Glycoprotein interactions in paramyxovirus fusion
نویسندگان
چکیده
منابع مشابه
Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: roles of conserved residues in cell fusion.
The role of residues in the conserved hydrophobic N-terminal fusion peptide of the paramyxovirus fusion (F) protein in causing cell-cell fusion was examined. Mutations were introduced into the cDNA encoding the simian virus 5 (SV5) F protein, the altered F proteins were expressed by using an eukaryotic vector, and their ability to mediate syncytium formation was determined. The mutant F protein...
متن کاملStructure of the primed paramyxovirus fusion protein.
V iruses with lipid envelopes must fuse their membranes with those of host cells to transfer their genomes and initiate infection. Depending on the virus, the membrane fusion process can occur at the plasma membrane, or at intracellular membranes following the internalization of virus particles. Not surprisingly, the viral proteins responsible for membrane fusion are highly diverse, as are the ...
متن کاملMutations in multiple domains activate paramyxovirus F protein-induced fusion.
SER virus, a paramyxovirus that is closely related to simian virus 5 (SV5), is unusual in that it fails to induce syncytium formation. The SER virus F protein has an unusually long cytoplasmic tail (CT), and it was previously observed that truncations or specific mutations of this domain result in enhanced syncytium formation. In addition to the long CT, the SER F protein has nine amino acid di...
متن کاملFusion protein of the paramyxovirus simian virus 5: nucleotide sequence of mRNA predicts a highly hydrophobic glycoprotein.
The nucleotide sequence of the mRNA coding for the fusion glycoprotein (F) of the paramyxovirus, simian virus 5, has been obtained. There is a single large open reading frame on the mRNA that encodes a protein of 529 amino acids with a molecular weight of 56,531. The proteolytic cleavage/activation site of F, to yield F2 and F1, contains five arginine residues. Six potential glycosylation sites...
متن کاملSequence analysis of the gene encoding the fusion glycoprotein of pneumonia virus of mice suggests possible conserved secondary structure elements in paramyxovirus fusion glycoproteins.
The gene encoding the fusion (F) glycoprotein of pneumonia virus of mice consists of 1657 bases and contains an open reading frame encoding 537 amino acids which is more similar to the F proteins of pneumoviruses than to those of other paramyxoviruses. Computer-assisted sequence analyses can be combined with data on the antigenicity of various F proteins to suggest a possible arrangement of sec...
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ژورنال
عنوان ژورنال: Future Virology
سال: 2009
ISSN: 1746-0794,1746-0808
DOI: 10.2217/fvl.09.17