Biogenesis of vaccinia: Evidence for more than 100 polypeptides in the virion

Essani, Karim; Dales, Samuel

doi:10.1016/0042-6822(79)90493-8

Cited by 94 publications

(42 citation statements)

References 24 publications

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“…Our rabbit and mouse immune sera against viral envelopes also had neutralizing potency and bound to the 54K, 32K, 30K and 21K proteins but not in the same way as the MAbs to the 16K and 14K envelope proteins. Proteins at 87K, 73K, 67K, 61K and 57K were found only in the core corresponding to the major core proteins described by Essani & Dales (1979) and Oie & Ichihashi (1981). Additionally, three proteins at 32K, 30K and 14K were found; the latter may be identical to a 13.8K core protein (Ichihashi et al, 1982), but it is well known that incubation of vaccinia virus with detergents does not completely remove tubules from the cores (Mbuy et al, 1982) which would result in tubule-specific antibodies after immunization with such a preparation.…”

Section: Discussionmentioning

confidence: 99%

Structural and functional analysis of orthopoxvirus epitopes with neutralizing monoclonal antibodies

Czerny¹,

Mahnel²

1990

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

Structural and functional analysis of orthopoxvirus epitopes with neutralizing monoclonal antibodies

Czerny¹,

Mahnel²

1990

Journal of General Virology

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“…As the prototypical and best-characterized member of the poxvirus family, VACV was the focus of most of these attempts. Early studies attempted to analyze the protein composition of purified VACV MVs utilizing mainly sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under different electrophoretic conditions (54,100,120,121,140). However, the early nomenclature for the proteins identified in these studies was based on their electrophoretic migration on SDS-PAGE gels, which made it difficult to compare results between different studies.…”

Section: Proteomic Studies Of Poxvirus Virionsmentioning

confidence: 99%

Poxvirus Proteomics and Virus-Host Protein Interactions

Vliet

Mohamed

Zhang

et al. 2009

Microbiol Mol Biol Rev

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SUMMARY Studies of the functional proteins encoded by the poxvirus genome provide information about the composition of the virus as well as individual virus-virus protein and virus-host protein interactions, which provides insight into viral pathogenesis and drug discovery. Widely used proteomic techniques to identify and characterize specific protein-protein interactions include yeast two-hybrid studies and coimmunoprecipitations. Recently, various mass spectrometry techniques have been employed to identify viral protein components of larger complexes. These methods, combined with structural studies, can provide new information about the putative functions of viral proteins as well as insights into virus-host interaction dynamics. For viral proteins of unknown function, identification of either viral or host binding partners provides clues about their putative function. In this review, we discuss poxvirus proteomics, including the use of proteomic methodologies to identify viral components and virus-host protein interactions. High-throughput global protein expression studies using protein chip technology as well as new methods for validating putative protein-protein interactions are also discussed.

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“…Like all poxviruses, the VV particle is large and complex, and more than 100 polypeptides have been identified in the purified virion (15). The virus genome encodes approximately 200 genes and has been sequenced for VV strains Copenhagen (18), modified virus Ankara (2), and most of the Western Reserve (WR) strain (see reference 46 for additional references).…”

mentioning

confidence: 99%

Vaccinia Virus F12L Protein Is Required for Actin Tail Formation, Normal Plaque Size, and Virulence

Zhang

Wilcock

Smith

2000

J Virol

109

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Vaccinia virus gene F12L is shown to encode a 65-kDa protein that is synthesized early and late during infection and that is not modified by glycosylation. Computational sequence comparison revealed that related proteins are encoded by all sequenced chordopoxviruses. A virus deletion mutant lacking the F12L gene (v⌬F12L) and a revertant virus with the F12L gene reinserted into the deletion mutant (vF12L-rev) were constructed and analyzed. A version of the F12L gene with a C-terminal amino acid tag derived from the influenza virus hemagglutinin and that is recognized by a monoclonal antibody was also inserted into the F12L locus of v⌬F12L. Loss of the F12L protein reduced the formation of IMV 2-fold, but there was a dramatic (99.5%) reduction in actin tail formation, and the levels of cell-associated enveloped virus and extracellular enveloped virus were reduced 8-to 11-fold and 7-fold, respectively. Consistent with the lack of actin tail formation, v⌬F12L produced a very small plaque. The v⌬F12L virus was severely attenuated in vivo, such that a dose of v⌬F12L 10,000-fold greater than the dose of wild-type virus that induced severe disease was unable to induce disease in mice infected intranasally.

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Biogenesis of vaccinia: Evidence for more than 100 polypeptides in the virion

Cited by 94 publications

References 24 publications

Structural and functional analysis of orthopoxvirus epitopes with neutralizing monoclonal antibodies

Structural and functional analysis of orthopoxvirus epitopes with neutralizing monoclonal antibodies

Poxvirus Proteomics and Virus-Host Protein Interactions

Vaccinia Virus F12L Protein Is Required for Actin Tail Formation, Normal Plaque Size, and Virulence

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