White P A, Nair S P, Kim M J, Wilson M, Henderson B
School of Biological Sciences, Macquarie University, Sydney, New South Wales, Australia.
Infect Immun. 1998 Jan;66(1):369-72. doi: 10.1128/IAI.66.1.369-372.1998.
The major outer membrane protein (OMP) of Actinobacillus actinomycetemcomitans is an OmpA homolog that demonstrates electrophoretic heat modifiability. The gene encoding this protein was isolated from a genomic library of A. actinomycetemcomitans NCTC 9710 by immunoscreening with serum from a patient with localized juvenile periodontitis. Expression of the cloned gene in Escherichia coli and subsequent Western blot analysis revealed a protein with an approximate molecular mass of 34 kDa. The amino acid sequence predicted from the cloned gene demonstrated that the mature protein had a molecular mass of 34,911 Da and significant identity to members of the OmpA family of proteins. We have named the major OMP of A. actinomycetemcomitans Omp34, and its corresponding gene has been named omp34.
伴放线放线杆菌的主要外膜蛋白（OMP）是一种OmpA同源物，具有电泳热可修饰性。通过用一名局限性青少年牙周炎患者的血清进行免疫筛选，从伴放线放线杆菌NCTC 9710的基因组文库中分离出编码该蛋白的基因。该克隆基因在大肠杆菌中的表达及随后的蛋白质印迹分析显示出一种分子量约为34 kDa的蛋白质。从克隆基因预测的氨基酸序列表明，成熟蛋白的分子量为34,911 Da，与OmpA蛋白家族成员具有显著同源性。我们将伴放线放线杆菌的主要OMP命名为Omp34，其相应基因命名为omp34。
