title: 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.
abstract: Newcastle disease virus (NDV)-induced membrane fusion requires an interaction between the hemagglutinin-neuraminidase (HN) attachment and the fusion (F) proteins, triggered by HN's binding to receptors. NDV HN has two sialic acid binding sites: site I, which also mediates neuraminidase activity, and site II, which straddles the membrane-distal end of the dimer interface. By characterizing the effect on receptor binding avidity and F-interactive capability of HN dimer interface mutations, we present evidence consistent with (i) receptor engagement by site I triggering the interaction with F and (ii) site II functioning to maintain high-avidity receptor binding during the fusion process.
authors: Department of Microbiology and Physiological Systems, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655-0002, USA.
authors: Paul J
authors: PJ
authors: Mahon
authors: Anne M
authors: AM
authors: Mirza
authors: Ronald M
authors: RM
authors: Iorio
mesh_terms: D001665:Binding Sites; D015707:HN Protein / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D009522:Newcastle disease virus / Q000502:physiology*; D011485:Protein Binding; D014760:Viral Fusion Proteins / Q000378:metabolism*; D053586:Virus Internalization
chemical_list: D015707:HN Protein; D014760:Viral Fusion Proteins; D019158:N-Acetylneuraminic Acid