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Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

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...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Structure of Porins01:21

Structure of Porins

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 precursors...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell types have...

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Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
10:21

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification

Published on: November 16, 2016

Outer membrane proteins of Pasteurella multocida.

Tamás Hatfaludi1, Keith Al-Hasani, John D Boyce

  • 1Department of Microbiology, Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Clayton, VIC 3800, Australia.

Veterinary Microbiology
|March 4, 2010
PubMed
Summary
This summary is machine-generated.

Pasteurella multocida outer membrane proteins and lipoproteins are crucial for host interaction and immune response. This review details their roles in pathogenesis and immunity for this common animal pathogen.

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Area of Science:

  • Veterinary Microbiology
  • Bacterial Pathogenesis
  • Immunology

Background:

  • Pasteurella multocida is a widespread bacterial pathogen affecting numerous animal species.
  • Outer membrane components, including transmembrane proteins and lipoproteins, mediate pathogen-host interactions.
  • These components are critical in modulating the host immune response during infection.

Purpose of the Study:

  • To review and synthesize current knowledge on Pasteurella multocida outer membrane proteins (OMPs).
  • To elucidate the specific roles of these OMPs in the pathogenesis of P. multocida infections.
  • To evaluate the involvement of P. multocida OMPs in host immunity.

Main Methods:

  • Comprehensive literature review of studies on P. multocida outer membrane proteins.
  • Analysis of research focusing on the structure and function of P. multocida OMPs.
  • Synthesis of data regarding the immunomodulatory and pathogenetic contributions of these proteins.

Main Results:

  • P. multocida OMPs and lipoproteins are key virulence factors.
  • These proteins are involved in bacterial adhesion, invasion, and immune evasion.
  • Specific OMPs elicit distinct host immune responses, influencing disease outcome.

Conclusions:

  • Outer membrane proteins are essential for Pasteurella multocida's ability to cause disease.
  • Understanding these proteins offers targets for vaccine development and therapeutic strategies.
  • Further research into P. multocida OMPs will enhance control of infections in animals.