Related Experiment Video

Updated: Jan 5, 2026

Monitoring Stub1-Mediated Pexophagy
08:26

Monitoring Stub1-Mediated Pexophagy

Published on: May 12, 2023

2.0K

The zinc containing pro-apoptotic protein siva interacts with the peroxisomal membrane protein pmp22

Matthias Nestler1, Ulrike Martin, Peter Hortschansky

  • 1Department of Cell and Molecular Biology, Leibniz-Institute for Natural Product Research and Infection Biology--Hans-Knöll-Institute, Jena, Germany. mnestler@fli-leibniz.de

Molecular and Cellular Biochemistry
|May 10, 2006
PubMed

Insights

Host Siva protein, upregulated during coxsackievirus B3 infection, interacts with peroxisomal membrane protein PMP22. This interaction may influence programmed cell death in response to viral myocarditis and pancreatitis.

Area of Science:

  • Virology
  • Immunology
  • Cell Biology

Background:

  • Host responses to pathogen attacks are critical for determining disease outcomes.
  • Coxsackievirus B3 (CVB3) infection can lead to severe myocarditis and pancreatitis.
  • The pro-apoptotic host protein Siva is upregulated following CVB3 infection, mediating programmed cell death.

Purpose of the Study:

  • To identify new host factors involved in the response to CVB3 infection.
  • To elucidate the molecular interactions of the Siva protein in the context of viral pathogenesis.

Main Methods:

  • Screening of a human heart cDNA library to identify Siva interaction partners.
  • Expression and purification of Siva protein in Escherichia coli for structural analysis.
  • Directed two-hybrid assays to map protein-protein interaction domains.

Main Results:

  • Identification of peroxisomal membrane protein 22 (PMP22) as a novel Siva interaction partner.
  • Analysis of Siva revealed it binds three zinc ions, indicating a complex structure.
  • The N-terminal region of Siva was identified as the binding site for CD27.

Conclusions:

  • PMP22 may play a role in the host's defense mechanisms against CVB3.
  • Understanding Siva's interactions provides insights into host-pathogen dynamics and programmed cell death pathways.
  • Further research is warranted to explore the functional significance of the Siva-PMP22 interaction in CVB3 pathogenesis.

More Related Videos

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro08:53

Using Scaffold Liposomes to Reconstitute Lipid-proximal Protein-protein Interactions In Vitro

Published on: January 11, 2017

9.3K
Identifying Protein-protein Interaction Sites Using Peptide Arrays07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

18.5K

Related Concept Videos

The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
8.1K
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
7.9K
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
5.1K
Phagocytosis of Apoptotic Cells01:17

Phagocytosis of Apoptotic Cells

Cells undergoing apoptosis form apoptotic bodies that must be removed immediately to prevent inflammation, autoimmune diseases, and necrosis. Phagocytosis is carried out by professional phagocytes such as macrophages or  immature dendritic cells. Non-professional phagocytes such as  epithelial cells and fibroblasts also take part in this process; however, they are not as effective as professional phagocytes. 
Normal cells contain receptors that prevent them from being recognized...
4.8K
Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
13.6K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
11.8K