Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 protein

Larisa V Kordyukova1, Eleonora V Shtykova2,3, Lyudmila A Baratova1

  • 1a Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University , Moscow , Russian Federation.

Insights

Influenza A virus M1 matrix protein structure is challenging to determine due to its disordered C-terminal region. This intrinsic disorder is crucial for the M1 protein's function and interactions within the virus.

Area of Science:

  • Virology
  • Structural Biology
  • Biophysics

Background:

  • Influenza A virus is a significant pathogen, necessitating detailed study of its components.
  • The M1 matrix protein is the most abundant viral component, forming a structural scaffold beneath the envelope.
  • The precise structure and function of the M1 protein remain incompletely understood, with ongoing debate.

Purpose of the Study:

  • To investigate the structural characteristics of the Influenza A virus M1 matrix protein.
  • To understand the role of intrinsic disorder in the M1 protein's C-terminal domain.
  • To explore M1 protein self-association and interactions with viral components and membranes.

Main Methods:

  • Synchrotron small-angle X-ray scattering (SAXS)
  • Atomic force microscopy (AFM)
  • Cryo-electron microscopy/tomography (cryo-EM/ET)

Main Results:

  • High-resolution crystal structures of full-length Influenza A virus M1 protein are unavailable, likely due to C-terminal disorder.
  • Alternative structural methods reveal similarities between Influenza A virus M1 protein and matrix proteins of other enveloped RNA viruses.
  • The intrinsic disorder in the M1 protein's C-terminal domain appears to have significant functional implications.

Conclusions:

  • The M1 matrix protein's structure is influenced by intrinsic disorder, particularly in its C-terminal region.
  • Common interaction principles and potential evolutionary links exist among matrix proteins of enveloped RNA viruses.
  • Understanding M1 protein structure is key to deciphering Influenza A virus assembly and lifecycle.

Related Concept Videos

What are Viruses?00:50

What are Viruses?

Overview
128.5K
Golgi Matrix Proteins01:12

Golgi Matrix Proteins

Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
2.5K
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.9K
Introduction to Virus01:28

Introduction to Virus

Viruses are unique biological entities that blur the boundary between living and non-living systems. Although they lack cellular structure and metabolic processes, they can exhibit characteristics of life when infecting a host. Their defining feature is a nucleic acid core, composed of either DNA or RNA, encapsulated within a protein coat called a capsid. This simple structure allows them to invade host cells and use their machinery for replication efficiently.Viral Structure and...
1.9K
Viruses of Archaea01:29

Viruses of Archaea

Archaeal viruses play a crucial role in the ecosystems of extremophilic archaea, particularly those belonging to the phyla Euryarchaeota and Crenarchaeota. By shaping host evolution and facilitating gene transfer, these viruses influence microbial communities and contribute to genetic diversity in extreme environments. The archaea they infect thrive in acidic hot springs and hydrothermal vents characterized by high temperatures and low pH. Archaeal viruses exhibit remarkable structural...
534
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.8K