摘要
利用FASTP等微型计算机程序将痘苗病毒血凝素(VVHA)与NBRF蛋白质序列库进行了比较分析,发现VVHA分子的不同区段分别与免疫球蛋白超家族(Ig Superfamily)及花生凝集素(PNA)有相似的一级结构。对VVHA与免疫球蛋白间相似区一级结构细节的分析指出,VVHA分子N端20～120的区段具备了Ig超家族在一级结构上的所有特点,两者不但在总体上很相似,而且在半胱氨酸附近的区域集中了最为保守的残基,以Kyte-Doolittle法比较相似区的疏水性,并以Chou-Fasman法预测相应的二级结构,结果都支持两者分子结构的相似性,因此,我们认为成熟VVHA分子N端约100个残基很可能形成一个与Ig可变区(V区)相似的结构域,其功能很可能与病毒的释放及其在细胞间的传播有关,VVHA的245～298位与PNA的97～150位在一级结构上相似,预测的二级结构也比较相似,其功能有待进一步研究。
Using the FASTP and other microcomputer programs, we have found significant similarity between the first 120 residues of vaccinia virus hema-gglutinin (VVHA) and immunoglobulin (Ig) V domain. In addition to an overall sequence similarity, consensus residues were found clustered around the two cysteines. The difference in the primary structure between WHA and Ig V region is no more than that between the well-known members of the Ig superfamily. The Kyte-Doolittle hydrophobicity plot and the results of the Chou-Fasman secondary structure prediction have led us to consider that mature WHA would probably have an Ig-like domain with the size of about 100 residues at its N-terminal. we have also found local similarities between WHA 245-298 region and peanut agglutinin 97-150 region. The probable biological significance of the above similarities is discussed.
出处
《病毒学报》
CAS
CSCD
北大核心
1989年第2期99-105,共7页
Chinese Journal of Virology
关键词
VVHA
免疫球蛋白
花生凝集素
Vaccinia virus hemagglutinin Immunoglobulin superfamily Peanut agglutinin Protein structure
