Paramyxovirus fusion proteins

Negative-strand RNA viruses, 158-163 ebola virus matrix protein/ glycoprotein, 162-163 hemagglutinin-neuraminidase and, 162 influenza A and, 158-163 Ml and, 161 Ms and, 161-162 neuraminidase and, 161 paramyxovirus fusion protein and, 162 Neuraminidase, negative-strand RNA viruses and, 161... 

Paramyxovirus fusion protein, negative-strand RNA viruses and, 162 Pariacoto virus, 223 Particle reconstruction images, 198 Parvoviridae family, 238-240 Desovirinae subfamily of 239 Parvovirinae subfamily of 239 of single-stranded DNA (ssDNA) viruses, 242... 

Many enveloped viruses share a common mechanism of fusion, mediated by a virus-encoded glycoprotein that contains heptad repeats in its extraceUnlar domain. Dnring the fnsion process, these domains rearrange to form highly structured and thermodynamically stable coiled-coils. Viruses encoding fusion proteins that have these domains inclnde members of the paramyxovirus family (e.g., respiratory syncytial virus, metapneumovirus, and measles virus), ebola virus, influenza, and members of the retroviridae (e.g., human T cell lenkemia virus type-1 and human immunodeficiency virus type-1, HlV-1). Peptide inhibitors of fusion that disrupt the... 

Paramyxoviruses cause respiratory tract diseases such as croup and pneumonia, as well as measles and mumps. The envelope proteins of these viruses share some features in common with influenza and retroviruses. These similarities include a precursor protein that is cleaved into two fragments, the second of which, called El, bears a fusion peptide at its amino terminus. In addition, peptides from the paramyxovirus FI proteins assemble into stable helical bundles resembling HIV gp41 and influenza HA2 (Baker et al, 1999 Lawless-Delmedico et al, 2000 Zhao et al, 2000). The paramyxovirus F protein differs from influenza HA and retroviral TM... 

Inhibitors of Protein-Protein Interactions in Paramyxovirus Fusion A Focus on Respiratory Syncytial Virus... 

The authors of the NDV-F structure propose that they have crystallized a mixture of the native and sprung forms of the spike protein, and that these two versions are similar enough structurally to pack into the same crystal lattice (Chen et al., 2001a). In light of the enormous structural changes that are observed on exposure of influenza HA to low pH, the possibility that minimal conformational changes occur in paramyxoviruses is remarkable. Furthermore, the long central helix of NDV-F is proposed to point in the opposite direction from that of influenza HA, such that extension of the central coiled coil sends the fusion peptides in the direction of the virus membrane (Fig. 12). 

Scheid, A., and Choppin, P. W., 1974, Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology 57 475. 

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