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首页> 外文期刊>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20千柱N-末端片段含有针对嗜血杆菌的保护性表位A和B型

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A conserved 80-kDa minor outer membrane protein, D15, ofHaemophilus 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 glutathioneS-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Haemophilus流感的保守的80kDa次要外膜蛋白，D15，D15，在实验室动物中是一种抵抗 H的保护性抗原。流感型（hia）或b型（hib）感染。为了将D15蛋白内的保护性B细胞表位定位，进一步探讨使用合成肽作为疫苗抗原的可能性，D15蛋白的20kDa n末端片段（截短的D15 [Td15]）表示为一种融合蛋白，含有谷胱甘肽 S -Transferase中的大肠杆菌Coli 。通过使用凝血酶从谷胱甘肽 -Transfers裂解Td15部分，并纯化为均匀性。纯化的可溶性TD15似乎含有免疫肿瘤的保护性表位，因为针对TD15的兔抗血清能够保护来自Hia或Hib菌血症的婴儿大鼠。因此，可溶性TD15的易溶性使其成为比在 E中作为包涵体产生的全长重组D15更好的候选抗原。 Coli 。此外，纯化的Td15片段和跨越成熟D15蛋白的氨基酸残基93-209的Td15衍生肽的混合物能够通过兔抗TD15抗血清抑制对婴儿大鼠赋予婴儿大鼠的HIB的保护，表明保护性D15的表位可能不是一致的。然而，汇集兔免疫血清的给药饲养与同一组肽的血清未能保护婴儿大鼠免受HIB感染的影响。

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