Electron Microscopy Analysis of Viral Morphogenesis

Pelchen–Matthews, Annegret; Marsh, Mark

doi:10.1016/s0091-679x(06)79020-3

Cited by 19 publications

(17 citation statements)

References 69 publications

(80 reference statements)

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“…By contrast, immunolabelling of sections of HIV-1 infected macrophages for Env indicates heavy labelling of virus particles in the assembly compartment (A. Pelchen-Matthews and M. Marsh, unpublished work). Given that antibody-Protein A-gold labelling of cryosections is inefficient (at best 10 %) [36], this suggests that macrophagederived HIV particles may have significantly higher levels of Env than T-cell-derived particles and, as a consequence, may be more infectious [37].…”

Section: Advantages Of Intracellular Virus Assemblymentioning

confidence: 99%

HIV assembly and budding in macrophages

Marsh

Theusner

Pelchen–Matthews

2009

Biochemical Society Transactions

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The formation of enveloped virus particles requires that key structural components of the virus, and the viral genomic RNA, are brought together at a cellular membrane system where new particles are assembled. The trafficking events, and the subsequent assembly and release of infectious virus particles, is co-coordinated through interactions between the viral structural proteins and cellular proteins. In the present paper, we consider how these events occur during HIV production in macrophages. In these cells, virus assembly appears to occur on a pre-existing specialized plasma membrane domain that is sequestered within the cells. The events that take place at these intracellular assembly sites may endow the virus with unique biochemical characteristics and allow virus release to be co-ordinated through the formation of infectious synapses.

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Section: Advantages Of Intracellular Virus Assemblymentioning

confidence: 99%

HIV assembly and budding in macrophages

Marsh

Theusner

Pelchen–Matthews

2009

Biochemical Society Transactions

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“…TEM has been used to study the generation of new virions, providing particularly striking images of viral factories for several virus families (Novoa et al, 2005) (Figure 4). TEM has also proved important for the characterization of morphological features at various stages in the assembly of viral particles, including the acquisition of lipid membranes by enveloped viruses, and for distinguishing between immature and mature particles (Hourioux et al, 2000;Pelchen-Matthews and Marsh, 2007) ( Figure 5). However, the recent development of new imaging techniques for light microscopy has progressively limited the use of TEM for studies of viruscell interactions.…”

Section: Study Of Virus-host Cell Interactionsmentioning

confidence: 99%

Viral detection by electron microscopy: past, present and future

Roingeard

2008

Biology of the Cell

109

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Viruses are very small and most of them can be seen only by TEM (transmission electron microscopy). TEM has therefore made a major contribution to virology, including the discovery of many viruses, the diagnosis of various viral infections and fundamental investigations of virus—host cell interactions. However, TEM has gradually been replaced by more sensitive methods, such as the PCR. In research, new imaging techniques for fluorescence light microscopy have supplanted TEM, making it possible to study live cells and dynamic interactions between viruses and the cellular machinery. Nevertheless, TEM remains essential for certain aspects of virology. It is very useful for the initial identification of unknown viral agents in particular outbreaks, and is recommended by regulatory agencies for investigation of the viral safety of biological products and/or the cells used to produce them. In research, only TEM has a resolution sufficiently high for discrimination between aggregated viral proteins and structured viral particles. Recent examples of different viral assembly models illustrate the value of TEM for improving our understanding of virus—cell interactions.

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“…In macrophages, for instance, assembling VLPs have often been viewed in what appears to be internal endosomal vesicles. 10,11 However, recent studies have demonstrated that these vesicles are, in fact, elaborate membrane invaginations that are continuous with the plasma membrane. 12,13 In contrast to HIV-1, betaretroviruses such as Mason-Pfizer monkey virus (MPMV) assemble in the apparent absence of membrane near the microtubule organizing center before trafficking to and budding through the plasma membrane.…”

Section: Introductionmentioning

confidence: 99%

Mechanisms for Env Glycoprotein Acquisition by Retroviruses

Johnson

2011

AIDS Research and Human Retroviruses

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A mandatory step in the formation of an infectious retroviral particle is the acquisition of its envelope glycoprotein (Env). This step invariably occurs by Env positioning itself in the host membrane at the location of viral budding and being incorporated along with the host membrane into the viral particle. In some ways, this step of the viral life cycle would appear to be imprecise. There is no specific sequence in Env or in the retroviral structural protein, Gag, that is inherently required for the production of an infectious Env-containing particle. Additionally, Env-defective proviruses can efficiently produce infectious particles with any of a number of foreign retroviral Env glycoproteins or even glycoproteins from unrelated viral families, a process termed pseudotyping. However, mounting evidence suggests that Env incorporation is neither passive nor random. Rather, several redundant mechanisms appear to contribute to the carefully controlled process of Env acquisition, many of which are apparently used by a wide variety of enveloped viruses. This review presents and discusses the evidence for these different mechanisms contributing to incorporation.

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Electron Microscopy Analysis of Viral Morphogenesis

Cited by 19 publications

References 69 publications

HIV assembly and budding in macrophages

HIV assembly and budding in macrophages

Viral detection by electron microscopy: past, present and future

Mechanisms for Env Glycoprotein Acquisition by Retroviruses

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