Characterization of vaccinia virus glycoproteins by monoclonal antibody precipitation

Payne, Lendon G.

doi:10.1016/0042-6822(92)90313-e

Cited by 64 publications

(93 citation statements)

References 28 publications

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“…While MV is susceptible to neutralization by complement (14,42), EV is relatively resistant due to the incorporation of host cell-derived complement-regulatory proteins into the EV outer envelope (42). Since A56 is incorporated into the EV envelope (29,30) and is not found on MV, it raises the possibility that VCP is also displayed on EV. If VCP is present on EV, this may provide additional protection against complement-mediated neutralization.…”

Section: Discussionmentioning

confidence: 99%

Cell Surface Expression of the Vaccinia Virus Complement Control Protein Is Mediated by Interaction with the Viral A56 Protein and Protects Infected Cells from Complement Attack

Girgis

DeHaven

Fan

et al. 2008

J Virol

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The vaccinia virus (VACV) complement control protein (VCP) is the major protein secreted from VACVinfected cells. It has been reported that VCP binds to the surfaces of uninfected cells by interacting with heparan sulfate proteoglycans (HSPGs). In this study, we show that VCP is also expressed on the surfaces of infected cells and demonstrate that surface localization occurs independently of HSPGs. Since VCP does not contain a transmembrane domain, we hypothesized that VCP interacts with a membrane protein that localizes to the infected-cell surface. We show that the VACV A56 membrane protein is necessary for the cell surface expression of VCP and demonstrate that VCP and A56 interact in VACV-infected cells. Since the surface expression of VCP was abrogated by reducing agents, we examined the contribution of an unpaired cysteine residue on VCP to VCP surface expression and VCP's interaction with A56. To do this, we mutated the unpaired cysteine in VCP and generated a recombinant virus expressing the altered form of VCP. Following the infection of cells with the mutant virus, VCP was neither expressed on the cell surface nor able to interact with A56. Importantly, the cell surface expression of VCP was found to protect infected cells from complementmediated lysis. Our findings suggest a new function for VCP that may be important for poxvirus pathogenesis and impact immune responses to VACV-based vaccines.The complement system is composed of ϳ30 soluble and cell surface proteins that work in concert to protect the host from invading pathogens (reviewed in references 46 and 47). Complement can become activated by multiple pathways that converge on the formation of a C3 convertase, the proteolytic complex responsible for cleaving the central complement component, C3. Cleavage of C3 results in the production of the anaphylatoxin C3a and the opsonic fragment C3b. The generation of C3b results in the formation of a C5 convertase, the proteolytic complex responsible for cleaving C5 into the C5a anaphylatoxin and C5b. C5b, in turn, nucleates the formation of a lytic pore called the membrane attack complex.

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Section: Discussionmentioning

confidence: 99%

Cell Surface Expression of the Vaccinia Virus Complement Control Protein Is Mediated by Interaction with the Viral A56 Protein and Protects Infected Cells from Complement Attack

Girgis

DeHaven

Fan

et al. 2008

J Virol

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“…The N135 site is in the connecting region between the ␣1 and ␣2 helices. Gel electrophoresis mobility differences after enzymatic deglycosylation of A33 and after virus growth in the presence of glycosylation inhibitors indicate that the N-linked sites are used in vaccinia virus (57). Variola virus and monkeypox virus A33 orthologs lack the N125 site, despite their 95% sequence identity with vaccinia virus A33.…”

Section: Fig 1 A33 Contains a Dimer Of C-type Lectin-like Domains (mentioning

confidence: 99%

“…1). The other cysteine, C36, is predicted to be inside the membrane and to be palmitoylated (21,57) (Fig. 1).…”

Section: Fig 1 A33 Contains a Dimer Of C-type Lectin-like Domains (mentioning

confidence: 99%

“…Several monoclonal antibodies (MAb) that bind to the ectodomain of A33 have been described (8,27,57). The MAbs 4, 66, and 105 precipitate A33 molecules from vaccinia virus EV in the range of 23 to 28 kDa, which was shown to result from the several glycosylation states of A33 (57). Although MAb 4 recognizes similarly sized proteins (A33 orthologs) in several other orthopoxviruses, MAb 4 does not bind to ectromelia virus proteins (62).…”

Section: A33 Dimer Of Ctlds Resembles Dimeric Ctlds Of Natural Killermentioning

confidence: 99%

“…A33 is a disulfide-bonded homodimer with both N-and O-linked glycosylation (57,62). Deletion of the A33R gene in vaccinia virus results in a smallplaque phenotype, defects in actin tail formation, and inefficient cell-to-cell spread in cell culture (63).…”

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confidence: 99%

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The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains

Singh

Gittis

et al. 2010

J Virol

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The current vaccine against smallpox is an infectious form of vaccinia virus that has significant side effects. Alternative vaccine approaches using recombinant viral proteins are being developed. A target of subunit vaccine strategies is the poxvirus protein A33, a conserved protein in the Chordopoxvirinae subfamily of Poxviridae that is expressed on the outer viral envelope. Here we have determined the structure of the A33 ectodomain of vaccinia virus. The structure revealed C-type lectin-like domains (

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Detection of Surrogate Cells Presenting Vaccinia Virus Protein by DNA Aptamers

Choi

Park

Hong

et al. 2016

Bulletin Korean Chem Soc

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Characterization of vaccinia virus glycoproteins by monoclonal antibody precipitation

Cited by 64 publications

References 28 publications

Cell Surface Expression of the Vaccinia Virus Complement Control Protein Is Mediated by Interaction with the Viral A56 Protein and Protects Infected Cells from Complement Attack

Cell Surface Expression of the Vaccinia Virus Complement Control Protein Is Mediated by Interaction with the Viral A56 Protein and Protects Infected Cells from Complement Attack

The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains

Detection of Surrogate Cells Presenting Vaccinia Virus Protein by DNA Aptamers

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