结构糖蛋白 E2 假定融合肽中特定氨基酸取代对古典猪瘟病毒复制的影响。
Effect of specific amino acid substitutions in the putative fusion peptide of structural glycoprotein E2 on Classical Swine Fever Virus replication.
机构信息
Plum Island Animal Disease Center, ARS, USDA, USA.
Biophysics Unit (CSIC-UPV/EHU), Department of Biochemistry and Molecular Biology, University of the Basque Country (UPV/EHU), P.O. Box 644, 48080 Bilbao, Spain.
出版信息
Virology. 2014 May;456-457:121-30. doi: 10.1016/j.virol.2014.03.005. Epub 2014 Apr 4.
E2, along with E(rns) and E1, is an envelope glycoprotein of Classical Swine Fever Virus (CSFV). E2 is involved in several virus functions: cell attachment, host range susceptibility and virulence in natural hosts. Here we evaluate the role of a specific E2 region, (818)CPIGWTGVIEC(828), containing a putative fusion peptide (FP) sequence. Reverse genetics utilizing a full-length infectious clone of the highly virulent CSFV strain Brescia (BICv) was used to evaluate how individual amino acid substitutions within this region of E2 may affect replication of BICv. A synthetic peptide representing the complete E2 FP amino acid sequence adopted a β-type extended conformation in membrane mimetics, penetrated into model membranes, and perturbed lipid bilayer integrity in vitro. Similar peptides harboring amino acid substitutions adopted comparable conformations but exhibited different membrane activities. Therefore, a preliminary characterization of the putative FP (818)CPIGWTGVIEC(828) indicates a membrane fusion activity and a critical role in virus replication.
E2 与 E(rns)和 E1 一起，是经典猪瘟病毒 (CSFV) 的一种包膜糖蛋白。E2 参与多种病毒功能：细胞附着、宿主范围易感性和天然宿主中的毒力。在这里，我们评估了一个特定的 E2 区域（818）CPIGWTGVIEC（828）的作用，该区域包含一个假定的融合肽（FP）序列。利用高度致病毒力的 CSFV 菌株 Brescia（BICv）的全长感染性克隆进行反向遗传学，评估了 E2 这一区域内的单个氨基酸取代如何影响 BICv 的复制。代表完整 E2 FP 氨基酸序列的合成肽在膜类似物中采用β型扩展构象，穿透模型膜，并在体外破坏脂质双层完整性。携带氨基酸取代的类似肽采用类似的构象，但表现出不同的膜活性。因此，对假定的 FP（818）CPIGWTGVIEC（828）的初步表征表明其具有膜融合活性和在病毒复制中的关键作用。
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