Receptor affinity purification of a lipid-binding adhesin from Haemophilus influenzae.
Receptor affinity purification of a lipid-binding adhesin from Haemophilus influenzae.
复制标题
流感嗜血杆菌脂质结合粘附素的受体亲和纯化。
DOI：
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发表时间：
1997
影响因子：
6.4
通讯作者：
C. Lingwood
中科院分区：
文献类型：
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作者：
J. Busse;E. Hartmann;C. Lingwood
13种流感嗜血杆菌临床菌株，包括b型、d型和无法分型的菌株，在体外特异性识别磷脂酰乙醇胺（PE）、神经节四糖基神经酰胺、神经节三糖基神经酰胺（Gg3）、磺胺氧半乳糖神经酰胺，以及在较小程度上磺胺氧半乳糖甘油。用PE亲和基质从b型和不可分型流感嗜血杆菌中纯化出约46 kDa的粘附素。在体外实验中，该粘附素是流感嗜血杆菌Gg3和PE结合的有效抑制剂，针对该蛋白的多克隆抗体可以阻止流感嗜血杆菌Gg3和PE的结合，并在体外培养HEp-2上皮细胞。
Thirteen clinical strains of Haemophilus influenzae, including types b, d, and untypeable, in vitro specifically recognize phosphatidylethanolamine (PE), gangliotetraosylceramide, gangliotriosylceramide (Gg3), sulfatoxygalactosylceramide, and to a lesser extent sulfatoxygalactosylglycerol. A PE affinity matrix was used to purify an adhesin of approximately 46 kDa from both type b and untypeable H. influenzae. This adhesin was a potent inhibitor of H. influenzae Gg3 and PE binding in vitro, and polyclonal antibodies specific for this protein prevented the attachment of H. influenzae Gg3 and PE and cultured HEp-2 epithelial cells in vitro.