Isolation and characterization of the measles virus F1 polypeptide: comparison with other paramyxovirus fusion proteins.
Isolation and characterization of the measles virus F1 polypeptide: comparison with other paramyxovirus fusion proteins.
复制标题
麻疹病毒 F1 多肽的分离和表征：与其他副粘病毒融合蛋白的比较。
DOI：
10.1016/0168-1702(85)90358-2
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发表时间：
1985
期刊：
影响因子：
3.7
通讯作者：
E. Norrby
中科院分区：
文献类型：
--
作者：
T. Varsanyi;H. Jörnvall;E. Norrby
Measles virus fusion (F) protein has been isolated by immunoadsorption to a complex of monoclonal antibodies bound to protein A-Sepharose. The 41-kDa F1component of the fusion protein was obtained pure in high yield by preparative SDS-polyacrylamide gel electrophoresis. The amino acid composition of the F1chain was determined and the N-terminal sequence was analyzed for 40 residues. The structure determined is largely hydrophobic, with 24 residues of Val, Ile, Leu, Met, Phe, or Ala. Comparison with previously published data on the F1polypeptide of Sendai virus showed considerable similarity in amino acid composition. Extensive N-terminal sequence homologies with F1polypeptides of different paramyxoviruses are also noticed, including a nine-residue segment strictly conserved among four F1polypeptides studied, as well as a weaker but distinct and Glyrich sequence homology with the influenza A and B virus HA2polypeptides. The evolutionary conservation of the N-terminal region at the site of cleavage of surface glycoproteins of the two families of myxoviruses highlights its specialized function in membrane fusion.
使用病毒基因的 cDNA 克隆和融合蛋白的生物学重要区域的序列分析仙台病毒 mRNA。
DOI：
10.1073/pnas.81.24.7732
发表时间：
1984
影响因子：
11.1
作者：
Hsu,M;Choppin,PW
通讯作者：
Choppin,PW
影响因子：
3.7
作者：
MERZ, DC;SCHEID, A;CHOPPIN, PW
通讯作者：
CHOPPIN, PW