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J P Clerx

Publications and source records attributed to J P Clerx.

8 recordsLinked to original sources

Genomic and biologic analyses of snowshoe hare virus field and laboratory strains.

Low-passage field strains of snowshoe hare (SSH) virus (Bunyaviridae), the prototype SSH virus (originally isolated in Montana), and La Crosse (LAC) virus were compared serologically by plaque-reduction neutralization (PRNT) and molecularly by oligonucleotide fingerprinting (ONF). The PRNT and ONF results confirmed the identity of the field strains, although some differences in the fingerprints were observed. We have examined the RNA genome variability in the two field and three laboratory strains of SSH virus, using direct sequence analysis of selected RNase T1 oligonucleotides. Few changes were observed among three Montana prototype-derived laboratory isolates, although they have different passage histories. In contrast, the field isolates differed greatly from the laboratory strains. In addition, we have located several of the larger T1 oligonucleotides within the known sequence of the small and large RNA genome segments. We then compared the viruses for their ability to replicate in and be transmitted by Aedes triseriatus mosquitoes. The oral infection rates for LAC, the field isolates, and the SSH prototype, as determined by immunofluorescent examination of midgut tissues, were 100%, 82%, and 47%, respectively. All viruses were also transmissible from mosquitoes to mice.

Aedes↗

Three-dimensional structure of rotavirus.

The three-dimensional structures of double and single-shelled simian rotavirus have been determined to a resolution of 40 A by image processing electron micrographs of unstained, unfixed virus particles embedded in vitreous ice. This study demonstrates that the icosahedral surface lattices in these structures have a triangulation number of 13 in a left-handed configuration. The double-shelled virion has a smooth outer surface with 60 slender spikes. The single-shelled virion, in contrast, exhibits a bristly surface. On the basis of these structures, the locations and number of copies of outer and inner shell proteins have been deduced. The spikes likely correspond to VP3, a hemagglutinin, while the rest of the mass density in the outer shell represents 780 molecules of VP7, a neutralization antigen. The 260 morphological units, located on all the local and strict 3-fold axes of the single-shelled virion are proposed to represent 260 trimers of VP6, which is a subgroup antigen. The regions of closed contact between the outer and the inner shells are located mainly near the local and strict 3-fold axes. A distinctive feature in the rotavirus structure is the presence of 132 large channels spanning across both the shells at all 5 and 6-co-ordinated positions linking the outermost surface with the inner core. In the transcriptionally active single-shelled virion, these channels may provide pathways for importing the metabolites required for the viral RNA transcription and exporting the newly synthesized RNA molecules for subsequent viral replication processes.

Capsid↗

Electron microscopy of vitrified-hydrated La Crosse virus.

La Crosse (LAC) virions were cryopreserved by rapid freezing in a thin layer of vitreous ice. The vitrified-hydrated LAC virions were subsequently imaged at -170 degrees C in a transmission electron microscope equipped with a low-temperature specimen holder. This cryoelectron microscopic technique eliminates the artifacts frequently associated with negative staining. Images of vitrified-hydrated LAC virions clearly revealed surface spikes as well as bilayer structure. Size measurements of the vitrified-hydrated LAC virions showed heterogeneity, with diameters ranging from 75 to 115 nm. Regardless of the particle size, the spike was about 10 nm long, and the bilayer was about 4 nm thick. The spikes are interpreted to be one or both of the glycoproteins, and the bilayer is interpreted to be the membrane envelope of the virus. In contrast to the pleomorphic appearance of the negatively stained LAC virions, the vitrified-hydrated LAC virions showed uniform spherical shapes regardless of their sizes.

Bunyaviridae↗

Tick-borne viruses structurally similar to Orthomyxoviruses.

Members of the Orthomyxoviridae are characterized at the structural level as enveloped, negative sense, RNA viruses that bud from the outer plasma membranes of infected cells and have seven or eight species of single-stranded RNA. None of the three types of orthomyxoviruses (influenza A, B, C) has been shown to be transmitted by arthropods; rather, the viruses are transmitted directly or indirectly from one infected vertebrate to another. Analyses of the virion RNA species and polypeptides of the tick-borne Thogoto and Dhori viruses indicate that they have structural characteristics similar to accepted members of the Orthomyxoviridae. For example, the viruses have seven size classes of single-stranded RNA with 3' end consensus sequences of HOUCGUUG (or U or A) UUGUUC. . . . The viruses contain 54-56 X 10(3) Da nucleocapsid protein, an internal 28 X 10(3) Da putative matrix protein plus minor 85-90 X 10(3) Da proteins, and a major outer 65 X 10(3) Da glycoprotein. In addition to their sensitivity to actinomycin D and alpha-amanitin the viruses morphologically and morphogenetically resemble orthomyxoviruses.

Amanitins↗

Structural characteristics of nairoviruses (genus Nairovirus, Bunyaviridae).

Viruses from six antigenic groups of arthropod-borne viruses [Crimean--Congo haemorrhagic fever (CCHF), Nairobi sheep disease (NSD), Qalyub (QYB), Sakhalin (SAK), Dera Ghazi Khan (DGK) and Hughes (HUG) serogroups], some previously categorized as bunyavirus-like viruses and others previously ungrouped, have recently been assembled by serological analyses into a new genus of viruses (Nairovirus genus) in the Bunyaviridae. Molecular studies of the virion RNA and viral polypeptides have been undertaken with representative members of the different serogroups [Hazara (HAZ) and Congo (CON) viruses, CCHF group; Dugbe (DUG) virus, NSD group; QYB, Omo and Bandia (BDA) viruses, QYB group; Avalon (AVA) virus, SAK group; DGK and Abu Mina (AM) viruses, DGK group; and HUG virus, HUG group]. In agreement with a recent study of QYB virus and in part agreement with an earlier report on DUG virus, the results of these molecular analyses indicate that nairoviruses have: (i) three virion RNA species (large, L, medium, M, and small, S) with apparent mol. wt. of 4.1 x 10(6) to 4.9 x 10(6), 1.5 x 10(6) to 1.9 x 10(6) and 0.6 x 10(6) to 0.7 x 10(6) respectively; (ii) a 48 x 10(3) to 54 x 10(3) mol. wt. nucleocapsid (N) polypeptide; and (iii) two external glycopolypeptides, 72 x 10(3) to 84 x 10(3) mol. w. (G1) and 30 x 10(3) to 40 x 10(3) mol. wt. (G2). Cross-immune precipitation analyses have confirmed that viruses in the Nairovirus genus share antigenic determinants and are antigenically distinct from representative members of th Bunyavirus, Phlebovirus and Uukuvirus genera (Bunyaviridae).

Antigens, Viral↗

Isolation and characterization of the immunoglobin of pike (Esox lucius L.).

The purification of the immunoglobul in from pike serum and its physicochemical characterization is presented. The immunoglobul in was prepared by means of gel filtration and ion exchange chromatography. Measurements in the analytical ultracentrifuge showed a sedimentation constant of 15.0 S. A molecular weight of 650.000 was calculated. The immunoglobulin was composed of heavy and light chains of molecular weights 60.000 and 22.500, respectively. It is likely that the immunoglobulin of pike is composed of 8 heavy and 8 light chains and possesses a tetrameric structure. The heavy chains contain 9.2% sugars and amino sugars. The amino acid composition of the chains is similar to that of other fish immunoglobulins.

Amino Acids↗

Some physicochemical properties of pike fry rhabdovirus RNA.

Pike fry rhabdovirus (pfr) rna has been characterized as a single-stranded non-segmented molecule of about 4 X 10(6) daltons. In sucrose gradients in 0-1 M-NaC1 it had a sedimentation coefficient of 40 to 45S, somewhat lower than that Of Semliki Forest virus RNA. The sedimentation velocity of the RNA is strongly influenced by the salt concentration and divalent cations. It shows a buoyant density of 1-65 g/ml in caesium sulphate. The base composition of the RNA is 21-6% G, 25-I% A, 22-4% C and 30-9% U. It is thus comparable to the RNAs of other rhabdoviruses.

Adenine↗