从Mycoplasma hyopneumoniae和Mycoplasma flocculare中未知功能的主导表面蛋白质中的差异域和内蛋白质加工
Priscila Souza Dos Santos1,2, Jéssica Andrade Paes1,2, Lais Del Prá Netto Machado1,2
1Laboratório de Genômica Estrutural e Funcional, Centro de Biotecnologia, Universidade Federal do Rio Grande do Sul (UFRGS), Porto Alegre, Brazil.
Heliyon
|May 30, 2023
概括
分析了未知功能的Mycoplasma hyopneumoniae表面蛋白质 (PUFs). 这些PUF可能与猪呼吸系统疾病的发展和病原体与宿主相互作用有关.
科学领域:
- 微生物学 微生物学
- 兽医科学 兽医科学 兽医科学
- 分子生物学分子生物学
背景情况:
- 在猪产业中,Mycoplasma hyopneumoniae由于猪类动物性肺炎 (PEP) 造成了重大经济损失.
- 病原体粘附和宿主免疫反应是PEP的关键,但关键决定因素仍然不清楚.
- 菌性肺炎菌具有许多功能不明的表面蛋白 (PUFs),可能参与宿主相互作用.
研究的目的:
- 在致病性M. hyopneumoniae菌株7448.8中研究五种丰富的表面PUF.
- 为了将这些PUF与非致病性M. hyopneumoniae和相关物种的ortologs进行比较.
- 确定这些PUF在M.hyopneumoniae致病性中的潜在作用.
主要方法:
- 对氨基酸序列进行比较的基分析.
- 蛋白质组数据分析以确定差异域,无序区域和动机.
- 对ortholog序列的遗传学分析.
主要成果:
- 在表面PUF中发现了不同的域,无序的区域和重复的图案.
- 发现了差异性内蛋白酶处理和抗原性的证据.
- 三种PUF在与呼吸系统疾病相关的Mycoplasma物种中显示出更高的保护性.
结论:
- 在M. hyopneumoniae中,表面占主导地位的PUF可能与致病性有关.
- 这些发现有助于理解M. hyopneumoniae与宿主相互作用.
- 对这些PUF的进一步研究可能会揭示新的诊断或治疗点.
相关概念视频
Membrane Domains
5.5K
The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
5.5K
Conservation of Protein Domains Over Different Proteins
11.0K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
11.0K
Insertion of Multi-pass Transmembrane Proteins in the RER
8.1K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
8.1K
Structure of Porins
3.0K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.0K
Mechanisms of Membrane Domain Formation
3.1K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.1K
Bacterial Protein Maturation
41
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
41


