A LEUCINE ZIPPER STRUCTURE PRESENT IN THE MEASLES-VIRUS FUSION PROTEIN IS NOT REQUIRED FOR ITS TETRAMERIZATION BUT IS ESSENTIAL FOR FUSION
A LEUCINE ZIPPER STRUCTURE PRESENT IN THE MEASLES-VIRUS FUSION PROTEIN IS NOT REQUIRED FOR ITS TETRAMERIZATION BUT IS ESSENTIAL FOR FUSION
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DOI：
10.1099/0022-1317-73-7-1703
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发表时间：
1992-07-01
影响因子：
3.8
通讯作者：
WILD, F
中科院分区：
文献类型：
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作者：
BUCKLAND, R;MALVOISIN, E;WILD, F
研究了麻疹病毒融合蛋白(F)中亮氨酸拉链基序的生物学作用。这个基序存在于所有副粘病毒F蛋白、所有冠状病毒刺突蛋白和许多逆转录病毒包膜蛋白中。通过类比其在某些转录因子中的作用，有人认为该基序可能是这些病毒膜蛋白齐聚的原因。在本研究中，利用定点突变技术对基序中的一个、两个或四个七元亮氨酸进行了替换。我们发现，当存在于基序中的所有四个七肽亮氨酸都发生突变时，融合被阻止，而细胞运输和F蛋白的寡聚体状态不受影响。
The biological role of a leucine zipper motif present in the measles virus fusion (F) protein has been investigated. This motif is present in all paramyxovirus F proteins, all coronavirus spike proteins and many if not all retrovirus envelope proteins. By analogy to its role in certain transcription factors, it has been suggested that the motif may be responsible for the oligomerization of these viral membrane proteins. In this study, one, two or four heptadic leucines in the motif were substituted using site-directed mutagenesis. We found that fusion is prevented when all four heptadic leucines present in the motif are mutated whereas cellular transport and the oligomeric state of the F protein are unaffected.