Loading...
Header Logo
Keywords
Last Name
Institution

Connection

Search Results to Ronald M Iorio PhD

This is a "connection" page, showing the details of why an item matched the keywords from your search.

                     
                     

One or more keywords matched the following properties of Iorio, Ronald

PropertyValue
overview

Academic Background

BA, University of Massachusetts
MS, PhD, Boston College

Viral pathogenesis and virulence; viral entry and the mechanism of virus-induced membrane fusion; viral glycoproteins and receptors

Paramyxoviruses are enveloped, negative-stranded RNA viruses, which include clinically important human pathogens such as measles, mumps, parainfluenza, and respiratory syncytial viruses; important animal pathogens, such as Newcastle disease (NDV), and Sendai viruses; and, emerging viruses such as Nipah and Hendra. Though primarily respiratory pathogens, several members of the group are capable of causing central nervous system disease. We are interested in understanding the molecular basis for the pathogenesis and virulence of this group of viruses.

Paramyxoviruses gain entry into the cell by mediating direct fusion of the virus and cell membranes. Fusion involves a virus-specific interaction between the two viral surface glycoprotein spikes, the attachment protein and the fusion protein. Mediated through this interaction, receptor binding by the attachment protein is thought to trigger a conformational change in the fusion protein from a metastable, pre-fusion form to a fusion-active form. We are exploring various aspects of the fusion process for several paramyxoviruses. We have developed a sensitive co-immunoprecipitation assay to detect the attachment-fusion protein complex at the cell surface and have identified mutations in several paramyxovirus attachment proteins that block fusion by modulating the interaction between the two surface glycoproteins. Our evidence is consistent with the idea that the attachment protein - fusion protein interaction regulates fusion by a different mechanism in viruses such as NDV, which recognize the ubiquitous sugar sialic acid as receptor, and viruses such as measles, which recognize specific proteins as receptors.

NDV virulence involves contributions from at least three viral proteins. The site of cleavage activation of the fusion protein is a major determinant of virulence. However, recent evidence has revealed that the attachment protein also plays a role. In addition, the V protein, produced by RNA editing from the P gene, is an interferon antagonist and thereby also plays a role in virulence. We are interested in understanding the mechanisms by which all three proteins exert their effects on NDV virulence, as well as the basis for the differences in virulence observed among members of the NDV serotype.

Rotation Projects

Rotation Projects

Rotation projects will involve construction of site-directed mutants or chimeras of either the attachment, fusion or V proteins and evaluation of their ability to promote the functions attributed to that protein. Depending on the target protein, the structure and function of each mutated or chimeric protein will be evaluated using several functional assays. These include flow cytometry (cell surface expression and antibody recognition), hemadsorption of red blood cells (receptor recognition activity), neuraminidase (receptor destroying activity), content mixing reporter gene assay (fusion), immunoprecipitation and SDS-PAGE (protein structure) and co-immunoprecipitation (determination of the ability of the mutated proteins to interact with a co-expressed protein). For the V protein, we will be evaluating various aspects of its interferon inhibitory activity.


One or more keywords matched the following items that are connected to Iorio, Ronald

Item TypeName
Academic Article Inhibition of fusion by neutralizing monoclonal antibodies to the haemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
Academic Article Functional chimeric HN glycoproteins derived from Newcastle disease virus and human parainfluenza virus-3.
Academic Article Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domain.
Academic Article 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.
Academic Article A single amino acid substitution in the hemagglutinin-neuraminidase of Newcastle disease virus results in a protein deficient in both functions.
Academic Article Neutralization map of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus: domains recognized by monoclonal antibodies that prevent receptor recognition.
Academic Article Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion.
Academic Article An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion.
Academic Article 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.
Academic Article Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.
Academic Article Functional and neutralization profile of seven overlapping antigenic sites on the HN glycoprotein of Newcastle disease virus: monoclonal antibodies to some sites prevent viral attachment.
Academic Article Identification of amino acid residues important to the neuraminidase activity of the HN glycoprotein of Newcastle disease virus.
Academic Article Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptors.
Academic Article Localization of a region in the fusion protein of avian metapneumovirus that modulates cell-cell fusion.
Academic Article 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.
Academic Article Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike.
Academic Article Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion.
Academic Article 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.
Academic Article 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.
Academic Article Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion.
Academic Article 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.
Academic Article Paramyxoviruses: different receptors - different mechanisms of fusion.
Academic Article Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion protein.
Academic Article 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.
Academic Article Individual N-glycans added at intervals along the stalk of the Nipah virus G protein prevent fusion but do not block the interaction with the homologous F protein.
Academic Article A mutation in the stalk of the newcastle disease virus hemagglutinin-neuraminidase (HN) protein prevents triggering of the F protein despite allowing efficient HN-F complex formation.
Academic Article Quantitative basic residue requirements in the cleavage-activation site of the fusion glycoprotein as a determinant of virulence for Newcastle disease virus.
Academic Article Reducing agent-sensitive dimerization of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus correlates with the presence of cysteine at residue 123.
Academic Article Glycosylation within an antigenic site on the HN glycoprotein of Newcastle disease virus interferes with its role in the promotion of membrane fusion.
Academic Article Site-directed mutagenesis of a conserved hexapeptide in the paramyxovirus hemagglutinin-neuraminidase glycoprotein: effects on antigenic structure and function.
Academic Article Structure and function of a membrane anchor-less form of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
Concept Protein Binding
Concept HN Protein
Concept Protein Folding
Concept Protein Interaction Mapping
Concept Protein Precursors
Concept Protein Structure, Secondary
Concept Protein Structure, Tertiary
Concept Protein Multimerization
Concept Protein Conformation
Academic Article Roles of the putative integrin-binding motif of the human metapneumovirus fusion (f) protein in cell-cell fusion, viral infectivity, and pathogenesis.

Search Criteria
  • Protein S