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Related Concept Videos

Conjugated Proteins02:50

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
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...
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.
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Coronavirus01:29

Coronavirus

Coronaviruses, including the severe acute respiratory syndrome coronavirus (SARS-CoV), are enveloped viruses characterized by their single-stranded, positive-sense RNA genome and helical nucleocapsid structure. The hallmark of these viruses is their club-shaped spike (S) glycoproteins that protrude from the viral envelope, facilitating attachment to host cells. Typically, coronaviruses infect the upper respiratory tract, often causing mild or asymptomatic disease. However, certain strains like...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Synergistic Protein-Protein and Protein-Lipid Interactions Drive SARS-CoV-2 Envelope Assembly.

Ryo Urano1, Shogo Yoshimoto2, Katsutoshi Hori2

  • 1Research Institute for Interdisciplinary Science, Okayama University, 3-1-1 Tsushima-naka, Okayama 700-8530, Japan.

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Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) envelope assembly requires synergistic interactions between matrix (M) and spike (S) proteins and specific lipids. This study reveals the minimal physical requirements for forming stable viral envelopes.

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Area of Science:

  • Virology
  • Biophysics
  • Computational Biology

Background:

  • Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) assembles its viral envelope at the endoplasmic reticulum-Golgi intermediate compartment (ERGIC).
  • The minimal molecular requirements for stable viral envelope formation remain incompletely understood.

Purpose of the Study:

  • To systematically examine how protein and lipid compositions and protein orientation influence membrane remodeling during viral envelope formation using molecular dynamics simulations.
  • To identify the minimal physical requirements for robust coronavirus envelope assembly.

Main Methods:

  • Coarse-grained molecular dynamics simulations of bicelle membrane patches.
  • Comparison of lipid-only systems with membranes containing matrix (M) and spike (S) proteins under varying lipid environments and orientations.

Main Results:

  • Lipid-only membranes showed stochastic closure; M or S proteins alone formed vesicles but lacked correct topology.
  • Co-assembly of M and S proteins in ERGIC-like lipid mixtures consistently yielded stable vesicles with correct topology.
  • Protein orientation and M-S contacts were crucial for membrane curvature, cholesterol redistribution, and ordered protein positioning during closure.

Conclusions:

  • An obligate-synergy model is proposed, where M-S protein-protein contacts, M-lipid, and S-lipid interactions cooperate for viral envelope assembly.
  • Findings identify minimal physical requirements for coronavirus envelope formation.
  • Mechanistic insights may guide the rational design of coronavirus virus-like particle (VLP) assembly systems.