FILAMENTOUS HEMAGGLUTININ OF BORDETELLA-PERTUSSIS - NUCLEOTIDE SEQUENCE AND CRUCIAL ROLE IN ADHERENCE
FILAMENTOUS HEMAGGLUTININ OF BORDETELLA-PERTUSSIS - NUCLEOTIDE SEQUENCE AND CRUCIAL ROLE IN ADHERENCE
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DOI：
10.1073/pnas.86.8.2637
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发表时间：
1989-04-01
影响因子：
11.1
通讯作者：
FALKOW, S
中科院分区：
文献类型：
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作者：
RELMAN, DA;DOMENIGHINI, M;FALKOW, S
丝状血凝素是百日咳杆菌的表面相关黏附蛋白，是一些新型无细胞百日咳疫苗的组成部分。包含丝状血凝素结构基因fhaB的开放阅读框的核苷酸序列表明，蛋白水解性加工是产生成熟的220 kDa丝状血凝素产物所必需的。在丝状血凝素中发现了一种Arg-Gly-Asp(RGD)三肽，可能与其黏附特性有关。FhaB中包含RGD区域的内部框内缺失导致百日咳杆菌与纤毛真核细胞的结合丧失，证实了该蛋白在宿主细胞结合和感染中的潜在作用。
Filamentous hemagglutinin is a surface-associated adherence protein of Bordetella pertussis, which is a component of some new acellular pertussis vaccines. The nucleotide sequence of an open reading frame that encompasses the filamentous hemagglutinin structural gene, fhaB, suggests that proteolytic processing is necessary to generate the mature 220-kDa filamentous hemagglutinin product. An Arg-Gly-Asp (RGD) tripeptide is found within filamentous hemagglutinin that may be involved in its adherence properties. An internal in-frame deletion in fhaB, encompassing the RGD region, causes loss of B. pertussis-binding to ciliated eukaryotic cells, confirming a potential role for this protein in host-cell binding and infection.