Characterization of E3/49K, a Novel, Highly Glycosylated E3 Protein of the Epidemic Keratoconjunctivitis-Causing Adenovirus Type 19a

Windheim, Mark; Burgert, Hans‐Gerhard

doi:10.1128/jvi.76.2.755-766.2002

Cited by 31 publications

(52 citation statements)

References 66 publications

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“…While monitoring the processing of E3/49K, we previously noted the emergence of 10-to 13-kDa C-terminal fragments (24). Whether the protein is further degraded or the putative large N-terminal cleavage fragment is secreted remained unclear, however.…”

Section: Resultsmentioning

confidence: 99%

“…E3/49K is a highly glycosylated type I transmembrane protein migrating with an apparent molecular weight (m r ) of 80-100 kDa and as such is by far the largest E3 protein. It is localized in the Golgi/ trans-Golgi network, in early endosomes, and in the late phase of infection in lysosomes as well (24).…”

mentioning

confidence: 99%

“…Overall, E3 represents one of the most divergent regions of Ads (20,21). Although some E3 proteins of species B, D, and E have been characterized biochemically (3,(22)(23)(24), no immunomodulatory function has been assigned to E3 proteins of Ads other than species C or to species-specific E3 proteins.…”

mentioning

confidence: 99%

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A unique secreted adenovirus E3 protein binds to the leukocyte common antigen CD45 and modulates leukocyte functions

Windheim

Southcombe

Kremmer

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Significance Human adenoviruses encode Early region 3 (E3) proteins that manipulate the host immune response to establish an infection or to persist longer. To date, only a few E3 functions from a single adenovirus species (C) have been characterized, all of which act directly on infected cells. Here we describe a secreted E3 protein that is uniquely expressed by species D adenoviruses. This protein targets noninfected leukocytes using a cell surface phosphatase as a receptor. We provide evidence that this interaction suppresses leukocyte activation and effector functions, implying that species D adenoviruses can affect the host distant from the site of infection.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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A unique secreted adenovirus E3 protein binds to the leukocyte common antigen CD45 and modulates leukocyte functions

Windheim

Southcombe

Kremmer

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…Confocal Immunofluorescence Microscopy-Cells were processed for immunofluorescence as described (52).…”

Section: Methodsmentioning

confidence: 99%

Two Distinct Transport Motifs in the Adenovirus E3/10.4-14.5 Proteins Act in Concert to Down-modulate Apoptosis Receptors and the Epidermal Growth Factor Receptor

Hilgendorf

Lindberg

Ruzsics

et al. 2003

Journal of Biological Chemistry

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“…In particular, the effects of N-and O-linked glycosylation on viral-host cell interactions have been studied, focusing predominantly on the glycosylated viral coat proteins of enveloped viruses or viruses utilizing sialic acid as a receptor (7,12,22,23,29). Adenovirus (Ad) is a nonenveloped virus that has been reported to contain glycosylated proteins (15,30,31) including a mono-GlcNac addition to the fiber knob protein (6). The effect of this glycosylation on Ad infection is unclear.…”

mentioning

confidence: 99%

Functional Effects of Coxsackievirus and Adenovirus Receptor Glycosylation on Homophilic Adhesion and Adenoviral Infection

Excoffon

Gansemer

Traver

et al. 2007

J Virol

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The coxsackievirus and adenovirus receptor (CAR) is both a viral receptor and homophilic adhesion protein.The extracellular portion of CAR consists of two immunoglobulin (Ig)-like domains, each with a consensus sequence for N-glycosylation. We used chemical, genetic, and biochemical studies to show that both sites are glycosylated and contribute to the function of CAR. Although the glycosylation of CAR does not alter cell surface levels or junctional localization, it affects both adhesion and adenovirus infection in unique ways. CAR-mediated adhesion appears to require at least one site of glycosylation since cells expressing CAR without glycosylation do not cluster with each other. In contrast, glycosylation of the Ig-like domain proximal to the membrane is key to the cooperative behavior of adenovirus binding and infection. Contrary to the hypothesis that cooperativity improves viral infection, our data show that although glycosylation of the D2 domain is required for adenovirus cooperative binding, it has a negative consequence upon infection. This is the first report dissecting the adhesion and receptor activities of CAR, revealing that factors other than the binding interface play a significant role in the function of CAR. These data have important implications for both cancers with altered glycosylation states and cancer treatments using oncolytic adenovirus.

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Characterization of E3/49K, a Novel, Highly Glycosylated E3 Protein of the Epidemic Keratoconjunctivitis-Causing Adenovirus Type 19a

Cited by 31 publications

References 66 publications

A unique secreted adenovirus E3 protein binds to the leukocyte common antigen CD45 and modulates leukocyte functions

A unique secreted adenovirus E3 protein binds to the leukocyte common antigen CD45 and modulates leukocyte functions

Two Distinct Transport Motifs in the Adenovirus E3/10.4-14.5 Proteins Act in Concert to Down-modulate Apoptosis Receptors and the Epidermal Growth Factor Receptor

Functional Effects of Coxsackievirus and Adenovirus Receptor Glycosylation on Homophilic Adhesion and Adenoviral Infection

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