Jianrong Li
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Ave No, Worcester, MA 01655 0122, USA
    J Virol 79:1180-90. 2005
  8. ncbi request reprint An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion
    Zhiyu Wang
    Department of Molecular Genetics and Microbiology, University of Massachusetts, 55 Lake Avenue North, 0165 0122, Worcester, MA, USA
    Virus Res 99:177-85. 2004
  9. pmc Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein
    Elizabeth A Corey
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA
    J Virol 81:9900-10. 2007
  10. pmc Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion
    Paul J Mahon
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01655, USA
    J Virol 82:10386-96. 2008

Collaborators

  • Siba K Samal
  • J P Langedijk
  • Elizabeth A Corey
  • Paul J Mahon
  • Jianrong Li
  • Anne M Mirza
  • Vanessa R Melanson
  • Judith G Alamares
  • Zhiyu Wang
  • Subbiah Elankumaran
  • Thomas A Musich
  • Edward Quinlan
  • Anne Mirza
  • Elizabeth Levandowsky

Detail Information

Publications15

  1. pmc Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor binding
    Elizabeth A Corey
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655 0122, USA
    J Virol 77:6913-22. 2003
    ..Instead, the interface mutations acted by weakening the interaction between HN and its receptor(s). The phenotype of these mutants correlates with the disruption of intermonomer subunit interactions...
  2. pmc Glycoprotein interactions in paramyxovirus fusion
    Ronald M Iorio
    Program in Immunology and Virology, University of Massachusetts Medical School, Worcester, MA 01655, USA and Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA, Tel 1 508 856 5257
    Future Virol 4:335-351. 2009
    ....
  3. pmc Paramyxoviruses: different receptors - different mechanisms of fusion
    Ronald M Iorio
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01655, USA
    Trends Microbiol 16:135-7. 2008
    ....
  4. pmc Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity
    R M Iorio
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655 0122, USA
    J Virol 75:1918-27. 2001
    ....
  5. pmc Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion
    Jianrong Li
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655 0122, USA
    J Virol 78:5299-310. 2004
    ..The data also indicate that the integrity of the HN dimer interface is critical to its receptor recognition activity...
  6. pmc Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
    Vanessa R Melanson
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Ave North, Worcester, MA 01655 0122, USA
    J Virol 78:13053-61. 2004
    ..These findings indicate that the intervening region is critical to the role of HN in the promotion of fusion and may be directly involved in its interaction with the homologous F protein...
  7. pmc Decreased dependence on receptor recognition for the fusion promotion activity of L289A-mutated newcastle disease virus fusion protein correlates with a monoclonal antibody-detected conformational change
    Jianrong Li
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Ave No, Worcester, MA 01655 0122, USA
    J Virol 79:1180-90. 2005
    ..This conformational change may reflect a destabilization of F structure induced by the L289A substitution, which may in turn indicate a lower energy requirement for fusion activation...
  8. ncbi request reprint An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion
    Zhiyu Wang
    Department of Molecular Genetics and Microbiology, University of Massachusetts, 55 Lake Avenue North, 0165 0122, Worcester, MA, USA
    Virus Res 99:177-85. 2004
    ..These findings localize the C-terminus of the F-specific domain in hPIV3 HN a full 10 residues closer to the membrane than previously shown...
  9. pmc Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein
    Elizabeth A Corey
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA
    J Virol 81:9900-10. 2007
    ..This points to an apparent difference in the way the MV and NDV glycoproteins interact to regulate fusion...
  10. pmc Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion
    Paul J Mahon
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01655, USA
    J Virol 82:10386-96. 2008
    ..These results confirm that neither the minimal interface form of HN nor the proposed drastic conformational change in the protein is required for fusion...
  11. pmc Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein
    Elizabeth A Corey
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA
    Virology 383:1-5. 2009
    ..These opposing results provide support for the existence of different mechanisms for the regulation of fusion by these two paramyxoviruses...
  12. pmc The interferon antagonistic activities of the V proteins from two strains of Newcastle disease virus correlate with their known virulence properties
    Judith G Alamares
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, MA 01655, USA
    Virus Res 147:153-7. 2010
    ..Four amino acid differences in the C-terminal region of V, as well as the N-terminal region, contribute to the difference in IFN-antagonistic activity between the two V proteins...
  13. pmc Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion
    Vanessa R Melanson
    Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655 0122, USA
    J Virol 80:623-33. 2006
    ..Our data support the idea that the F-interactive site on HN is defined by the stalk region of the protein...
  14. pmc Monoclonal antibody routinely used to identify avirulent strains of Newcastle disease virus binds to an epitope at the carboxy terminus of the hemagglutinin-neuraminidase protein and recognizes individual mesogenic and velogenic strains
    Judith G Alamares
    Department of Molecular Genetics and Microbiology, Program in Immunology and Virology, University of Massachusetts Medical School, 55 Lake Ave No, Worcester, MA 01655 0122, USA
    J Clin Microbiol 43:4229-33. 2005
    ..In addition, we have shown that AVS-I does recognize at least one mesogenic strain and one velogenic strain of the virus, calling into question the potential of this antibody as a diagnostic reagent for avirulent NDV strains...
  15. pmc Role of the two sialic acid binding sites on the newcastle disease virus HN protein in triggering the interaction with the F protein required for the promotion of fusion
    Paul J Mahon
    Department of Microbiology and Physiological Systems, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655 0002, USA
    J Virol 85:12079-82. 2011
    ....