Angulo A, Viñuela E, Alcamí A
Centro de Biología Molecular, Facultad de Ciencias, Universidad Autónoma, Madrid, Spain.
J Virol. 1992 Jun;66(6):3869-72. doi: 10.1128/JVI.66.6.3869-3872.1992.
Comparison of the amino acid sequence of the African swine fever virus attachment protein p12 from different field virus isolates, deduced from the nucleotide sequence of the gene, revealed a high degree of conservation. No mutations were found after adaptation to Vero cells, and a polypeptide with similar characteristics was present in an IBRS2-adapted virus. The sequence of the 5' flanking region was conserved among the isolates, whereas sequences downstream of the gene were highly variable in length and contained direct repeats in tandem that may account for the deletions found in different isolates. Protein p12 was synthesized in swine macrophages infected with all of the viruses tested.
通过对非洲猪瘟病毒附着蛋白p12基因核苷酸序列推导得出的不同野外病毒分离株的氨基酸序列进行比较,发现其具有高度保守性。适应Vero细胞后未发现突变,且在适应IBRS2的病毒中存在具有相似特征的多肽。分离株中5'侧翼区域的序列是保守的,而该基因下游的序列长度高度可变,并且包含串联直接重复序列,这可能解释了不同分离株中发现的缺失情况。在感染所有测试病毒的猪巨噬细胞中均合成了蛋白p12。