The changing faces of Streptococcus antigen I/II polypeptide family adhesins.

The changing faces of Streptococcus antigen I/II polypeptide family adhesins.
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DOI:
10.1111/j.1365-2958.2010.07212.x
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发表时间:
2010-07
影响因子:
3.6
通讯作者:
Jenkinson HF
Jenkinson HF
中科院分区:
生物学2区
文献类型:
--
作者:
Brady LJ;Maddocks SE;Larson MR;Forsgren N;Persson K;Deivanayagam CC;Jenkinson HF

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变形链球菌抗原 I/II (AgI/II) 蛋白是革兰氏阳性细菌中最早发现的细胞壁锚定粘附素之一。它介导变形链球菌附着在牙齿表面,并且一直是龋齿免疫研究的焦点。 AgI/II 家族多肽识别唾液糖蛋白,还参与生物膜形成、血小板聚集、组织侵袭和免疫调节。编码AgI/II家族多肽的基因存在于人类口腔固有的链球菌属物种以及化脓性链球菌、无乳链球菌和猪链球菌中。 AgI/II 蛋白不同区域的功能证据已经出现。戈登链球菌 SspB (AgI/II) C 端部分的序列基序与牙龈卟啉单胞菌结合,从而促进这种厌氧病原体在口腔定植。随着区域晶体结构的解析,其他表位的重要性现在更加清晰。中央V(可变)区的新图像出现了,预计包含碳水化合物结合沟槽,由氨基末端α螺旋和羧基末端聚脯氨酸螺旋之间不寻常的关联形成的茎从细胞表面突出。这种呈现模式对于确定其他革兰氏阳性表面蛋白的功能构象可能很重要,这些表面蛋白具有侧翼为α螺旋和富含脯氨酸区域的粘附素结构域。
Streptococcus mutans antigen I/II (AgI/II) protein was one of the first cell-wall anchored adhesins identified in Gram-positive bacteria. It mediates attachment of Streptococcus mutans to tooth surfaces and has been a focus for immunization studies against dental caries. The AgI/II family polypeptides recognize salivary glycoproteins, and are also involved in biofilm formation, platelet aggregation, tissue invasion, and immune modulation. The genes encoding AgI/II family polypeptides are found amongst Streptococcus species indigenous to the human mouth, as well as in S. pyogenes, S. agalactiae, and S. suis. Evidence of functionalities for different regions of the AgI/II proteins has emerged. A sequence motif within the C-terminal portion of Streptococcus gordonii SspB (AgI/II) is bound by Porphyromonas gingivalis, thus promoting oral colonization by this anaerobic pathogen. The significance of other epitopes is now clearer following resolution of regional crystal structures. A new picture emerges of the central V (variable) region, predicted to contain a carbohydrate-binding trench, being projected from the cell surface by a stalk formed by an unusual association between an amino-terminal α-helix and a carboxy-terminal polyproline helix. This presentation mode might be important in determining functional conformations of other Gram-positive surface proteins that have adhesin domains flanked by α-helical and proline-rich regions.
DOI: 10.1128/iai.01315-07
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影响因子: 3.1
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