由SIGN-R1与C1q相互作用启动的肺炎球菌多糖体的主导补充固定通路
Young-Sun Kang1, Yoonkyung Do, Hae-Kyung Lee
1Laboratory of Cellular Physiology and Immunology and Chris Browne Center for Immunology and Immune Diseases, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Cell
|April 18, 2006
概括
子学菌素SIGN-R1通过激活补充物C3.3来帮助抗感染. 这项研究揭示了SIGN-R1启动了一种不寻常的C3激活通路,这对于对S. pneumoniae的天生的免疫力至关重要.
科学领域:
- 免疫学 免疫学 免疫学
- 微生物学 微生物学
- 分子生物学分子生物学
背景情况:
- 血清补充蛋白对抗感染的天生的免疫力至关重要.
- C3转化酶对补体激活至关重要,导致病原体的opsonization.
- 脏在清除血液传播的病原体中发挥作用,例如S. pneumoniae.
研究的目的:
- 为了研究子莱克SIGN-R1在补充C3代谢和先天性抵抗中的作用.
- 阐明SIGN-R1在S. pneumoniae感染期间影响补充激活的机制.
主要方法:
- 使用了有条件的SIGN-R1淘汰赛小鼠.
- 静脉注射S. pneumoniae或其囊型多糖体.
- 评估了C3蛋白解,C3沉积在细菌上,以及C3连接体的形成.
- 研究了SIGN-R1的直接结合,以补充成分C1q.
主要成果:
- 在SIGN-R1淘汰赛小鼠中,C3代谢受损,S. pneumoniae上的C3沉积减少.
- SIGN-R1直接与C1q结合,独立于抗体或B因子,启动C3转化酶组合.
- 这种相互作用促进C3碎片的形成和沉积在脏巨细胞内的微生物上.
结论:
- 跨膜学菌素SIGN-R1是对S. pneumoniae天生的耐药性的关键调解者.
- SIGN-R1采用非传统的C3激活途径,与经典或替代途径不同.
- 这一途径通过促进脏中的C3沉积和opsonization来增强微生物清除.
相关概念视频
01:24Oligosaccharide Assembly
2.6K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
2.6K
01:30Assembly of Signaling Complexes
4.7K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
4.7K
01:11IP3/DAG Signaling Pathway
12.5K
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
12.5K
01:25Selectins
3.6K
Cell adhesion is an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
3.6K
01:31Immunoglobulin-like Cell Adhesion Molecules
3.3K
Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
3.3K
01:27Complement System
10.6K
The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
10.6K