UMMS Affiliation

Department of Molecular Genetics and Microbiology

Publication Date

5-9-2000

Document Type

Article

Subjects

Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; COS Cells; HN Protein; Leucine; Membrane Fusion; Molecular Sequence Data; Mutagenesis; Newcastle disease virus; Protein Processing, Post-Translational; Viral Fusion Proteins

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The role of a leucine heptad repeat motif between amino acids 268 and 289 in the structure and function of the Newcastle disease virus (NDV) F protein was explored by introducing single point mutations into the F gene cDNA. The mutations affected either folding of the protein or the fusion activity of the protein. Two mutations, L275A and L282A, likely interfered with folding of the molecule since these proteins were not proteolytically cleaved, were minimally expressed at the cell surface, and formed aggregates. L268A mutant protein was cleaved and expressed at the cell surface although the protein migrated slightly slower than wild type on polyacrylamide gels, suggesting an alteration in conformation or processing. L268A protein was fusion inactive in the presence or absence of HN protein expression. Mutant L289A protein was expressed at the cell surface and proteolytically cleaved at better than wild-type levels. Most importantly, this protein mediated syncytium formation in the absence of HN protein expression although HN protein enhanced fusion activity. These results show that a single amino acid change in the F(1) portion of the NDV F protein can alter the stringent requirement for HN protein expression in syncytium formation.

Rights and Permissions

Citation: J Virol. 2000 Jun;74(11):5101-7.

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Journal of virology

PubMed ID

10799584

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