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首页> 外文期刊>Infection and immunity >The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species.
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The hbpA gene of Haemophilus influenzae type b encodes a heme-binding lipoprotein conserved among heme-dependent Haemophilus species.

机译：b型流感嗜血杆菌的hbpA基因编码在依赖于血红素的嗜血杆菌属物种中保守的血红素结合脂蛋白。

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摘要

A membrane-associated lipoprotein of Haemophilus influenzae type b has previously been shown to bind heme in vitro and to promote binding of this compound by Escherichia coli recombinants expressing this protein. The H. influenzae type b heme-binding protein A (HbpA) was found to be highly conserved with respect to both antigenicity and apparent molecular weight among heme-requiring Haemophilus species pathogenic for humans. To further the characterization of the structure and function of HbpA, the complete nucleotide sequence of its gene, hbpA, was determined. Analysis of the nucleotide sequence revealed a single large open reading frame of 1,638 bp encoding a protein of 546 amino acid residues, with a molecular weight of 60,695. The sequence of the amino-terminal end of this protein contained a potential site for lipid acylation and for cleavage by signal peptidase II, consistent with earlier biochemical evidence which indicated that HbpA is a lipoprotein. A search of GenBank for proteins with amino acid sequence similarity to HbpA revealed that the periplasmic dipeptide transport protein of E. coli, DppA, has 53% sequence identity to HbpA.
机译：先前已显示，b型流感嗜血杆菌的膜相关脂蛋白在体外结合血红素，并通过表达该蛋白的大肠杆菌重组体促进该化合物的结合。发现在人类致病的需要血红素的嗜血杆菌属物种中，流感嗜血杆菌b型血红素结合蛋白A（HbpA）在抗原性和表观分子量方面都高度保守。为了进一步表征HbpA的结构和功能，确定了其基因hbpA的完整核苷酸序列。核苷酸序列分析揭示了一个大的开放阅读框，长1,638 bp，编码一个546个氨基酸残基的蛋白质，分子量为60,695。该蛋白氨基末端的序列包含脂质酰化和信号肽酶II切割的潜在位点，这与早期的生化证据表明HbpA是一种脂蛋白一致。在GenBank中搜索与HbpA氨基酸序列相似的蛋白质后发现，大肠杆菌的周质二肽转运蛋白DppA与HbpA具有53％的序列同一性。

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