Capsid protein VP1 (p85) of aleutian disease virus is a major DNA-binding protein

Willwand, Kurt; Kaaden, Oskar‐Rüger

doi:10.1016/0042-6822(88)90145-6

Cited by 15 publications

(19 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This is suggested by the data that show that MC-ADV g-8 and -15 did not detect VP-1 after tryptic digestion. The hypothesis that VP-1 is embedded in the virion is also supported by the findings of WiUwand and Kaaden [41] and Alexandersen etal. [4] who have shown that VP-1 of intact empty capsids interacts with viral DNA via a unique region of VP-1 resulting in encapsidation of the viral DNA.…”

Section: Discussionsupporting

confidence: 55%

Topographical analysis of the G virion of Aleutian mink disease parvovirus with monoclonal antibodies

Barnard

Johnson

1992

Archives of Virology

View full text Add to dashboard Cite

The topography of the Aleutian mink disease parvovirus (ADV) G virion was analyzed with monoclonal antibodies and polyclonal antiserum. There was homology between the two major structural proteins as others have previously reported. Trypsin treatment of the virion with subsequent immunoblotting revealed that VP2 represents the main peptide on the exterior of virion and that VP1 is probably embedded within the capsid. Additional analyses of the trypsin-treated virions showed that VP2 is responsible for binding complement and that it also represents the structural part of the virion that binds to cellular receptors. A third protein, p34, was detected that might represent a third structural polypeptide because of its many unique epitopes relative to the other peptides detected.

show abstract

Section: Discussionsupporting

confidence: 55%

Topographical analysis of the G virion of Aleutian mink disease parvovirus with monoclonal antibodies

Barnard

Johnson

1992

Archives of Virology

View full text Add to dashboard Cite

show abstract

“…We have previously reported the isolation of ADV from bone marrow cells of a naturally infected mink (VAN DAWEN et al, 1983), subsequently designated ADV SL3 isolate, and its adaptation to cell culture conditions. Although now relatively well defined in vitvo (LOCHELT and KAADEN, 1987;KAADEN et al, 1986;KIEREK-JASZCZUK et al, 1986;WILLWAND and KAADEN, 1988), nothing was known about its in vivo pathogenicity. This prompted us to infect six Aleutian (aa)-genotype violet mink with the ADV SL3 isolate.…”

Section: Introductionmentioning

confidence: 99%

Violet Mink Develop an Acute Disease after Experimental Infection with Aleutian Disease Virus (ADV) Isolate ADV SL3

Haas

Wohlsein

Trautwein

et al. 1990

Journal of Veterinary Medicine, Series B

View full text Add to dashboard Cite

Summary Six‐Aleutian (aa)‐genotype violet mink were infected intraperitoneally with the Aleutian Disease Virus (ADV) bone marrow derived isolate ADV SL3. All animals developed virus‐specific antibodies and hypergammaglobulinaemia. Mortality during the fourteen week duration of the infection was 50%. The virus induced (histo)pathological lesions typical for Aleutian Disease. By immunohistochemical examination using a virus capsid‐specific monoclonal antibody viral antigen was detected in lymph nodes, spleen, kidneys and once in hepatic Kupffer cells. By Southern blot and in situ hybridization studies with strand‐specific RNA probes able to distinguish viral replicative forms from merely sequestered genomic DNA, ADV replication was detected in mesenteric lymph nodes and spleen. In one mink DNA replicative forms were also found in bone marrow cells or mononuclear cells of the peripheral blood, respectively. Only single‐stranded viral DNA was detected in liver, kidney, gut and lung of infected animals. From Southern blot hybridization results a different, possibly organ‐specific permissiveness of ADV in vivo is suggested. Zusammenfassung Akute Erkrankung von Aleuten‐Genotyp‐Nerzen nach experimenteller Infektion mit dem Aleutian Disease Virus (ADV)‐Isolat ADV SL3 Sechs Aleutian(aa)‐Genotyp‐Nerze wurden mit dem Aleutian Disease Virus (ADV)‐Knochen‐markisolat ADV SL3 intraperitoneal infiziert. Alle Tiere serokonvertierten und entwickelten eine Hypergammaglobulinämie. Die Mortalität innerhalb der 14wöchigen Versuchsdauer betrug 50%. Das Virus induzierte Aleutian Disease‐typische (histo)pathologische Alterationen. Aufgrund immunhistochemischer Untersuchungen mit einem Viruskapsid‐spezifischen monoklonalen Antikörper wurde virales Antigen in Lymphknoten, Milz und Nieren, sowie einmal in Kupfferschen Sternzellen der Leber gefunden. Mittels Southern blot‐ und in situ‐Hybridisierungen mit strangspezifischen RNA‐Sonden, die eine Diskriminierung virusreplikativer von (sequestrierter) viraler Genom‐DNA erlaubten, konnte eine effiziente Virusvermehrung in mesenterialen Lymphknoten sowie Milz nachgewiesen werden. Bei je einem Nerz gelang dieser Nachweis auch in Knochenmarkzellen sowie in mononukleären Zellen des peripheren Blutes. In Leber, Niere, Darm und Lunge waren replikative DNA‐Formen nicht nachweisbar. Aufgrund der Southern blot‐Hybridisierungen ergaben sich Hinweise für eine differente, eventuell organspezifische Permissivität von ADV in vivo.

show abstract

“…The major structural protein VP1 is able to bind DNA in contrast to both minor structural proteins VP2 and VP3 [61]. The DNA binding domain was detected in the N-terminal first five amino acids of VP1 (Ala-1-Pro-Lys-Arg-Lys-5).…”

Section: Assemblymentioning

confidence: 95%

Recombinant Virus Like Particles as Drug Delivery System

Georgens¹,

Weyermann²,

Zimmer

2005

CPB

View full text Add to dashboard Cite

The drug delivery system described here is based on a virus like particle consisting of the recombinant expressed major capsid protein of Polyomavirus, VP1. Polyoma, a murine virus belonging to the Papovaviridae, forms a non-enveloped icosahedral capsid. These capsids are organized as a double shell composed of three different proteins: VP1,VP2 and VP3. The outer shell of the vision is composed of 360 VP1 molecules arranged as 72 pentamers. These capsids have a diameter of about 50 nm. The VP1 protein acts as a major ligand for certain membrane receptors during virus infection. Furthermore, the N-terminus of the VP1 protein contains a DNA-binding domain and a nuclear localization sequence. The recombinant production of the VP1 protein offers a save way to obtain a highly purified, non pathogenic pharmaceutical excipient. Combining these aspects, VP1 proteins provide a targeting as well as a drug binding site when used as a save drug carrier for gene therapy. Current applications are also including oligonucleotides as well as small molecules as well as vaccines.

show abstract

Capsid protein VP1 (p85) of aleutian disease virus is a major DNA-binding protein

Cited by 15 publications

References 35 publications

Topographical analysis of the G virion of Aleutian mink disease parvovirus with monoclonal antibodies

Topographical analysis of the G virion of Aleutian mink disease parvovirus with monoclonal antibodies

Violet Mink Develop an Acute Disease after Experimental Infection with Aleutian Disease Virus (ADV) Isolate ADV SL3

Recombinant Virus Like Particles as Drug Delivery System

Contact Info

Product

Resources

About