艾滋病毒gp120的V2域模仿了CD4和整蛋白4β7之间的相互作用
Donald Van Ryk1, Sinmanus Vimonpatranon1,2, Joe Hiatt1
1Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland, United States of America.
PLoS pathogens
|December 8, 2023
概括
CD4受体和HIV gp120与整体4β7.7相互作用. 这种结合机制解释了对CD4+ T细胞和肠道组织的HIV热带性,揭示了病毒进化和受体相互作用之间的联系.
科学领域:
- 免疫学 免疫学 免疫学
- 病毒学 病毒学
- 结构生物学 结构生物学
背景情况:
- CD4受体对适应性免疫非常重要,并作为HIV的主要对接点.
- 艾滋病毒对CD4+T细胞和肠道组织的热带性是其致病的关键方面.
- 艾滋病毒包膜蛋白gp120与CD4和整体蛋白4β7.7结合.
研究的目的:
- 为了研究CD4和4β7.7之间的分子相互作用.
- 阐明这些相互作用如何与HIV gp120结合有关.
- 了解艾滋病毒对CD4+T细胞和肠道组织的热流的基础.
主要方法:
- 分析CD4和4β7.7之间的分子相互作用.
- 结合接口和序列的比较.
- 研究CD4中Phe43等特定残留物的作用.
主要成果:
- CD4通过特定位点直接与4β7结合,包括CD4 D2.2.中的KIDIV序列.
- 艾滋病毒gp120使用类似的序列 (KLDIV) 进行4β7结合.
- 在CD4中的Phe43残留物对于gp120和4β7.7的结合至关重要.
结论:
- 艾滋病毒gp120与CD4和4β7结合,模仿了CD4-4β7相互作用的方面.
- 这些发现揭示了gp120对CD4和4β7.7的特异性之间的相互关系.
- 这表明病毒进化与CD4和4β7之间的动态相互作用有关.
更多相关视频
11:45Imaging of HIV-1 Envelope-induced Virological Synapse and Signaling on Synthetic Lipid Bilayers
Published on: March 8, 2012
12.3K
10:50Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
Published on: September 15, 2010
9.6K
相关概念视频
Immunoglobulin-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
Integrins
4.0K
Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
4.0K
Activation of Integrins
3.5K
Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding...
3.5K
Intracellular Signaling Affects Focal Adhesions
2.7K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
2.7K
Assembly of Signaling Complexes
5.8K
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,...
5.8K
