Antibodies specific for the high-molecular-weight adhesion proteins of nontypeable Haemophilus influenzae are opsonophagocytic for both homologous and heterologous strains.
Antibodies specific for the high-molecular-weight adhesion proteins of nontypeable Haemophilus influenzae are opsonophagocytic for both homologous and heterologous strains.
复制标题
对不可分型流感嗜血杆菌高分子量粘附蛋白具有特异性的抗体对于同源和异源菌株均具有调理吞噬作用。
DOI：
10.1128/cvi.00221-06
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
Barenkamp,StephenJ
中科院分区：
文献类型：
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作者：
Winter,LindaE;Barenkamp,StephenJ
不可分型流感嗜血杆菌 (NTHI) 的 HMW1/HMW2 样粘附蛋白由 75% 的 NTHI 菌株表达。针对这些蛋白质的抗体在体外具有调理吞噬作用，并且在动物感染模型中具有保护作用。本研究的目的是确定高滴度抗 HMW1/HMW2 免疫血清对同源和异源 NTHI 菌株的调理吞噬活性。使用来自 5 个原型 NTHI 品系的纯化 HMW1/HMW2 样蛋白对龙猫进行免疫。在使用人类早幼粒细胞系 HL-60 作为吞噬细胞来源的测定中监测血清调理吞噬活性。免疫前血清没有表现出对任何菌株的调理吞噬作用。相比之下，免疫血清显示出以 1:320 至 1:640 滴度杀死 5 种同源 NTHI 菌株。免疫血清还证明能杀死八种异源 NTHI 菌株，这些菌株以 0 至 1:640 的滴度表达 HMW1/HMW2 样蛋白。异源菌株的杀灭有时表现出前带现象。没有一种免疫血清能够杀死不表达 HMW1/HMW2 样蛋白的 NTHI 菌株。在大多数情况下，用从同源或异源 NTHI 菌株纯化的 HMW1/HMW2 样蛋白吸附免疫血清，消除了同源菌株的调理吞噬杀伤作用。这些数据表明，用 HMW1/HMW2 样蛋白免疫后产生的抗体对同源和异源 NTHI 均具有调理吞噬作用，并强烈表明功能活性抗体识别的共同表位存在于不相关 NTHI 菌株的 HMW1/HMW2 样蛋白上。这些结果支持继续研究 HMW1/HMW2 样蛋白作为预防 NTHI 疾病的潜在候选疫苗。
The HMW1/HMW2-like adhesion proteins of nontypeableHaemophilus influenzae(NTHI) are expressed by 75% of NTHI strains. Antibodies directed against these proteins are opsonophagocytic in vitro and are protective in an animal model of infection. The objective of the present study was to determine the opsonophagocytic activity of high-titer anti-HMW1/HMW2 immune sera against both homologous and heterologous NTHI strains. Chinchillas were immunized with purified HMW1/HMW2-like proteins from five prototype NTHI strains. Serum opsonophagocytic activity was monitored in an assay that uses a human promyelocytic cell line, HL-60, as the source of phagocytic cells. Preimmune sera did not demonstrate opsonophagocytic killing of any strains. In contrast, the immune sera demonstrated killing of the five homologous NTHI strains at titers ranging from 1:320 to 1:640. The immune sera also demonstrated killing of eight heterologous NTHI strains that express HMW1/HMW2-like proteins at titers ranging from 0 to 1:640. Killing of heterologous strains sometimes demonstrated a prozone phenomenon. None of the immune sera killed NTHI strains that did not express HMW1/HMW2-like proteins. Adsorption of immune sera with HMW1/HMW2-like proteins purified from either homologous or heterologous NTHI strains eliminated opsonophagocytic killing of homologous strains in most cases. These data demonstrate that antibodies produced following immunization with the HMW1/HMW2-like proteins are opsonophagocytic for both homologous and heterologous NTHI and strongly suggest that common epitopes recognized by functionally active antibodies exist on the HMW1/HMW2-like proteins of unrelated NTHI strains. The results argue for the continued investigation of the HMW1/HMW2-like proteins as potential vaccine candidates for the prevention of NTHI disease.