The N-terminal half part of the oral streptococcal antigen I/IIf contains two distinct functional domains.
The N-terminal half part of the oral streptococcal antigen I/IIf contains two distinct functional domains.
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口腔链球菌抗原 I/IIf 的 N 端半部分包含两个不同的功能域。
DOI：
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发表时间：
1997
影响因子：
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通讯作者：
J. Ogier
中科院分区：
文献类型：
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作者：
M. Sciotti;C. Chatenay‐Rivauday;I. Yamodo;J. Ogier
许多兴趣集中在含有细胞表面多肽的口腔链球菌抗原I/II家族，其具有许多结合功能，即对唾液成分（1）和单核细胞（4）。这些性质可能是至关重要的口腔链球菌的定植能力，参与龋齿的病因学和亚急性炎症性疾病的发病机制。到目前为止，大多数关于抗原I/II的结合活性的研究集中在与唾液受体的粘附上，并且涉及两个非常保守的区域，N-末端丙氨酸富集区（A）和中间脯氨酸富集区（P）（1，2）。我们的目标是调查的结合库的抗原I/IIf从变形链球菌的特异性和本地化的相关功能域，在检查的重组抗原I/IIf（recI/IIf）的衍生物对人类唾液成分，上皮细胞和单核细胞的膜成分，以及对细胞外和基质蛋白的结合活性。
Much interest has been focused on the oral streptococcal antigen I/II family containing cell surface polypeptides to which have been attributed a number of binding functions, namely towards salivary constituents (1) and monocytes (4). These properties could be critical in the colonization ability of oral streptococci involved in the aetiology of dental caries and in the pathogenesis of subacute inflammatory disorders. Up to now, most of the studies of the binding activity of the antigens I/II focused on adhesion to salivary receptors and concerned two well conserved regions, the N-terminal alanine-rich domain (A) and the middle proline-rich region (P) (1, 2). Our goal is to investigate the binding-repertoire of the antigen I/IIf from Streptococcus mutans in terms of specificity and localization of relevant functional domains, in examining the binding activity of derivatives of the recombinant antigen I/IIf (recI/IIf) towards human salivary components, membrane components of epithelial cells and monocytes, as well as towards extracellular and matrix proteins.
人粒细胞在细胞表面表达 55 kDa 脂多糖结合蛋白，该蛋白与杀菌/通透性增加蛋白相同。
DOI：
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发表时间：
1993
期刊：
Journal of immunology (Baltimore, Md. : 1950)
影响因子：
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作者：
Weersink,AJ;vanKessel,KP;vandenTol,ME;vanStrijp,JA;Torensma,R;Verhoef,J;Elsbach,P;Weiss,J
通讯作者：
Weiss,J