[26] Eukaryotic cloning vectors derived from bovine papillomavirus DNA

Author(s):  
Peter M. Howley ◽  
Nava Sarver ◽  
Ming-Fan Law
1992 ◽  
Vol 64 (1) ◽  
pp. 83-90 ◽  
Author(s):  
Linda Anne Kowalski ◽  
Su-Sing Tsang ◽  
Allan J. Davison

1983 ◽  
Vol 3 (6) ◽  
pp. 1032-1039
Author(s):  
Y Wang ◽  
C Stratowa ◽  
M Schaefer-Ridder ◽  
J Doehmer ◽  
P H Hofschneider

We have constructed a recombinant pBR322 plasmid composed of a subgenomic transforming fragment of bovine papillomavirus DNA and the hepatitis B surface antigen gene from cloned hepatitis B virus DNA and used it for transfection of NIH 3T3 mouse fibroblasts. The transformed cells retain the plasmids in extrachromosomal form with a copy number of about 50 to 100 per cell. Expression of the hepatitis B surface antigen gene linked to bovine papillomavirus DNA is independent of its orientation relative to the bovine papillomavirus vector. Cell lines continuously secreting high amounts of hepatitis B surface antigen into the medium could be established. The antigen is released into the culture medium as 22-nm particles, having the same physical properties and constituent polypeptides as those found in the serum of hepatitis B virus-infected patients.


Author(s):  
E. Van Dyk ◽  
A-M Bosman ◽  
E. Van Wilpe ◽  
J. H. Williams ◽  
R. G. Bengis ◽  
...  

Papillomavirus was detected electron microscopically in cutaneous fibropapillomas of a giraffe (Giraffa camelopardalis) and a sable antelope (Hippotragus niger). The virus particles measured 45 nm in diameter. Histopathologically, the lesions showed histopathological features similar to those of equine sarcoid as well as positive immunoperoxidase-staining of tissue sections for papillomavirus antigen. Polymerase chain reaction (PCR) detected bovine papillomavirus (BPV) DNA. Bovine papillomavirus-1 was characterised by real-time PCR in the sable and giraffe, and cloning and sequencing of the PCR product revealed a similarity to BPV-1. As in the 1st giraffe, the lesions from a 2nd giraffe revealed locally malignant pleomorphism, possibly indicating the lesional end-point of papilloma infection. Neither virus particles nor positively staining papillomavirus antigen could be demonstrated in the 2nd giraffe but papillomavirus DNA was detected by real-time PCR which corresponded with BPV-1 and BPV-2.


2010 ◽  
Vol 146 (3-4) ◽  
pp. 269-275 ◽  
Author(s):  
Lies Bogaert ◽  
Ann Martens ◽  
Wijbe Martin Kast ◽  
Eric Van Marck ◽  
Hilde De Cock

2010 ◽  
Vol 42 (4) ◽  
pp. 327-331 ◽  
Author(s):  
R. HARALAMBUS ◽  
J. BURGSTALLER ◽  
J. KLUKOWSKA-RÖTZLER ◽  
R. STEINBORN ◽  
S. BUCHINGER ◽  
...  

2006 ◽  
Vol 80 (9) ◽  
pp. 4363-4371 ◽  
Author(s):  
Yan Hu ◽  
Randolph V. Clower ◽  
Thomas Melendy

ABSTRACT In addition to viral proteins E1 and E2, bovine papillomavirus type 1 (BPV1) depends heavily on host replication machinery for genome duplication. It was previously shown that E1 binds to and recruits cellular replication proteins to the BPV1 origin of replication, including DNA polymerase α-primase, replication protein A (RPA), and more recently, human topoisomerase I (Topo I). Here, we show that Topo I specifically stimulates the origin binding of E1 severalfold but has no effect on nonorigin DNA binding. This is highly specific, as binding to nonorigin DNA is not stimulated, and other cellular proteins that bind E1, such as RPA and polymerase α-primase, show no such effect. The stimulation of E1's origin binding by Topo I is not synergistic with the stimulation by E2. Although the enhanced origin binding of E1 by Topo I requires ATP and Mg2+ for optimal efficiency, ATP hydrolysis is not required. Using an enzyme-linked immunosorbent assay, we showed that the interaction between E1 and Topo I is decreased in the presence of DNA. Our results suggest that Topo I participates in the initiation of papillomavirus DNA replication by enhancing E1 binding to the BPV1 origin.


Virology ◽  
1997 ◽  
Vol 228 (1) ◽  
pp. 1-10 ◽  
Author(s):  
THOMAS A ZANARDI ◽  
CHRISTINE M STANLEY ◽  
BRADLEY M SAVILLE ◽  
SUSAN M SPACEK ◽  
MICHAEL R LENTZ

1998 ◽  
Vol 72 (8) ◽  
pp. 6822-6831 ◽  
Author(s):  
Dina Lepik ◽  
Ivar Ilves ◽  
Arnold Kristjuhan ◽  
Toivo Maimets ◽  
Mart Ustav

ABSTRACT p53 protein was able to block human and bovine papillomavirus DNA amplificational replication while not interfering with Epstein-Barr virus oriP once-per-cell cycle replication. Oligomerization, intact DNA-binding, replication protein A-binding, and proline-rich domains of the p53 protein were essential for efficient inhibition, while the N-terminal transcriptional activation and C-terminal regulatory domains were dispensable for the suppressor activity of the p53 protein. The inhibition of replication was caused neither by the downregulation of expression of the E1 and E2 proteins nor by cell cycle block or apoptosis. Our data suggest that the intrinsic activity of p53 to suppress amplificational replication of the papillomavirus origin may have an important role in the virus life cycle and in virus-cell interactions.


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