Lectin activity of the pneumococcal pilin proteins.

Lectin activity of the pneumococcal pilin proteins.
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DOI:
10.1038/s41598-017-17850-9
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发表时间:
2017-12-19
期刊:
影响因子:
4.6
通讯作者:
Jennings MP
Jennings MP
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Day CJ;Paton AW;Harvey RM;Hartley-Tassell LE;Seib KL;Tiralongo J;Bovin N;Savino S;Masignani V;Paton JC;Jennings MP

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肺炎链球菌是全球发病率和死亡率的主要原因。此前已对肺炎链球菌的Pilus-1蛋白、RrgA、RrgB和RrgC在感染、侵袭性疾病和可能的候选疫苗中的作用进行了评估。在这项研究中,我们研究了所有三种Pilus-1蛋白的聚糖结合库,发现尖端粘附素RrgA在三种蛋白中具有最广泛的聚糖识别,与麦芽糖/纤维素二糖,α/β连接的半乳糖和血型A和H抗原结合。RrgB只结合甘露糖,而RrgC结合了一个也被RrgA识别的聚糖子集。利用通过聚糖阵列分析鉴定的四种寡糖作为竞争性抑制剂,测试了肺炎链球菌TIGR4对上皮细胞的粘附性。血H三糖对肺炎链球菌TIGR4粘附的阻断效果最好。粘附是疾病的第一步,宿主糖缀合物是许多粘附素的共同目标。本研究已经确定了Pilus-1蛋白作为一种新的凝集素参与了肺炎链球菌对宿主糖基化的靶向。
Streptococcus pneumoniae is a leading cause of morbidity and mortality globally. The Pilus-1 proteins, RrgA, RrgB and RrgC of S. pneumoniae have been previously assessed for their role in infection, invasive disease and as possible vaccine candidates. In this study we have investigated the glycan binding repertoire of all three Pilus-1 proteins, identifying that the tip adhesin RrgA has the broadest glycan recognition of the three proteins, binding to maltose/cellobiose, α/β linked galactose and blood group A and H antigens. RrgB only bound mannose, while RrgC bound a subset of glycans also recognized by RrgA. Adherence of S. pneumoniae TIGR4 to epithelial cells was tested using four of the oligosaccharides identified through the glycan array analysis as competitive inhibitors. The blood group H trisaccharide provided the best blocking of S. pneumoniae TIGR4 adherence. Adherence is the first step in disease, and host glycoconjugates are a common target for many adhesins. This study has identified Pilus-1 proteins as new lectins involved in the targeting of host glycosylation by S. pneumoniae.
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发表时间: 2004-01-01
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