University of Massachusetts Medical School Faculty Publications

UMMS Affiliation

Department of Microbiology and Physiological Systems

Date

8-2013

Document Type

Article

Medical Subject Headings

Amino Acid Substitution; HN Protein; Mutant Proteins; Newcastle disease virus; Protein Binding; *Protein Multimerization; Viral Fusion Proteins; *Virus Internalization

Disciplines

Virology

Abstract

Newcastle disease virus (NDV)-induced membrane fusion requires formation of a complex between the hemagglutinin-neuraminidase (HN) and fusion (F) proteins. Substitutions for NDV HN stalk residues A89, L90, and L94 block fusion by modulating formation of the HN-F complex. Here, we demonstrate that a nearby L97A substitution, though previously shown to block fusion, allows efficient HN-F complex formation and likely acts by preventing changes in the HN stalk required for triggering of the bound F protein.

Comments

Citation: Mirza AM, Iorio RM. 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. J Virol. 2013 Aug;87(15):8813-5. doi: 10.1128/JVI.01066-13. Link to article on publisher's site

Publisher PDF posted as allowed by the publisher's author rights policy at http://journals.asm.org/site/misc/ASM_Author_Statement.xhtml.

Related Resources

Link to Article in PubMed

PubMed ID

23740987

Included in

Virology Commons

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