title: A Y526Q mutation in the Newcastle disease virus HN protein reduces its functional activities and attenuates virus replication and pathogenicity.
abstract: The hemagglutinin-neuraminidase (HN) protein of Newcastle disease virus (NDV) is a multifunctional protein that plays a crucial role in virus infectivity. In this study, using the mesogenic strain Beaudette C (BC), we mutated three conserved amino acids thought to be part of the binding/catalytic active site in the HN protein. We also mutated five additional residues near the proposed active site that are nonconserved between BC and the avirulent strain LaSota. The eight recovered NDV HN mutants were assessed for effects on biological activities. While most of the mutations had surprisingly little effect, mutation at conserved residue Y526 reduced the neuraminidase, receptor binding, and fusion activities and attenuated viral virulence in eggs and young birds.
authors.affiliation: Virginia-Maryland Regional College of Veterinary Medicine, University of Maryland, College Park, MD 20742, USA.
authors.forename: Sunil K
authors.initials: SK
authors.lastname: Khattar
authors.forename: Yongqi
authors.initials: Y
authors.lastname: Yan
authors.forename: Aruna
authors.initials: A
authors.lastname: Panda
authors.forename: Peter L
authors.initials: PL
authors.lastname: Collins
authors.forename: Siba K
authors.initials: SK
authors.lastname: Samal
mesh_terms: D000818:Animals; D002642:Chick Embryo; D015707:HN Protein / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D008968:Molecular Conformation; D020125:Mutation, Missense; D009521:Newcastle Disease / Q000821:virology*; D009522:Newcastle disease virus / Q000737:chemistry / Q000235:genetics / Q000472:pathogenicity* / Q000502:physiology; D011487:Protein Conformation; D014779:Virus Replication
chemical_list: D015707:HN Protein