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At least 1,369 records · Page 76Linked to original sources
PubMed1984

The antiviral spectrum of (E)-5-(2-bromovinyl)-2'-deoxyuridine.

The antiviral activity spectrum of (E)-5-(2-bromovinyl)-2'-deoxyuridine (BVdU) is not restricted to herpes simplex virus type 1 (HSV-1) and varicella-zoster virus (VZV) but also encompasses several other herpesviruses such as suid herpesvirus type 1 (SHV-1), bovid herpesvirus type 1 (BHV-1), simian varicella virus (SVV), herpesvirus saimiri, herpesvirus platyrrhinae, and the baculovirus Trichoplusia ni multiple nuclear polyhedrosis virus. Other herpesviruses such as herpes simplex virus type 2, cytomegalovirus and Epstein-Barr virus are also inhibited by BVdU, albeit to a lesser extent than HSV-1, VZV, SHV-1, BHV-1 and SVV.

Antiviral Agents↗
PubMed1981

Biological and biochemical investigations on five European isolates of Mamestra brassica nuclear polyhedrosis virus.

Five multiply enveloped European isolates of Mamestra brassicae nuclear polyhedrosis virus (Oxford, German, French, Dutch and Danish) were found to be very closely related serologically using the enzyme linked immunosorbent assay (ELISA) double antibody sandwich method and immunodiffusion. By SDS-polyacrylamide gel electrophoresis of viral proteins and restriction endonuclease analysis of DNA using seven enzymes there appeared to be two variants as the Oxford and German isolates were distinct from the other three. The German isolate was shown to be more susceptible to Nonidet P40 detergent treatment affecting some nucleocapsid structural polypeptides which also reduced antigenicity in gel immunodiffusion plates. In bioassays of polyhedra, the Dutch isolate showed a higher LD50 than the other viruses although this was not statistically significant.

Antigens, Viral↗
PubMed1992

Unusual morphology of a virus which produces carbon dioxide sensitivity in mosquitoes.

A virus, named Matsu, presumed to be the etiologic agent of hereditary sensitivity to carbon dioxide in Culex quinquefasciatus mosquitoes, was adapted to growth in the C6/36 line of Aedes albopictus cells. Though it was expected that the mosquito virus would be a rhabdovirus like sigma, the etiologic agent of hereditary carbon dioxide sensitivity in Drosophila melanogaster flies, that was not the case. The virion of Matsu was found to be unlike any previously described virus. It was pleomorphic, enveloped, from 200 to 550 nm in maximum diameter, and contained from three to several dozen virus-like polyhedral structures approximately 30 nm in diameter.

Animals↗
PubMed2004

The refined structure of Nudaurelia capensis omega virus reveals control elements for a T = 4 capsid maturation.

Large-scale reorganization of protein interactions characterizes many biological processes, yet few systems are accessible to biophysical studies that display this property. The capsid protein of Nudaurelia capensis omega Virus (NomegaV) has previously been characterized in two dramatically different T = 4 quasi-equivalent assembly states when expressed as virus-like particles (VLPs) in a baculovirus system. The procapsid (pH 7), is round, porous, and approximately 450 A in diameter. It converts, in vitro, to the capsid form at pH 5 and the capsid is sealed shut, shaped like an icosahedron, has a maximum diameter of 410 A and undergoes an autocatalytic cleavage at residue 570. Residues 571-644, the gamma peptide, remain associated with the particle and are partially ordered. The interconversion of these states has been previously studied by solution X-ray scattering, electron cryo microscopy (CryoEM), and site-directed mutagenesis. The particle structures appear equivalent in authentic virions and the low pH form of the expressed and assembled protein. Previously, and before the discovery of the multiple morphological forms of the VLPs, we reported the X-ray structure of authentic NomegaV at 2.8 A resolution. These coordinates defined the fold of the protein but were not refined at the time because of technical issues associated with the approximately 2.5 million reflection data set. We now report the refined, authentic virus structure that has added 29 residues to the original model and allows the description of the chemistry of molecular switching for T = 4 capsid formation and the multiple morphological forms. The amino and carboxy termini are internal, predominantly helical, and disordered to different degrees in the four structurally independent subunits; however, the refined structure shows significantly more ordered residues in this region, particularly at the amino end of the B subunit that is now seen to invade space occupied by the A subunits. These additional residues revealed a previously unnoticed strong interaction between the pentameric, gamma peptide helices of the A and B subunits that are largely proximal to the quasi-6-fold axes. One C-terminal helix is ordered in the C and D subunits and stabilizes a flat interaction in two interfaces between the protein monomers while the other, quasi-equivalent, interactions are bent. As this helix is arginine rich, the comparable, disordered region in the A and B subunits probably interacts with RNA. One of the subunit-subunit interfaces has an unusual arrangement of carboxylate side chains. Based on this observation, we propose a mechanism for the control of the pH-dependent transitions of the virus particle.

Amino Acid Sequence↗
PubMed2002

Phylogenetic analysis of acute bee paralysis virus strains.

Reverse transcription-PCR assays have been established for a quick, sensitive, and specific diagnosis of acute bee paralysis virus (ABPV), a common virus of the honeybee (Apis mellifera), directly from clinical samples. A 3,071-nucleotide fragment of the ABPV genome, which includes the entire capsid polyprotein gene, was amplified from Austrian, German, Polish, and Hungarian ABPV samples and sequenced, and the sequences were compared. The alignment of a smaller fragment with ABPV sequences from the United States and the United Kingdom revealed nucleotide identity rates between 89 and 96%, respectively. Phylogenetic trees which display the molecular relationship between the viruses of different geographic origin were constructed.

Animals↗
PubMed2006

Occurrence of six honeybee viruses in diseased Austrian apiaries.

The occurrence, prevalence, and distribution patterns of acute bee paralysis virus (ABPV), black queen cell virus (BQCV), chronic bee paralysis virus (CBPV), deformed wing virus (DWV), Kashmir bee virus (KBV), and sacbrood virus (SBV) were investigated in 90 Austrian honeybee colonies suffering from symptoms of depopulation, sudden collapse, paralysis, or dark coloring by employing reverse transcription-PCR. Infestation with parasites was also recorded. The samples originated from all parts of Austria. The most prevalent virus was DWV, present in 91% of samples, followed by ABPV, SBV, and BQCV (68%, 49%, and 30%, respectively). CBPV was detected in 10% of colonies, while KBV was not present in any sample. In most samples, more than one virus was identified. The distribution pattern of ABPV, BQCV, CBPV, and SBV varied considerably in the different geographic regions investigated, while DWV was widespread in all Austrian federal states. In bees that showed dark coloring and disorientation, CBPV was always detected. Simultaneous infections of DWV and ABPV were most frequently observed in colonies suffering from weakness, depopulation, and sudden collapse. Bees obtained from apparently healthy colonies within the same apiaries showed a similar distribution pattern of viruses; however, the relative virus load was 10 to 126 times lower than in bees from diseased colonies. A limited number of bee samples from surrounding central European countries (Germany, Poland, Hungary, and Slovenia) were also tested for the presence of the above viruses. Variances were found in the distribution of BQCV and SBV.

Animal Husbandry↗
PubMed1979

[Ultracytological studies of the morphogenesis and structure of the nuclear polyhedrosis virus in the silkworm moth, Bombyx mori L].

An electron-microscopic investigation was made on hypodermal tissues of silkworms spontaneously infested by nuclear polyhedral disease, due to low temperature stress. It was established that the polyhedral virus is formed in the viroplasma produced after viral cell infection, is included in the intimate and developing membrane singly or in fascicles containing several (up to 9) and is finally incapsulated in polyhedral protein. Besides viral rods, various polymorphic forms were observed in the nucleus and around the polyhedras in the process of formation, which are considered as viral substructures (or nucleocapsidless viruses), membrane structures and surplus synthetized polyhedral protein. It can be presumed that virus replication in single cell nucleus is a continuous process which goes on until complete nuclear structure depletion.

Animals↗