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Book: Agriculture in the Malaysian region

Hill, Ronald D.

2012

Author's details	R. D. Hill
Language	English
Size	XXI, 347 S. : Ill., graph. Darst., Kt.
Edition	2. ed.
Publisher	NUS Press
Publishing place	Singapore
Publishing country	Singapore
Document type	Book
Note	originally publ. by Akadémiai Kiadó, Budapest in 1982 ; the author has updated the original text while retaining the original framework of analysis ...
HBZ-ID	HT017364358
ISBN	978-9971-69-601-6 ; 9971-69-601-0
Database	Catalogue ZB MED Nutrition, Environment, Agriculture

In stock of ZB MED Bonn / Germany

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138/538	available for loan (reading room)	Freihandmagazin (U1)

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Article: A human papillomavirus 16 E2-TopBP1 dependent SIRT1-p300 acetylation switch regulates mitotic viral and human protein levels.

Prabhakar, Apurva T / James, Claire D / Youssef, Aya H / Hossain, Reafa A / Hill, Ronald D / Bristol, Molly L / Wang, Xu / Dubey, Aanchal / Morgan, Iain M

bioRxiv : the preprint server for biology

2024

Abstract: An interaction between human papillomavirus 16 (HPV16) E2 and the cellular proteins TopBP1 and BRD4 is required for E2 plasmid segregation function. The E2-TopBP1 interaction promotes increased mitotic E2 protein levels in U2OS and N/Tert-1 cells, as ... ...

Abstract	An interaction between human papillomavirus 16 (HPV16) E2 and the cellular proteins TopBP1 and BRD4 is required for E2 plasmid segregation function. The E2-TopBP1 interaction promotes increased mitotic E2 protein levels in U2OS and N/Tert-1 cells, as well as in human foreskin keratinocytes immortalized by HPV16 (HFK+HPV16). SIRT1 deacetylation reduces E2 protein stability and here we demonstrate that increased E2 acetylation occurs during mitosis in a TopBP1 interacting dependent manner, promoting E2 mitotic stabilization. p300 mediates E2 acetylation and acetylation is increased due to E2 switching off SIRT1 function during mitosis in a TopBP1 interacting dependent manner, confirmed by increased p53 stability and acetylation on lysine 382, a known target for SIRT1 deacetylation. SIRT1 can complex with E2 in growing cells but is unable to do so during mitosis due to the E2-TopBP1 interaction; SIRT1 is also unable to complex with p53 in mitotic E2 wild type cells but can complex with p53 outside of mitosis. E2 lysines 111 and 112 are highly conserved residues across all E2 proteins and we demonstrate that K111 hyper-acetylation occurs during mitosis, promoting E2 interaction with Topoisomerase 1 (Top1). We also demonstrate that K112 ubiquitination promotes E2 proteasomal degradation during mitosis. The results present a model in which the E2-TopBP1 complex inactivates SIRT1 during mitosis and E2 acetylation on K111 by p300 increases, promoting interaction with Top1 that protects K112 from ubiquitination and therefore E2 proteasomal degradation. Importance: Human papillomaviruses are causative agents in around 5% of all human cancers. While there are prophylactic vaccines that will significantly alleviate HPV disease burden on future generations, there are currently no anti-viral strategies available for the treatment of HPV cancers. To generate such reagents, we must understand more about the HPV life cycle, and in particular about viral-host interactions. Here we describe a novel mitotic complex generated by the HPV16 E2 protein interacting with the host protein TopBP1 that controls the function of the deacetylase SIRT1. The E2-TopBP1 interaction disrupts SIRT1 function during mitosis in order to enhance acetylation and stability of viral and host proteins. This novel complex is essential for the HPV16 life cycle and represents a novel anti-viral therapeutic target.
Language	English
Publishing date	2024-01-16
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.01.15.575713
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Human papillomavirus 16 E2 interaction with TopBP1 is required for E2 and viral genome stability during the viral life cycle.

Prabhakar, Apurva T / James, Claire D / Fontan, Christian T / Otoa, Raymonde / Wang, Xu / Bristol, Molly L / Hill, Ronald D / Dubey, Aanchal / Morgan, Iain M

bioRxiv : the preprint server for biology

2023

Abstract: CK2 phosphorylation of HPV16 E2 at serine 23 promotes interaction with TopBP1, and this interaction is important for E2 plasmid segregation function. Here we demonstrate that the E2-TopBP1 interaction is critical for E2 and viral genome stability during ... ...

Abstract	CK2 phosphorylation of HPV16 E2 at serine 23 promotes interaction with TopBP1, and this interaction is important for E2 plasmid segregation function. Here we demonstrate that the E2-TopBP1 interaction is critical for E2 and viral genome stability during the viral life cycle. Introduction of the S23A mutation into the HPV16 genome results in a loss of E2 expression and viral genome integration during organotypic rafting. Co-culture of N/Tert-1+E2-S23A cells with J2 fibroblasts results in E2-S23A degradation via the proteasome, wild-type E2 is not degraded. TopBP1 siRNA treatment of N/Tert-1+E2-WT cells results in E2 degradation only in the presence of J2 cells demonstrating the critical role for TopBP1 in maintaining E2 stability. The CK2 inhibitor CX4945 promotes E2-WT degradation in the presence of fibroblasts as it disrupts E2-TopBP1 interaction. siRNA targeting SIRT1 rescues E2-S23A stability in N/Tert-1 cells treated with J2 fibroblasts, with an increased E2-S23A acetylation. The results demonstrate that the E2-TopBP1 interaction is critical during the viral life cycle as it prevents fibroblast stimulated SIRT1 mediated deacetylation of E2 that promotes protein degradation. This means that the E2-TopBP1 complex maintains E2 and viral genome stability and that disruption of this complex can promote viral genome integration. Finally, we demonstrate that HPV11 E2 also interacts with TopBP1 and that this interaction is critical for HPV11 E2 stability in the presence of J2 cells. Treatment of N/Tert-1+11E2-WT cells with CX4945 results in 11E2 degradation. Therefore, CK2 inhibition is a therapeutic strategy for alleviating HPV11 diseases, including juvenile respiratory papillomatosis. Importance: Human papillomaviruses are pathogens that cause a host of diseases ranging from benign warts to cancers. There are no therapeutics available for combating these diseases that directly target viral proteins or processes, therefore we must enhance our understanding of HPV life cycles to assist with identifying novel treatments. In this report, we demonstrate that HPV16 and HPV11 E2 protein expression is dependent upon TopBP1 interaction in keratinocytes interacting with fibroblasts, which recapitulate stromal interactions in culture. The degradation of 16E2 promotes HPV16 genome integration, therefore the E2-TopBP1 interaction is critical during the viral life cycle. We demonstrate that the CK2 inhibitor CX4945 disrupts HPV11 interaction with TopBP1 and destabilizes HPV11 E2 protein in the presence of J2 fibroblasts; we propose that CX4945 could alleviate HPV11 disease burden.
Language	English
Publishing date	2023-01-13
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.01.11.523702
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Direct interaction with the BRD4 carboxyl-terminal motif (CTM) and TopBP1 is required for human papillomavirus 16 E2 association with mitotic chromatin and plasmid segregation function.

Prabhakar, Apurva T / James, Claire D / Fontan, Christian T / Otoa, Raymonde / Wang, Xu / Bristol, Molly L / Hill, Ronald D / Dubey, Aanchal / Wu, Shwu-Yuan / Chiang, Cheng-Ming / Morgan, Iain M

bioRxiv : the preprint server for biology

2023

Abstract: During the human papillomavirus 16 life cycle, the E2 protein binds simultaneously to the viral genome and host chromatin throughout mitosis, ensuring viral genomes reside in daughter cell nuclei following cell division. Previously, we demonstrated that ... ...

Abstract	During the human papillomavirus 16 life cycle, the E2 protein binds simultaneously to the viral genome and host chromatin throughout mitosis, ensuring viral genomes reside in daughter cell nuclei following cell division. Previously, we demonstrated that CK2 phosphorylation of E2 on serine 23 promotes interaction with TopBP1, and that this interaction is required for optimum E2 mitotic chromatin association and plasmid segregation function. Others have implicated BRD4 in mediating the plasmid segregation function of E2 and we have demonstrated that there is a TopBP1-BRD4 complex in the cell. We therefore further investigated the role of the E2-BRD4 interaction in mediating E2 association with mitotic chromatin and plasmid segregation function. Using a combination of immunofluorescence and our novel plasmid segregation assay in U2OS and N/Tert-1 cells stably expressing a variety of E2 mutants, we report that direct interaction with the BRD4 carboxyl-terminal motif (CTM) and TopBP1 is required for E2 association with mitotic chromatin and plasmid segregation. We also identify a novel TopBP1 mediated interaction between E2 and the BRD4 extra-terminal (ET) domain Importance: HPV16 is a causative agent in around 3-4% of all human cancers and currently there are no anti-viral therapeutics available for combating this disease burden. In order to identify new therapeutic targets, we must increase our understanding of the HPV16 life cycle. Previously, we demonstrated that an interaction between E2 and the cellular protein TopBP1 mediates the plasmid segregation function of E2, allowing distribution of viral genomes into daughter nuclei following cell division. Here, we demonstrate that E2 interaction with an additional host protein, BRD4, is also essential for E2 segregation function, and that BRD4 exists in a complex with TopBP1. Overall, these results enhance our understanding of a critical part of the HPV16 life cycle and presents several therapeutic targets for disruption of the viral life cycle.
Language	English
Publishing date	2023-05-26
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.05.25.542291
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Human Papillomavirus 16 E2 Interaction with TopBP1 Is Required for E2 and Viral Genome Stability during the Viral Life Cycle.

Prabhakar, Apurva T / James, Claire D / Fontan, Christian T / Otoa, Raymonde / Wang, Xu / Bristol, Molly L / Hill, Ronald D / Dubey, Aanchal / Morgan, Iain M

Journal of virology

2023 Volume 97, Issue 3, Page(s) e0006323

Abstract: CK2 phosphorylation of HPV16 E2 at serine 23 promotes interaction with TopBP1, and this interaction is important for E2 plasmid segregation function. Here, we demonstrate that the E2-TopBP1 interaction is critical for E2 and viral genome stability during ...

Abstract	CK2 phosphorylation of HPV16 E2 at serine 23 promotes interaction with TopBP1, and this interaction is important for E2 plasmid segregation function. Here, we demonstrate that the E2-TopBP1 interaction is critical for E2 and viral genome stability during the viral life cycle. Introduction of the S23A mutation into the HPV16 genome results in a loss of E2 expression and viral genome integration during organotypic rafting. Coculture of N/Tert-1+E2-S23A cells with J2 fibroblasts results in E2-S23A degradation via the proteasome; wild-type E2 is not degraded. TopBP1 siRNA treatment of N/Tert-1+E2-WT cells results in E2 degradation only in the presence of J2 cells demonstrating the critical role for TopBP1 in maintaining E2 stability. The CK2 inhibitor CX4945 promotes E2-WT degradation in the presence of fibroblasts as it disrupts E2-TopBP1 interaction. siRNA targeting SIRT1 rescues E2-S23A stability in N/Tert-1 cells treated with J2 fibroblasts, with an increased E2-S23A acetylation. The results demonstrate that the E2-TopBP1 interaction is critical during the viral life cycle as it prevents fibroblast stimulated SIRT1 mediated deacetylation of E2 that promotes protein degradation. This means that the E2-TopBP1 complex maintains E2 and viral genome stability and that disruption of this complex can promote viral genome integration. Finally, we demonstrate that HPV11 E2 also interacts with TopBP1 and that this interaction is critical for HPV11 E2 stability in the presence of J2 cells. Treatment of N/Tert-1 + 11E2-WT cells with CX4945 results in 11E2 degradation. Therefore, CK2 inhibition is a therapeutic strategy for alleviating HPV11 diseases, including juvenile respiratory papillomatosis.
MeSH term(s)	Humans ; Carrier Proteins/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Genome, Viral ; Genomic Instability ; Human papillomavirus 16/metabolism ; Human Papillomavirus Viruses ; Nuclear Proteins/metabolism ; Oncogene Proteins, Viral/genetics ; Oncogene Proteins, Viral/metabolism ; Sirtuin 1/metabolism
Chemical Substances	Carrier Proteins ; DNA-Binding Proteins ; Nuclear Proteins ; Oncogene Proteins, Viral ; Sirtuin 1 (EC 3.5.1.-) ; TOPBP1 protein, human ; E2 protein, Human papillomavirus type 16
Language	English
Publishing date	2023-02-22
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.00063-23
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 609: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Direct interaction with the BRD4 carboxyl-terminal motif (CTM) and TopBP1 is required for human papillomavirus 16 E2 association with mitotic chromatin and plasmid segregation function.

Prabhakar, Apurva T / James, Claire D / Fontan, Christian T / Otoa, Raymonde / Wang, Xu / Bristol, Molly L / Yeager, Calvin / Hill, Ronald D / Dubey, Aanchal / Wu, Shwu-Yuan / Chiang, Cheng-Ming / Morgan, Iain M

Journal of virology

2023 Volume 97, Issue 10, Page(s) e0078223

Abstract: Importance: Human papillomavirus 16 (HPV16) is a causative agent in around 3%-4% of all human cancers, and currently, there are no anti-viral therapeutics available for combating this disease burden. In order to identify new therapeutic targets, we must ...

Abstract	Importance: Human papillomavirus 16 (HPV16) is a causative agent in around 3%-4% of all human cancers, and currently, there are no anti-viral therapeutics available for combating this disease burden. In order to identify new therapeutic targets, we must increase our understanding of the HPV16 life cycle. Previously, we demonstrated that an interaction between E2 and the cellular protein TopBP1 mediates the plasmid segregation function of E2, allowing distribution of viral genomes into daughter nuclei following cell division. Here, we demonstrate that E2 interaction with an additional host protein, BRD4, is also essential for E2 segregation function, and that BRD4 exists in a complex with TopBP1. Overall, these results enhance our understanding of a critical part of the HPV16 life cycle and presents several therapeutic targets for disruption of the viral life cycle.
MeSH term(s)	Humans ; Bromodomain Containing Proteins ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Chromatin/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Human papillomavirus 16/genetics ; Human papillomavirus 16/metabolism ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Oncogene Proteins, Viral/genetics ; Oncogene Proteins, Viral/metabolism ; Plasmids/genetics ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	BRD4 protein, human ; Bromodomain Containing Proteins ; Cell Cycle Proteins ; Chromatin ; DNA-Binding Proteins ; Nuclear Proteins ; Oncogene Proteins, Viral ; Transcription Factors ; E2 protein, Human papillomavirus type 16 ; TOPBP1 protein, human
Language	English
Publishing date	2023-09-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.00782-23
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 609: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

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Book: Diabetes and primary eye care

Ariffin, A. / Hill, Ronald D. / Leigh, O.

(Modern optometry)

1992

Author's details	A. Ariffin ; R. D. Hill ; O. Leigh
Series title	Modern optometry
Language	English
Size	VII, 207 S. : Ill., graph. Darst.
Publisher	Blackwell
Publishing place	Oxford u.a.
Publishing country	Great Britain
Document type	Book
HBZ-ID	HT004176854
ISBN	0-632-03142-5 ; 978-0-632-03142-9
Database	Catalogue ZB MED Medicine, Health

In stock of ZB MED Cologne/Königswinter

Shelf mark	Loan status	Location
1992 A 1938	order for loan	Magazin

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Book: Agriculture in the Malaysian region

Hill, Ronald D

2012

Author's details	R. D. Hill
Keywords	Agriculture/Economic aspects ; Agriculture/History ; Traditional farming ; Strukturwandel ; Landwirtschaftliche Entwicklung ; Agrarboden ; Landwirtschaft ; Agrargeschichte ; Singapur ; Brunei ; Malaysia
Language	English
Size	XXI, 347 S., Ill., graph. Darst., Kt.
Edition	2. ed.
Publisher	NUS Press
Publishing place	Singapore
Document type	Book
Note	originally publ. in 1982 ; the author has updated the original text while retaining the original framework of analysis ...
ISBN	9789971696016 ; 9971696010
Database	ECONomics Information System

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Book ; Conference proceedings: Fishing in troubled waters

Hill, Ronald D

proceedings of an Academic Conference on Territorial Claims in the South China Sea

(Centre of Asian Studies occasional papers and monographs ; 97)

1991

Institution	Academic Conference on Territorial Claims in the South China Sea
Author's details	ed. by R. D. Hill
Series title	Centre of Asian Studies occasional papers and monographs ; 97
Keywords	Südchinesisches Meer ; Staatsgebiet ; Küstengewässer
Language	English
Size	IX, 359 S, Kt
Publisher	Centre of Asian Studies, Univ. of Hong Kong
Publishing place	Hong Kong
Document type	Book ; Conference proceedings
Database	Former special subject collection: coastal and deep sea fishing

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Book ; Conference proceedings: Fishing in troubled waters

Hill, Ronald D

proceedings of an Academic Conference on Territorial Claims in the South China Sea

(Centre of Asian Studies occasional papers and monographs ; 97)

1991

Institution	Academic Conference on Territorial Claims in the South China Sea
Author's details	ed. by R. D. Hill
Series title	Centre of Asian Studies occasional papers and monographs ; 97
Keywords	Südchinesisches Meer ; Staatsgebiet ; Küstengewässer
Language	English
Size	IX, 359 S, Kt
Publisher	Centre of Asian Studies, Univ. of Hong Kong
Publishing place	Hong Kong
Document type	Book ; Conference proceedings
Database	ECONomics Information System

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