The nucleotide sequence of the mRNA encoding the fusion protein of measles virus (Edmonston strain): A comparison of fusion proteins from several different paramyxoviruses

Richardson, Christopher D.; Hull, D.R.; Greer, Peter A.; Hasel, Karl W.; Berkovich, A.; Englund, George; Bellini, William J.; Rima, B. K.; Lazzarini, Robert A.

doi:10.1016/0042-6822(86)90212-6

Cited by 165 publications

(89 citation statements)

References 45 publications

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“…8 in Richardson et al, 1986), in which analogues of Fzh, H, Flh and Z can be detected around residues 70 to 90, 140 to 180, 200 to 220 and 460 to 490, respectively. Residues 220 to 460 of measles virus F protein are predicted to be poor in a-helix but rich in fl-sheet, alternating with turn or coil conformation.…”

Section: Resultsmentioning

confidence: 98%

Sequence analysis of the gene encoding the fusion glycoprotein of pneumonia virus of mice suggests possible conserved secondary structure elements in paramyxovirus fusion glycoproteins

Chambers

Pringle²,

Easton³

1992

Journal of General Virology

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Section: Resultsmentioning

confidence: 98%

Sequence analysis of the gene encoding the fusion glycoprotein of pneumonia virus of mice suggests possible conserved secondary structure elements in paramyxovirus fusion glycoproteins

Chambers

Pringle²,

Easton³

1992

Journal of General Virology

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“…One-hundred and eight overlapping pentadecamer peptides covering the whole sequence of the F protein of the measles virus (strains Edmonston and Hall& Richardson et al, 1986;Buckland et aL, 1987) were synthesized on a multiple peptide synthesizer (Zinsser SMPS 350; Zinsser Analytics). p-Benzyloxybenzyl alcohol resin (30 mg) loaded with the first Fmoc-amino acid was filled in separate small tubes (Eppendorf cups).…”

Section: Methodsmentioning

confidence: 99%

Heterogeneity of linear B cell epitopes of the measles virus fusion protein reacting with late convalescent sera

Wiesmüller

Spahn²,

Handtmann³

et al. 1992

Journal of General Virology

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B cell epitopes of the measles virus fusion protein were mapped, by reacting sera from late convalescent donors with synthetic overlapping pentadecapeptides, segments covering the whole F protein sequence. When the regions of antibody binding were compared with the predicted secondary structure of the F protein, no detectable pattern became apparent. Exposed sequences as well as sequences hidden in the viral membrane or in the protein core of both the F1 and F2 polypeptides were recognized by the antibodies. The heterogeneity of the binding patterns was not merely dependent on the anti-measles virus titre. The importance of antibodies recognizing linear epitopes of the measles virus fusion protein for the immune protection is presently not known.

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“…Whereas H binds to the MV receptors CD46 (2, 3) and signaling lymphocytic activation molecule (4,5), F carries a hydrophobic fusion peptide that mediates membrane fusion upon receptor binding of H (6). MV H is thought to exist at the viral surface as a tetramer consisting of a dimer of two covalently linked dimers (7), whereas F is considered to trimerize.…”

Section: Measles Virus (Mv)mentioning

confidence: 99%

Measles Virus Envelope Glycoproteins Hetero-oligomerize in the Endoplasmic Reticulum

Plemper

Hammond

Cattaneo

2001

Journal of Biological Chemistry

123

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The endoplasmic reticulum (ER) was investigated as the initial oligomerization site for the envelope glycoproteins H and F of measles virus (MV), a clinically relevant member of the Paramyxoviridae family, and consequences of this interaction for viral replication were studied. Both proteins were tagged at their cytosolic tails with RRR and KKXX motifs, respectively, resulting in their efficient retention in the ER. Cotransfection of the retained constructs with transport competent MV glycoproteins revealed a dominant negative effect on their biological activity indicating intracellular complex formation and thus retention. Pulse-chase analysis and co-immunoprecipitation experiments demonstrated that this effect is based on both homo-and hetero-oligomerization in the ER. Recombinant viruses additionally expressing ERretained F showed an altered cytopathic phenotype accompanied by greatly reduced particle release. Similar mutant viruses additionally expressing ERretained H could not be rescued indicating an even greater negative effect of this protein on virus viability. Our study suggests that both homo-and heterooligomerization of MV glycoproteins occur in the ER and that these events are of significance for early steps of particle assembly.

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The nucleotide sequence of the mRNA encoding the fusion protein of measles virus (Edmonston strain): A comparison of fusion proteins from several different paramyxoviruses

Cited by 165 publications

References 45 publications

Sequence analysis of the gene encoding the fusion glycoprotein of pneumonia virus of mice suggests possible conserved secondary structure elements in paramyxovirus fusion glycoproteins

Sequence analysis of the gene encoding the fusion glycoprotein of pneumonia virus of mice suggests possible conserved secondary structure elements in paramyxovirus fusion glycoproteins

Heterogeneity of linear B cell epitopes of the measles virus fusion protein reacting with late convalescent sera

Measles Virus Envelope Glycoproteins Hetero-oligomerize in the Endoplasmic Reticulum

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