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Comparison of protein expression during wild-type, and E1B-55k-deletion, adenovirus infection using quantitative time-course proteomics

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Comparison of protein expression during wild-type, and E1B-55k-deletion, adenovirus infection using quantitative time-course proteomics. / Fu, Yen Rong; Turnell, Andrew S; Davis, Simon; Heesom, Kate J; Evans, Vanessa C; Matthews, David A.

In: Journal of General Virology, Vol. 98, No. 6, 20.06.2017, p. 1377-1388.

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Fu, Yen Rong ; Turnell, Andrew S ; Davis, Simon ; Heesom, Kate J ; Evans, Vanessa C ; Matthews, David A. / Comparison of protein expression during wild-type, and E1B-55k-deletion, adenovirus infection using quantitative time-course proteomics. In: Journal of General Virology. 2017 ; Vol. 98, No. 6. pp. 1377-1388.

Bibtex

@article{c5585f744bf84b3582c6edfcdffad5da,
title = "Comparison of protein expression during wild-type, and E1B-55k-deletion, adenovirus infection using quantitative time-course proteomics",
abstract = "Adenovirus has evolved strategies to usurp host-cell factors and machinery to facilitate its life cycle, including cell entry, replication, assembly and egress. Adenovirus continues, therefore, to be an important model system for investigating fundamental cellular processes. The role of adenovirus E1B-55k in targeting host-cell proteins that possess antiviral activity for proteasomal degradation is now well established. To expand our understanding of E1B-55k in regulating the levels of host-cell proteins, we performed comparative proteome analysis of wild-type, and E1B-55k-deletion, adenovirus-infected cancer cells. As such we performed quantitative MS/MS analysis to monitor protein expression changes affected by viral E1B-55k. We identified 5937 proteins, and of these, 69 and 58 proteins were down-regulated during wild-type and E1B-55k (dl1520) adenovirus infection, respectively. This analysis revealed that there are many, previously unidentified, cellular proteins subjected to degradation by adenovirus utilizing pathways independent of E1B-55k expression. Moreover, we found that ALCAM, EPHA2 and PTPRF, three cellular proteins that function in the regulation of cell-cell contacts, appeared to be degraded by E1B-55k/E4orf3 and/or E1B-55k/E4orf6 complexes. These molecules, like integrin α3 (a known substrate of E1B-55k/E4orf6), are critical regulators of cell signalling, cell adhesion and cell surface modulation, and their degradation during infection is, potentially, pertinent to adenovirus propagation. The data presented in this study illustrate the broad nature of protein down-regulation mediated by adenovirus.",
keywords = "Adenoviridae, Adenoviridae Infections, Adenovirus E1B Proteins, Cell Line, Tumor, Gene Deletion, Host-Pathogen Interactions, Humans, Proteome, Proteomics, Tandem Mass Spectrometry, Time Factors, Journal Article",
author = "Fu, {Yen Rong} and Turnell, {Andrew S} and Simon Davis and Heesom, {Kate J} and Evans, {Vanessa C} and Matthews, {David A}",
year = "2017",
month = "6",
day = "20",
doi = "10.1099/jgv.0.000781",
language = "English",
volume = "98",
pages = "1377--1388",
journal = "Journal of General Virology",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "6",

}

RIS - suitable for import to EndNote

TY - JOUR

T1 - Comparison of protein expression during wild-type, and E1B-55k-deletion, adenovirus infection using quantitative time-course proteomics

AU - Fu, Yen Rong

AU - Turnell, Andrew S

AU - Davis, Simon

AU - Heesom, Kate J

AU - Evans, Vanessa C

AU - Matthews, David A

PY - 2017/6/20

Y1 - 2017/6/20

N2 - Adenovirus has evolved strategies to usurp host-cell factors and machinery to facilitate its life cycle, including cell entry, replication, assembly and egress. Adenovirus continues, therefore, to be an important model system for investigating fundamental cellular processes. The role of adenovirus E1B-55k in targeting host-cell proteins that possess antiviral activity for proteasomal degradation is now well established. To expand our understanding of E1B-55k in regulating the levels of host-cell proteins, we performed comparative proteome analysis of wild-type, and E1B-55k-deletion, adenovirus-infected cancer cells. As such we performed quantitative MS/MS analysis to monitor protein expression changes affected by viral E1B-55k. We identified 5937 proteins, and of these, 69 and 58 proteins were down-regulated during wild-type and E1B-55k (dl1520) adenovirus infection, respectively. This analysis revealed that there are many, previously unidentified, cellular proteins subjected to degradation by adenovirus utilizing pathways independent of E1B-55k expression. Moreover, we found that ALCAM, EPHA2 and PTPRF, three cellular proteins that function in the regulation of cell-cell contacts, appeared to be degraded by E1B-55k/E4orf3 and/or E1B-55k/E4orf6 complexes. These molecules, like integrin α3 (a known substrate of E1B-55k/E4orf6), are critical regulators of cell signalling, cell adhesion and cell surface modulation, and their degradation during infection is, potentially, pertinent to adenovirus propagation. The data presented in this study illustrate the broad nature of protein down-regulation mediated by adenovirus.

AB - Adenovirus has evolved strategies to usurp host-cell factors and machinery to facilitate its life cycle, including cell entry, replication, assembly and egress. Adenovirus continues, therefore, to be an important model system for investigating fundamental cellular processes. The role of adenovirus E1B-55k in targeting host-cell proteins that possess antiviral activity for proteasomal degradation is now well established. To expand our understanding of E1B-55k in regulating the levels of host-cell proteins, we performed comparative proteome analysis of wild-type, and E1B-55k-deletion, adenovirus-infected cancer cells. As such we performed quantitative MS/MS analysis to monitor protein expression changes affected by viral E1B-55k. We identified 5937 proteins, and of these, 69 and 58 proteins were down-regulated during wild-type and E1B-55k (dl1520) adenovirus infection, respectively. This analysis revealed that there are many, previously unidentified, cellular proteins subjected to degradation by adenovirus utilizing pathways independent of E1B-55k expression. Moreover, we found that ALCAM, EPHA2 and PTPRF, three cellular proteins that function in the regulation of cell-cell contacts, appeared to be degraded by E1B-55k/E4orf3 and/or E1B-55k/E4orf6 complexes. These molecules, like integrin α3 (a known substrate of E1B-55k/E4orf6), are critical regulators of cell signalling, cell adhesion and cell surface modulation, and their degradation during infection is, potentially, pertinent to adenovirus propagation. The data presented in this study illustrate the broad nature of protein down-regulation mediated by adenovirus.

KW - Adenoviridae

KW - Adenoviridae Infections

KW - Adenovirus E1B Proteins

KW - Cell Line, Tumor

KW - Gene Deletion

KW - Host-Pathogen Interactions

KW - Humans

KW - Proteome

KW - Proteomics

KW - Tandem Mass Spectrometry

KW - Time Factors

KW - Journal Article

U2 - 10.1099/jgv.0.000781

DO - 10.1099/jgv.0.000781

M3 - Article

VL - 98

SP - 1377

EP - 1388

JO - Journal of General Virology

JF - Journal of General Virology

SN - 0022-1317

IS - 6

ER -