Budding of enveloped viruses from the plasma membrane

Cadd, Tamarra L.; Skoging, Ulrica; Liljeström, Peter

doi:10.1002/bies.950191109

Cited by 28 publications

(23 citation statements)

References 88 publications

(35 reference statements)

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“…In our knowledge no tools for such analysis exist in commonly used MD packages and molecular visualization programs, such as GROMACS [22], NAMD [23], AMBER [24], VMD [10], and PyMol [11]. All existing tools are based on the assumption that the membrane is planar and the membrane normal is oriented along Z axis of the simulation box, which is obviously not the case for the curved membrane.…”

Section: Methodsmentioning

confidence: 99%

“…Such phenomena include the formation of synaptic vesicles [18], formation of apoptotic bodies [19, 20], the processes of membrane fusion [21, 22], and budding of enveloped viruses from the plasma membrane [23, 24]. Another intriguing phenomenon is the formation of blebs—small spontaneous bulges on the membrane, which lack support of filaments or cytoskeleton proteins and often observed during apoptosis [19, 20] blood cell maturing [10] and mitosis [11] (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

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Cholesterol Induces Uneven Curvature of Asymmetric Lipid Bilayers

Yesylevskyy

Demchenko

Kraszewski

et al. 2013

The Scientific World Journal

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A remarkable flexibility is observed in biological membranes, which allows them to form the structures of different curvatures. We addressed the question of intrinsic ability of phospholipid membranes to form highly curved structures and the role of cholesterol in this process. The distribution of cholesterol in the highly curved asymmetric DOPC/DOPS lipid bilayer was investigated by the coarse-grained molecular dynamics simulations in the membrane patches with large aspect ratio. It is shown that cholesterol induces uneven membrane curvature promoting the formation of extended flattened regions of the membrane interleaved by sharp bends. It is shown that the affinity of cholesterol to anionic DOPS or neutral DOPC lipids is curvature dependent. The cholesterol prefers DOPS to DOPC in either planar or highly curved parts of the membrane. In contrast, in the narrow interval of moderate membrane curvatures this preference is inverted. Our data suggest that there is a complex self-consistent interplay between the membrane curvature and cholesterol distribution in the asymmetric lipid bilayers. The suggested new function of cholesterol may have a biological relevance.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Cholesterol Induces Uneven Curvature of Asymmetric Lipid Bilayers

Yesylevskyy

Demchenko

Kraszewski

et al. 2013

The Scientific World Journal

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“…Viral morphogenesis is a complex phenomenon requiring concerted actions of many viral and host components (for review, see Cadd et al, 1997;Garoff et al, 1998;Nayak, 2000;Pettersson, 1991;Simons and Garoff, 1980). Among the host components that are intimately involved in regulating different aspects of the influenza virus life cycle, lipid rafts play a number of important roles.…”

Section: Role Of Lipid Rafts In Virus Buddingmentioning

confidence: 99%

Assembly and budding of influenza virus

Nayak¹,

Hui²,

Barman³

2004

Virus Research

308

262

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Influenza viruses are causative agents of an acute febrile respiratory disease called influenza (commonly known as "flu") and belong to the Orthomyxoviridae family. These viruses possess segmented, negative stranded RNA genomes (vRNA) and are enveloped, usually spherical and bud from the plasma membrane (more specifically, the apical plasma membrane of polarized epithelial cells). Complete virus particles, therefore, are not found inside infected cells. Virus particles consist of three major subviral components, namely the viral envelope, matrix protein (M1), and core (viral ribonucleocapsid [vRNP]). The viral envelope surrounding the vRNP consists of a lipid bilayer containing spikes composed of viral glycoproteins (HA, NA, and M2) on the outer side and M1 on the inner side. Viral lipids, derived from the host plasma membrane, are selectively enriched in cholesterol and glycosphingolipids. M1 forms the bridge between the viral envelope and the core. The viral core consists of helical vRNP containing vRNA (minus strand) and NP along with minor amounts of NEP and polymerase complex (PA, PB1, and PB2). For viral morphogenesis to occur, all three viral components, namely the viral envelope (containing lipids and transmembrane proteins), M1, and the vRNP must be brought to the assembly site, i.e. the apical plasma membrane in polarized epithelial cells. Finally, buds must be formed at the assembly site and virus particles released with the closure of buds. Transmembrane viral proteins are transported to the assembly site on the plasma membrane via the exocytic pathway. Both HA and NA possess apical sorting signals and use lipid rafts for cell surface transport and apical sorting. These lipid rafts are enriched in cholesterol, glycosphingolipids and are relatively resistant to neutral detergent extraction at low temperature. M1 is synthesized on free cytosolic polyribosomes. vRNPs are made inside the host nucleus and are exported into the cytoplasm through the nuclear pore with the help of M1 and NEP. How M1 and vRNPs are directed to the assembly site on the plasma membrane remains unclear. The likely possibilities are that they use a piggy-back mechanism on viral glycoproteins or cytoskeletal elements. Alternatively, they may possess apical determinants or diffuse to the assembly site, or a combination of these pathways. Interactions of M1 with M1, M1 with vRNP, and M1 with HA and NA facilitate concentration of viral components and exclusion of host proteins from the budding site. M1 interacts with the cytoplasmic tail (CT) and transmembrane domain (TMD) of glycoproteins, and thereby functions as a bridge between the viral envelope and vRNP. Lipid rafts function as microdomains for concentrating viral glycoproteins and may serve as a platform for virus budding. Virus bud formation requires membrane bending at the budding site. A combination of factors including concentration of and interaction among viral components, increased viscosity and asymmetry of the lipid bilayer of the lipid raft as well as pulling and pushi...

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“…Most likely, this can be explained by the fact that SFV is an alphavirus, which is structurally different from the two negative strand RNA viruses FPV and VSV. Alphaviruses have a very high protein content, and the icosahedral lattices of the spike and capsid proteins are connected by strong protein-protein interactions (31,32). These tightly packed protein assemblies might cause the ordered structure of the membrane, sensed by the lipid probe.…”

Section: Fig 2 Cholesterol Extractability In Viral and Cellular Memmentioning

confidence: 99%