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编码双组分脑膜炎球菌乳铁蛋白受体的lbpBA的鉴定与分子分析。

Identification and molecular analysis of lbpBA, which encodes the two-component meningococcal lactoferrin receptor.

作者信息

Lewis L A, Rohde K, Gipson M, Behrens B, Gray E, Toth S I, Roe B A, Dyer D W

机构信息

Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73103, USA.

出版信息

Infect Immun. 1998 Jun;66(6):3017-23. doi: 10.1128/IAI.66.6.3017-3023.1998.

DOI:10.1128/IAI.66.6.3017-3023.1998
PMID:9596785
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC108307/
Abstract

We identified lbpB, encoding the lipoprotein component of the meningococcal lactoferrin receptor. An LbpB mutant was unable to acquire Fe from lactoferrin and exhibits decreased surface binding to lactoferrin. Primer extension and reverse transcription-PCR analysis indicate that lbpB and lbpA are cotranscribed on a polycistronic Fe-repressible mRNA.

摘要

我们鉴定出了lbpB，它编码脑膜炎球菌乳铁蛋白受体的脂蛋白成分。一个LbpB突变体无法从乳铁蛋白获取铁，并且表现出与乳铁蛋白的表面结合能力下降。引物延伸和逆转录-聚合酶链反应分析表明，lbpB和lbpA在一个多顺反子铁可阻遏信使核糖核酸上共同转录。

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Biochemical analysis of lactoferrin receptors in the Neisseriaceae: identification of a second bacterial lactoferrin receptor protein.奈瑟菌科中乳铁蛋白受体的生化分析：第二种细菌乳铁蛋白受体蛋白的鉴定
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Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins.淋球菌转铁蛋白受体的结合及表面暴露特性取决于两种转铁蛋白结合蛋白。
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