Coronavirus pleomorphism

Kanso, M. A.; Naime, Marwa; Chaurasia, Vikash; Tontiwattanakul, Khemapat; Fried, Eliot; Giacomin, A. Jeffrey

doi:10.1063/5.0094771

Cited by 9 publications

(3 citation statements)

References 31 publications

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“…We also investigated the impact of aspherical membrane cap morphology on the radius of induced scission necks by membrane-remodeling proteins (Figure B,C). This can be a representation of (I) the tubular membrane invagination in yeast endocytosis and (II) the aspherical morphology of the membrane wrapping of elongated viruses such as coronavirus, Ebola, Marburg, and bullet-shaped Rhabdoviruses. − Influenza A virus is also known as a pleomorphic virus which displays a range of morphologies from filamentous to spherical . Here, for simplicity, we only considered prolate-shaped caps with an aspect ratio ( r 2 / r 1 ) > 1 (Figure B) and oblate-shaped caps with an aspect ratio <1 (Figure C).…”

Section: Resultsmentioning

confidence: 99%

Comparing Multifunctional Viral and Eukaryotic Proteins for Generating Scission Necks in Membranes

Alimohamadi,

Luo,

Gupta

et al. 2024

ACS Nano

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Deterministic formation of membrane scission necks by protein machinery with multiplexed functions is critical in biology. A microbial example is M2 viroporin, a proton pump from the influenza A virus that is multiplexed with membrane remodeling activity to induce budding and scission in the host membrane during viral maturation. In comparison, the dynamin family constitutes a class of eukaryotic proteins implicated in mitochondrial fission, as well as various budding and endocytosis pathways. In the case of Dnm1, the mitochondrial fission protein in yeast, the membrane remodeling activity is multiplexed with mechanoenzyme activity to create fission necks. It is not clear why these functions are combined in these scission processes, which occur in drastically different compositions and solution conditions. In general, direct experimental access to changing neck sizes induced by individual proteins or peptide fragments is challenging due to the nanoscale dimensions and influence of thermal fluctuations. Here, we use a mechanical model to estimate the size of scission necks by leveraging small-angle X-ray scattering structural data of protein−lipid systems under different conditions. The influence of interfacial tension, lipid composition, and membrane budding morphology on the size of the induced scission necks is systematically investigated using our data and molecular dynamic simulations. We find that the M2 budding protein from the influenza A virus has robust pH-dependent membrane activity that induces nanoscopic necks within the range of spontaneous hemifission for a broad range of lipid compositions. In contrast, the sizes of scission necks generated by mitochondrial fission proteins strongly depend on lipid composition, which suggests a role for mechanical constriction.

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Section: Resultsmentioning

confidence: 99%

Comparing Multifunctional Viral and Eukaryotic Proteins for Generating Scission Necks in Membranes

Alimohamadi,

Luo,

Gupta

et al. 2024

ACS Nano

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“…3B and C). This can be a representation of (I) the tubular membrane invagination in yeast endocytosis 61 and (II) the aspherical morphology of the membrane wrapping of elongated viruses such as coronavirus, Ebola, Marburg, and bullet-shaped Rhabdoviruses [62][63][64][65][66] . Influenza A virus is also known as a pleomorphic virus which displays a range of morphologies from filamentous to spherical 67 .…”

Section: The Morphology Of Membrane Caps Influences the Radius Of Ind...mentioning

confidence: 99%

Comparing multifunctional viral and eukaryotic proteins for generating scission necks in membranes

Alimohamadi,

Luo,

Gupta

et al. 2024

Preprint

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Deterministic formation of membrane scission necks by protein machinery with multiplexed functions is critical in biology. A microbial example is the M2 viroporin, a proton pump from the influenza A virus which is multiplexed with membrane remodeling activity to induce budding and scission in the host membrane during viral maturation. In comparison, the dynamin family constitutes a class of eukaryotic proteins implicated in mitochondrial fission, as well as various budding and endocytosis pathways. In the case of Dnm1, the mitochondrial fission protein in yeast, the membrane remodeling activity is multiplexed with mechanoenzyme activity to create fission necks. It is not clear why these functions are combined in these scission processes, which occur in drastically different compositions and solution conditions. In general, direct experimental access to changing neck sizes induced by individual proteins or peptide fragments is challenging due to the nanoscale dimensions and influence of thermal fluctuations. Here, we use a mechanical model to estimate the size of scission necks by leveraging Small-Angle X-ray Scattering (SAXS) structural data of protein-lipid systems under different conditions. The influence of interfacial tension, lipid composition, and membrane budding morphology on the size of the induced scission necks is systematically investigated using our data and molecular dynamic simulations. We find that the M2 budding protein from the influenza A virus has robust pH-dependent membrane activity that induces nanoscopic necks within the range of spontaneous hemi-fission for a broad range of lipid compositions. In contrast, the sizes of scission necks generated by mitochondrial fission proteins strongly depend on lipid composition, which suggests a role for mechanical constriction.

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“…These peplomers, identically charged, repel one another over the surface of their convex capsids to form beautiful polyhedra. 4,5 These convex capsids may or may not be spherical, 6 and their peplomer population declines after infection. 7 These peplomers are short, equidimensional, and bulbous with triangular bulbs.…”

Section: Introductionmentioning

confidence: 99%

Coronavirus peplomer interaction

Pak¹,

Chakraborty

Kanso

et al. 2022

Physics of Fluids

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By virtue of their lack of motility, viruses rely entirely on their own temperature (Brownian motion) to position themselves properly for cell attachment. Spiked viruses use one or more spikes (called peplomers) to attach. The coronavirus uses adjacent peplomer pairs. These peplomers, identically charged, repel one another over the surface of their convex capsids to form beautiful polyhedra. We identify the edges of these polyhedra with the most important peplomer hydrodynamic interactions. These convex capsids may be spherical or not, and their peplomer population declines with infection time. These peplomers are short, equidimensional, and bulbous, with triangular bulbs. In this short paper, we explore the interactions between nearby peplomer bulbs. By interactions, we mean the hydrodynamic interferences between the velocity profiles caused by the drag of the suspending fluid when the virus rotates. We find that these peplomer hydrodynamic interactions raise rotational diffusivity of the virus, and thus affect its ability to infect.

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Coronavirus pleomorphism

Cited by 9 publications

References 31 publications

Comparing Multifunctional Viral and Eukaryotic Proteins for Generating Scission Necks in Membranes

Comparing Multifunctional Viral and Eukaryotic Proteins for Generating Scission Necks in Membranes

Comparing multifunctional viral and eukaryotic proteins for generating scission necks in membranes

Coronavirus peplomer interaction

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