PILR alpha and PILR beta have a siglec fold and provide the basis of binding to sialic acid
文献类型：期刊论文
| 作者 | Lu, Qiong1,2; Lu, Guangwen1; Qi, Jianxun1; Wang, Han1,2; Xuan, Yifang3; Wang, Qihui1; Li, Yan1; Zhang, Yanfang4; Zheng, Chunfu5,6; Fan, Zheng1 |
| 刊名 | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
 |
| 出版日期 | 2014-06-03 |
| 卷号 | 111期号:22页码:8221-8226 |
| 英文摘要 | Paired immunoglobulin-like type 2 receptor alpha (PILR alpha) and beta (PILR beta) belong to the PILR family and are related to innate immune regulation in various species. Despite their high sequence identity, PILR alpha and PILR beta are shown to have variant sialic acid (SA) binding avidities. To explore the molecular basis of this interaction, we solved the crystal structures of PILR alpha and PILR beta at resolutions of 1.6 and 2.2 angstrom, respectively. Both molecules adopt a typical siglec fold but use a hydrophobic bond to substitute the siglecspecific disulfide linkage for protein stabilization. We further used HSV-1 glycoprotein B (gB) as a representative molecule to study the PILR-SA interaction. Deploying site-directed mutagenesis, we demonstrated that three residues (Y2, R95, and W108) presented on the surface of PILR alpha form the SA binding site equivalent to those in siglecs but are arranged in a unique linear mode. PILR beta differs from PILR alpha in one of these three residues (L108), explaining its inability to engage gB. Mutation of L108 to tryptophan in PILR beta restored the gB-binding capacity. We further solved the structure of this PILR beta mutant complexed with SA, which reveals the atomic details mediating PILR/SA recognition. In comparison with the free PILR structures, amino acid Y2 oriented variantly in the complex structure, thereby disrupting the linear arrangement of PILR residues Y2, R95, and W108. In conclusion, our study provides significant implications for the PILR-SA interaction and paves the way for understanding PILR-related ligand binding. |
| WOS标题词 | Science & Technology |
| 类目[WOS] | Multidisciplinary Sciences |
| 研究领域[WOS] | Science & Technology - Other Topics |
| 关键词[WOS] | TYPE-2 RECEPTOR-ALPHA ; VIRUS GLYCOPROTEIN-D ; CRYSTAL-STRUCTURE ; CELL-ADHESION ; RECOGNITION ; ACTIVATION ; COMPLEX ; DOMAIN ; SIALOADHESIN ; RESOLUTION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000336687900079 |
| 源URL | [http://124.16.173.210/handle/834782/1339]  |
| 专题 | 天津工业生物技术研究所_蛋白质工程与疫苗实验室 高福_期刊论文 |
| 作者单位 | 1.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Chinese Acad Sci, Beijing Inst Life Sci, Res Network Immun & Hlth, Beijing 100101, Peoples R China 4.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Lab Prot Engn & Vaccines, Tianjin 300308, Peoples R China 5.Soochow Univ, Inst Biol, Suzhou 215123, Peoples R China 6.Soochow Univ, Inst Med Sci, Suzhou 215123, Peoples R China 7.Chinese Ctr Dis Control & Prevent, Off Director Gen, Beijing 102206, Peoples R China |
| 推荐引用方式 GB/T 7714 | Lu, Qiong,Lu, Guangwen,Qi, Jianxun,et al. PILR alpha and PILR beta have a siglec fold and provide the basis of binding to sialic acid[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2014,111(22):8221-8226. |
| APA | Lu, Qiong.,Lu, Guangwen.,Qi, Jianxun.,Wang, Han.,Xuan, Yifang.,...&Gao, George F..(2014).PILR alpha and PILR beta have a siglec fold and provide the basis of binding to sialic acid.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,111(22),8221-8226. |
| MLA | Lu, Qiong,et al."PILR alpha and PILR beta have a siglec fold and provide the basis of binding to sialic acid".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 111.22(2014):8221-8226. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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