Sequence Elements of the Fusion Peptide of Human Respiratory Syncytial Virus Fusion Protein Required for Activity.
From: Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, 28220 Madrid, Spain.
The Journal of general virology
- Publish Date: Jun 2006
- ISSN: 0022-1317
- Volume: 87
- Issue: Pt 6
- Pages: 1649-58
- Medium: Print
- Language: English
- Citation (JAMA): Martín Diana, Calder Lesley J, García-Barreno Blanca, et al. Sequence Elements of the Fusion Peptide of Human Respiratory Syncytial Virus Fusion Protein Required for Activity.. J. Gen. Virol. Jun 2006;87:1649-58
Abstract
We have reported previously the expression and purification of an anchorless form of the human respiratory syncytial virus (HRSV) F protein (F(TM-)) representing the ectodomain of the full-length F. F(TM-) molecules are seen as unaggregated cones by electron microscopy but completion of proteolytic cleavage of the F0 monomers in the F(TM-) trimer leads to a change in shape from cones to lollipops that aggregate into rosettes. This aggregation apparently occurs by interaction of the fusion peptides of F(TM-) molecules that are exposed after cleavage. Since exposure of the fusion peptide is a key event in the process of membrane fusion, changes associated with F(TM-) cleavage may reflect those occurring in full-length F during membrane fusion. Deletions or substitutions that changed either the length, charge or hydrophobicity of the fusion peptide inhibited aggregation of F(TM-), and these mutants remained as unaggregated cones after cleavage. In contrast, more conservative changes did not inhibit the change of shape and aggregation of F(TM-). When the same changes were introduced in the fusion peptide of full-length F, only the mutations that inhibited aggregation of F(TM-) prevented membrane fusion. Thus, the conformational changes that follow completion of cleavage of the F(TM-) protein require a functional fusion peptide. These sequence constraints may restrict accumulation of sequence changes in the fusion peptide of HRSV F when compared with other hydrophobic regions of the molecule.
Mesh Headings (Keywords): Amino Acid Sequence, Amino Acid Substitution, Animals, Cell Line, Cricetinae, Giant Cells, Humans, Membrane Fusion, Mutagenesis, Site-Directed, Peptides, Respiratory Syncytial Virus, Human, Sequence Deletion, Viral Fusion Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 16690930
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