Martin D, Munson R, Grass S, Chong P, Hamel J, Zobrist G, Klein M, Brodeur B R
National Laboratory for Immunology, Laboratory Centre for Disease Control, Ottawa, Canada.
Infect Immun. 1991 Apr;59(4):1457-64. doi: 10.1128/iai.59.4.1457-1464.1991.
The P2 protein of Haemophilus influenzae type b has a porin activity and is the most abundant protein in the outer membrane. We have employed fusion protein constructs and synthetic peptides along with monoclonal antibodies to map B-cell epitopes in this protein. A linear, surface-exposed epitope was identified between residues 158 and 174. A second surface-exposed epitope was identified near the carboxy-terminal end of the protein (residues 319 to 341). Two additional B-cell epitopes were identified. One was localized between residues 28 and 55, whereas the other was located between residues 148 and 174. These epitopes were not present on the surface of intact H. influenzae cells. Thus, four distinct immunogenic and antigenic regions on the P2 protein have been identified.
b型流感嗜血杆菌的P2蛋白具有孔蛋白活性,是外膜中含量最丰富的蛋白质。我们利用融合蛋白构建体、合成肽以及单克隆抗体来绘制该蛋白中的B细胞表位。在第158至174位氨基酸残基之间鉴定出一个线性的、暴露于表面的表位。在该蛋白的羧基末端附近(第319至341位氨基酸残基)鉴定出第二个暴露于表面的表位。还鉴定出另外两个B细胞表位。一个位于第28至55位氨基酸残基之间,而另一个位于第148至174位氨基酸残基之间。这些表位不存在于完整的流感嗜血杆菌细胞表面。因此,已在P2蛋白上鉴定出四个不同的免疫原性和抗原性区域。