Development of inhibitory peptide in oral bacterial coaggregation

本研究的目的是确定介导牙龈卟啉单胞菌与口腔革兰氏阳性菌共聚集的共粘附素，并开发共聚集抑制肽。在牙龈卟啉单胞菌的各种组分中，菌毛对牙龈卟啉单胞菌与口腔链球菌的共聚集有较强的抑制作用。利用重组fimbrillin和合成肽的抑制研究表明，fimbrillin的氨基酸残基266-286包含参与共聚集的结构域。以前，我们报道了该结构域介导牙龈卟啉单胞菌与富含脯氨酸蛋白（REP）和statherin的结合。因此，该肽可能是一种有效的抑制牙龈卟啉单胞菌粘附的抑制剂。我们还报道了PRP的羧基末端片段负责REP结合牙龈卟啉单胞菌。在这项研究中，我们发现该片段抑制牙龈卟啉单胞菌粘附于形成菌斑的革兰氏阳性菌， ...更多信息 该片段似乎也是有效的聚集抑制肽之一。为了鉴定来自革兰氏阳性菌的粘附素，检查了来自口腔链球菌的表面组分与牙龈卟啉单胞菌纤毛的相互作用。35-kDa口腔链球菌表面组分与牙龈卟啉单胞菌菌毛反应。部分纯化的35-kDa蛋白抑制牙龈卟啉单胞菌和口腔链球菌之间的共聚集。抗35-kDa蛋白的抗体与血链球菌和戈登链球菌发生反应，表明口腔链球菌35-kDa表面蛋白的相似蛋白存在于多种口腔革兰阳性菌中。它们似乎在共聚集中也起着重要作用。35 kDa蛋白中牙龈卟啉单胞菌结合区的进一步鉴定正在进行中。在本研究中，我们获得了几种抑制牙龈卟啉单胞菌粘附革兰氏阳性菌的肽。虽然这些肽的进一步评估是必要的，他们可能是可用的，以防止牙龈卟啉单胞菌粘附牙菌斑。少

The objects of this study are to determine the coadhesins which mediate coaggregation between Pomhyromonas gingivalis and oral gram-positive bacteria, and to develop inhibitory peptide in the coaggregation. Among various components of P.gingivalis, fimbriae strongly inhibited the coaggregation between P.gingivalis and Streptococcus oralis by the turbidimetric method. The inhibition studies using recombinant fimbrillin and synthetic peptides showed that amino acid residues 266-286 of fimbrillin contain a domain involved in the coaggregation. Previously, we reported that this domain mediates the binding of P.gingivalis to praline-rich protein (REP) and statherin. Therefore, this peptide may acy as an effective inhibitor against P.gingivalis adherence. We also reported that the carboxyl-terminal fragment of PRP is responsible for the REP-binding to P.gingivalis. In this study, we found that this fragment inhibited P.gingivalis adherence to plaque-forming gram-positive bacteria as well as … More to PRP.This fragment also appears to be one of the potent coaggregation-inhibitory peptides. To identify the coadhesin from gram-positive bacteria, the interactions of surface components from S.oralis with P.gingivalis flmbriae were examined. 35-kDa S.orals surface component reacted with P.gingivalis fimbriae. The partial purified 35-kDa protein inhibited the coaggregation between P.gingivalis and S.oralls. The antibodies against 35-kDa protein reacted with Streptococcus sanguis and Streptococcus gordonii, indicating that the similar proteins related to 35-kDa S.oralis surface protein exsit in various oral gram-positive bacteria. They also seems to play an important role in the coaggregation. Further identification of the P.gingivalis binding region in the 35-kDa protein is in progress. In-this study, we obtained several peptides which inhibit P.gingivalls adherence to gram-positive bacteria. Although further evaluation of these peptides are necessary, they may be avairable to prevent P.gingivalls adherence to dental plaque. Less