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Measles Virus Fusion: Role of the Cysteine-rich Region of the Fusion Glycoprotein

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Journal J Virol
Date 1994 Nov 1
PMID 7933140
Citations 25
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Abstract

Measles virus (MV) fusion requires the participation of both the fusion (F) and hemagglutinin (H) glycoproteins. The canine distemper virus fusion protein (CDVF) cannot substitute for the measles virus fusion protein (MVF) in this process. Introduction of restriction enzyme sites into the cDNAs of CDVF and MVF by site-directed mutagenesis facilitated the production of chimeric F proteins which were tested for their capacity to give fusion when coexpressed with MVH. Fusion resulted when the amino-terminal half of the MVF cysteine-rich region was transferred to CDVF.

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References
1.
Buckland R, Gerald C, Barker R, Wild T . Fusion glycoprotein of measles virus: nucleotide sequence of the gene and comparison with other paramyxoviruses. J Gen Virol. 1987; 68 ( Pt 6):1695-703. DOI: 10.1099/0022-1317-68-6-1695. View

2.
Iwata S, Schmidt A, Titani K, Suzuki M, Kido H, Gotoh B . Assignment of disulfide bridges in the fusion glycoprotein of Sendai virus. J Virol. 1994; 68(5):3200-6. PMC: 236811. DOI: 10.1128/JVI.68.5.3200-3206.1994. View

3.
Kunkel T, Roberts J, Zakour R . Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 1987; 154:367-82. DOI: 10.1016/0076-6879(87)54085-x. View

4.
Portner A, Scroggs R, Naeve C . The fusion glycoprotein of Sendai virus: sequence analysis of an epitope involved in fusion and virus neutralization. Virology. 1987; 157(2):556-9. DOI: 10.1016/0042-6822(87)90301-1. View

5.
Barrett T, Clarke D, Evans S, Rima B . The nucleotide sequence of the gene encoding the F protein of canine distemper virus: a comparison of the deduced amino acid sequence with other paramyxoviruses. Virus Res. 1987; 8(4):373-86. DOI: 10.1016/0168-1702(87)90009-8. View