関連する実験動画
Updated: Sep 10, 2025

12:22
Biomimetic Materials to Characterize Bacteria-host Interactions
Published on: November 16, 2015
9.5K
ストレプトコッカス・ミュータンス コラーゲン結合タンパク質 Cnm は多機能的粘着剤:構造的調査
Joshua L Mieher1, Norbert Schormann1, Ren Wu1
1Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, USA.
Molecular oral microbiology
|August 27, 2025
まとめ
Streptococcus mutansのコラーゲン結合アデシンCnmは,コラーゲンとグリコタンパク質340の両方に結合する. 主要な残留物Y176とF192は,この二重結合に不可欠であり,毒性を影響する.
科学分野:
- 微生物学
- 構造生物学
- 生物化学
背景:
- コラーゲン結合アデシン (Cnm) は,Streptococcus mutansの毒性因子である.
- Cnmは特定のS. mutans血清型に存在し,細胞壁に固定された表面粘着剤である.
- それはLPXTGのアデシンファミリーに属します.
研究 の 目的:
- S. mutans CnmのN2ドメインの結晶構造を決定する.
- コラーゲンの結合をS. mutans Cnmにモデル化するために
- Cnmの多機能結合特性について研究する.
主な方法:
- Cnm N2ドメインの結晶構造の決定
- Staphylococcus aureus Cnaを用いたホモロジーモデリング
- プロテイン対プロテインドッキングとコンペティションアッセイ
- アラニン置換変異
主要な成果:
- S. mutans Cnm N2ドメインの結晶構造が決定された.
- モデリングは,Cnaと比較して,コラーゲン結合に関与する保存および異なる残基を特定した.
- Cnmは,グリコプロテイン340 (Gp340) のスキャベンジャー受容体システインに富んだドメイン (SRCR) に高い親和性で結合する.
- コラーゲンとSRCRドメインはCnmの共通の結合部位を共有しています.
- 残留物Y176とF192は,コラーゲンとGp340の両方に結合する上で重要であることが確認された.
結論:
- S. mutans Cnmは多機能結合能力を有している.
- コラーゲンとGp340結合部位はCnm N2領域で重なり合っている.
- 主要な残留物Y176とF192は,S. mutansの毒性におけるその重要性を強調する,コラーゲンとGp340の両方のCnmの相互作用に不可欠である.
関連する概念動画
Structural Protein Function
28.4K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
28.4K
Immunoglobulin-like Cell Adhesion Molecules
3.4K
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...
3.4K
Structure of Cadherins
3.6K
The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins” is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
3.6K
Adherens Junctions
5.0K
Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types – adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
Adherens Junctions are Dynamic
5.0K
Tension Response at Adherens Junctions
2.8K
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
2.8K
Fimbriae, Pili, and Axial Filaments
339
Fimbriae and pili are specialized bacterial surface structures that play pivotal roles in adhesion, genetic exchange, and motility. Composed primarily of pilin protein, these hairlike appendages are crucial for bacterial survival and pathogenicity in various environments.Fimbriae: Adhesion and PathogenicityFimbriae are fine, filamentous structures measuring 2–10 nanometers in diameter and are densely distributed on the bacterial cell surface. They facilitate bacterial adhesion to abiotic...
339

