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从流感嗜血杆菌中通过受体亲和纯化脂质结合黏附素

Receptor affinity purification of a lipid-binding adhesin from Haemophilus influenzae.

作者信息

Busse J, Hartmann E, Lingwood C A

机构信息

Department of Microbiology, Research Institute, Hospital for Sick Children, Toronto, Canada.

出版信息

J Infect Dis. 1997 Jan;175(1):77-83. doi: 10.1093/infdis/175.1.77.

DOI:10.1093/infdis/175.1.77
PMID:8985199
Abstract

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.

摘要

13株流感嗜血杆菌临床菌株,包括b型、d型和不可分型,在体外能特异性识别磷脂酰乙醇胺(PE)、神经节四糖神经酰胺、神经节三糖神经酰胺(Gg3)、硫酸化半乳糖基神经酰胺,以及程度较轻的硫酸化半乳糖基甘油。使用PE亲和基质从b型和不可分型流感嗜血杆菌中纯化出一种约46 kDa的黏附素。这种黏附素在体外是流感嗜血杆菌Gg3和PE结合的有效抑制剂,针对该蛋白的多克隆抗体在体外可阻止流感嗜血杆菌Gg3和PE与培养的HEp-2上皮细胞的附着。

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Enteropathogenic Escherichia coli virulence factor bundle-forming pilus has a binding specificity for phosphatidylethanolamine.
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Infect Immun. 2001 Nov;69(11):6573-9. doi: 10.1128/IAI.69.11.6573-6579.2001.
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Heat-inducible surface stress protein (Hsp70) mediates sulfatide recognition of the respiratory pathogen Haemophilus influenzae.热诱导表面应激蛋白(Hsp70)介导呼吸道病原体流感嗜血杆菌对硫脂的识别。
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