Genetic relatedness of two nucleopolyhedrosis viruses pathogenic for Orgyia pseudotsugata

Journal of General Virology

Martignoni

Beaudreau

1982

SUMMARYTo investigate the DNA sequence homology between the multicapsid nuclear polyhedrosis virus of Autographa californica and the multicapsid and single capsid nuclear polyhedrosis virus of Orgyia pseudotsugata, the stringency of hybridization conditions was varied. Thirteen to 25 % homology between the multicapsid viruses of A. californica and O. pseudotsugata was detected in 20, 30 and 40% formamide, indicating that fairly stable duplexes were being formed. Under the most stringent conditions in 50% formamide little homology was detected. In contrast to the multicapsid viruses, the single capsid virus of O. pseudotsugata demonstrated about 10% sequence homology in 20% formamide, but these duplexes were unstable and the percentage homology decreased markedly in the higher formamide concentrations. Examination of the specific regions of homology by hybridizing labelled DNA to Southern blots of the virus DNAs revealed that the regions of homology between these viruses were not limited to one region of the genome but were found on a number of restriction fragments.

Section: Methodsmentioning

confidence: 99%

DNA Sequence Homology between Autographa californica and Orgyia pseudotsugata Nuclear Polyhedrosis Viruses

Journal of General Virology

Martignoni

Beaudreau

1982

“…For example, compared to OpMNPV, OpSNPV has fewer nucleocapsids per polyhedron (670 vs 1600) [8,9], has longer nucleocapsids (277 vs 227 ml) [4], a larger genome [10] with a lower G ? C content [11], was thermo inactivated at a lower temperature (55 vs 60°C), and causes a significantly longer mean survival time (6.85 vs 5.83 days) [12]. This could result in relatively more OpSNPV production because the insects can continue to feed and grow right up until they die.…”

Section: Nucleocapsid Aggregation: Multiple Versus Single Nucleocapsimentioning

confidence: 99%

Baculovirus nucleocapsid aggregation (MNPV vs SNPV): an evolutionary strategy, or a product of replication conditions?

2014

Virus Genes

Lepidopteran nucleopolyhedroviruses are members of the Baculoviridae and have been categorized as having two morphotypes of occluded virions: multiple nucleocapsids or single nucleocapsids within the virion envelope. Although it is a definitive characteristic of specific viruses, it appears to lack a defined genetic basis and is independent of virus phylogeny. This review summarizes the factors that appear to influence this trait and the role that it may play in virus biology.

“…From the predicted secondary structure, it appears that the tyrosines could be clustered in close proximity in two areas of the NH2-terminal region. mology (12). In addition, the two viruses show distinct nucleocapsid proteins when analyzed by polyacrylamide gel electrophoresis (unpublished data).…”

Section: Methodsmentioning

confidence: 99%

“…Although the polyhedrin molecules from these two NPVs are identical in molecular weight and have closely related amino acid composition and antigenicity (8), the viruses are genetically distinct. They have been distinguished based on genome size (NPBV, 86 X 106 daltons; NPSV, 103 X 106 daltons) (9), G-C content of their DNA (10,11), and restriction endonuclease fragment patterns, and have been demonstrated to have 1% or less DNA sequence homology (12).…”

mentioning

confidence: 99%

Tryptic peptide analysis and NH ₂ -terminal amino acid sequences of polyhedrins of two baculoviruses from Orgyia pseudotsugata

Proc. Natl. Acad. Sci. U.S.A.

Bailey

Brimhall

et al. 1979

Comparative analysis of the tryptic peptides and terminal amino acid sequence was made on polyhedrins from two genetically different baculoviruses that are naturally pathogenic for the same insect host. A distinctive feature of baculovirus subgroups A [nucleopolyhedrosis viruses (NPVs)] and B [granulosis viruses (GVs)] is the occlusion of the virions in a crystalline protein matrix. This protein is termed polyhedrin and granulin in NPVs and GVs, respectively. The crystal stabilizes the virions outside the host, and viable NPVs have been recovered from soil up to 11 years after a virus outbreak (1). The crystalline protein is composed of protein subunits of 25,000-30,000 daltons (2) and is soluble at alkaline pH. After ingestion, the crystals are dissolved by the alkaline pH of the insect midgut, thereby releasing the virions and allowing the infection to proceed. The primary structure of polyhedrin and granulin appears to be highly conserved. Studies using complement fixation indicated that granulins and polyhedrins from baculoviruses that infect Lepidoptera were antigenically related but differed from those produced by viruses that infect Hymenoptera (3). More recently it has been demonstrated that polyhedrins and granulins from a variety of Lepidoptera viruses have related tryptic peptide maps (4-6).Orgyia pseudotsugata (the Douglas-fir tussock moth) is infected by two NPVs termed the nucleopolyhedrosis bundle virus (NPBV) and the nucleopolyhedrosis single-rod virus (NPSV) based on the number of nucleocapsids per envelope (7). Although the polyhedrin molecules from these two NPVs are identical in molecular weight and have closely related amino acid composition and antigenicity (8), the viruses are genetically distinct. They have been distinguished based on genome size (NPBV, 86 X 106 daltons; NPSV, 103 X 106 daltons) (9), G-C content of their DNA (10, 11), and restriction endonuclease fragment patterns, and have been demonstrated to have 1% or less DNA sequence homology (12).This report compares the elution profiles of tryptic fragments of polyhedrin and the amino acid sequences of the NH2-terminal 36 amino acids of polyhedrins from the two NPVs pathogenic for 0. pseudotsugata. The sequences are also compared to that reported for the polyhedrin of an NPV pathogenic for the silkworm. MATERIALS AND METHODSProduction and Purification of NPVs. NPVs were produced in 0. pseudotsugata larvae infected per os or by injection with infectious hemolymph. At death or at an advanced stage of infection the insects were homogenized in a Virtis blender, passed through two layers of gauze, made 50% sucrose (wt/wt), and centrifuged at 17,000 X g for 30 min at 200C. This supernatant was discarded, and the pellet was suspended in TNS buffer (20 mM Tris-HCI/0.9% NaCl/0.00075% sodium dodecyl sulfate, pH 7.2), layered on a step gradient consisting of 12 ml of 58% sucrose (wt/wt) overlaid with 12 ml of 52% sucrose (wt/wt), and centrifuged at 112,000 X g in a Beckman SW 27 rotor for 1 hr at 15°C. The interface between the 52 an...