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首页> 美国卫生研究院文献>Infection and Immunity >A 20-Kilodalton N-Terminal Fragment of the D15 Protein Contains a Protective Epitope(s) against Haemophilus influenzae Type a and Type b
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A 20-Kilodalton N-Terminal Fragment of the D15 Protein Contains a Protective Epitope(s) against Haemophilus influenzae Type a and Type b

机译：D15蛋白的20千达尔顿N末端片段包含针对a型和b型流感嗜血杆菌的保护性抗原决定簇。

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摘要

A conserved 80-kDa minor outer membrane protein, D15, of Haemophilus influenzae has been shown to be a protective antigen in laboratory animals against H. influenzae type a (Hia) or type b (Hib) infection. To localize the protective B-cell epitope(s) within the D15 protein and to further explore the possibility of using synthetic peptides as vaccine antigens, a 20-kDa N-terminal fragment of D15 protein (truncated D15 [tD15]) was expressed as a fusion protein with glutathione S-transferase in Escherichia coli. The tD15 moiety was cleaved from glutathione S-transferase by using thrombin and purified to homogeneity. The purified soluble tD15 appeared to contain immunodominant protective epitope(s) against Hia and Hib, since rabbit antisera directed against tD15 were capable of protecting infant rats from Hia or Hib bacteremia. The ease of purification of soluble tD15, therefore, makes it a better candidate antigen than the full-length recombinant D15 which is produced as inclusion bodies in E. coli. Furthermore, both the purified tD15 fragment and a mixture of tD15-derived peptides spanning amino acid residues 93 to 209 of the mature D15 protein were capable of inhibiting the protection against Hib conferred on infant rats by rabbit anti-tD15 antiserum, indicating that the protective epitopes of D15 may not be conformational. However, the administration of pooled rabbit immune sera raised against the same panel of peptides failed to protect infant rats from Hib infection.
机译：在实验动物中，保守的80 kDa流感嗜血小膜外膜蛋白D15被证明是针对甲型流感嗜血杆菌（Hia）或乙型流感嗜血杆菌（Hib）感染的保护性抗原。为了在D15蛋白中定位保护性B细胞表位，并进一步探索使用合成肽作为疫苗抗原的可能性，D15蛋白的20 kDa N端片段（截短的D15 [tD15]）表示为大肠杆菌中带有谷胱甘肽S-转移酶的融合蛋白。通过使用凝血酶从谷胱甘肽S-转移酶上切割tD15部分并纯化至均质。纯化的可溶性tD15似乎含有针对Hia和Hib的免疫保护性抗原决定簇，因为针对tD15的兔抗血清能够保护幼鼠免受Hia或Hib菌血症的侵害。因此，可溶性tD15的纯化容易性使其成为比在大肠杆菌中作为包涵体产生的全长重组D15更好的候选抗原。此外，纯化的tD15片段和跨越tD15的成熟D15蛋白氨基酸残基93至209的肽的混合物均能够抑制兔抗tD15抗血清赋予幼鼠抗Hib的保护作用，表明这种保护性D15的抗原决定簇可能不是构象的。然而，针对同一组肽段的合并兔免疫血清的施用未能保护幼鼠免受Hib感染。

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