Vector relationships and other characteristics of barley yellow striate mosaic virus (BYSMV)

Barley yellow striate mosaic virus (BYSMV) was inoculated by its planthopper vector Laodelphax striatellus (Homoptera, Delphacidae) to 44 species of Gramineae, 26 of which in eight tribes were infected. The virus was not transmitted through wheat seed nor did it infect five dicotyledonous hosts of other rhabdoviruses. The most susceptible species were in the tribes Festuceae and Hordeae. Barley, Bromus spp., oats, Phalaris canariensis, Setaria italica, Sorghum spp., and sweet corn cv. Golden were diagnostic hosts. Electron microscopy of crude sap was also a sensitive diagnostic method. Properties of BYSMV were determined by injecting L. striatellus with crude sap from infected barley. Sap was infectious after 10 min at 50–55 °C but not after 10 min at 60 °C, when diluted with buffer to 10^--² but not to 10^--³, when stored for 2 but not 4 days at 5 °C or when kept for 1 but not 2 days at 22 °C. The planthopper Javesella pellucida was an experimental vector of BYSMV but the virus was not transmitted by the leafhoppers Macrosteles sexnotatus or Psammotettix striatus (Homoptera, Cicadellidae). The latent period of BYSMV in L. striatellus was most commonly 15 or 16 days (minimum, 9 days; maximum, 29 days). The minimum acquisition access period for transmission was between 1 h and 5 h, and the minimum inoculation feeding time was 15 min. After 24 h and 8 day acquisition feeds, 30.4% and 42.8% respectively of L. striatellus transmitted BYSMV. When transferred daily, infective hoppers transmitted virus intermittently. The maximum retention of infectivity by L. striatellus was 36 days. Two of five infective females transmitted BYSMV transovarially. Larvae became infective in the second wk after hatching and transmitted for up to 3 wk.     

Computer analysis between nucleotide and amino acid sequences of bean golden mosaic virus and those of maize streak, wheat dwarf, chloris striate mosaic, and beet curly top viruses

Bean golden mosaic virus (BGMV) DNA 1 and 2 have little sequence homology with maize streak virus (MSV), wheat dwarf virus (WDV), and chloris striate mosaic virus (CSMV) DNAs. BGMV DNA 1 and beet curly top virus (BCTV) DNA are closely related, whereas BGMV DNA 2 and BCTV DNA are not related. Direct amino acid homologies of predicted proteins between BGMV ORFs and MSV ORFs, WDV ORFs or CSMV ORFs were 40-50%. BGMV 1L1 and BCTV L1, and BGMV IL3 and BCTV L4 were highly conserved. The sequence TAATATTAC was detected in the loops of hairpin structures of 5 gemini-viruses.     

The tobacco mosaic virus particle: structure and assembly

A short account is given of the physical and chemical studies that have led to an understanding of the structure of the tobacco mosaic virus particle and how it is assembled from its constituent coat protein and RNA. The assembly is a much more complex process than might have been expected from the simplicity of the helical design of the particle. The protein forms an obligatory intermediate (a cylindrical disk composed of two layers of protein units), which recognizes a specific RNA hairpin sequence. This extraordinary mechanism simultaneously fulfils the physical requirement for nucleating the growth of the helical particle and the biological requirement for specific recognition of the viral DNA.     

Purification and some particle properties of anthriscus yellows virus, a phloem-limited semi-persistent aphid-borne virus

Anthriscus yellows virus (AYV), a phloem-limited virus transmitted in the semi-persistent manner by the aphid Cavariella aegopodii, was purified by treatment of leaf extracts with cellulasc, followed by differential and sucrose density gradient centrifugation. ‘The preparations contained isometric particles c. 29 nm in diameter which were unstable unless stored in buffer at pH 8.0 containing 1 mM CaCl₂,. The particles sedimented as two components, ’full‘ nucleoprotein particles with A₂₆₀/A₂₈₀= 1.83 containing about 42% nucleic acid, and ’empty‘ protein shells with A₂₆₀,/A₂₈₀= 0.73; their buoyant densities in CsCl solutions were 1.52 and 1.27 g/cm³. Respectively. Yields of ihe nircleoprotein particles were c. 1.75 mg/kg leaf tissue. The particles contained a single species of RNA, of mol. wt 3.6 × 10 “(10 000 nucleotides). Particle protein preparations contained four electrophoretic species, of mol. wt (× 10³) 35.0, 28.3, 23.3 and 22.3.C. aegopodii did not transmit AYV from purified preparations. A rabbit injected with AYV preparations produced antibodies that coated AYV particles in electron microscope tests, but gave variable reactions in immunosorbent electron microscopy (ISEM), depending on the composition of the medium. No reactions were obtained in enzyme-linked inimunosorbent asjay (ELISA). No serological relationship was detected in ISEM between AYV and any of 10 viruses that resembled it in one or more properties.     

Nicotiana velutina mosaic virus: purification, properties and affinities with other rod-shaped viruses

Nicotiana velutina mosaic virus (NVMV), found in Australia, was transmitted by inoculation of sap to twenty species in the Solanaceae and Chenopodiaceae, and to Gomphrena globosa; its host range closely resembles that of potato mop-top virus (PMTV). Infectivity was abolished when sap was kept at room temperature between 1 and 4 days, or when heated for 10 min between 60 and 70 °C. NVMV was frequently transmitted through the seed of four Nicotiana spp. NVMV and PMTV were purified by a method that involved redissolving virus particles sedimented by low speed centrifugation of leaf extracts, followed by sedimentation through sucrose cushions. NVMV preparations contain rod-shaped particles about 18 nm wide and with a large range of lengths, the commonest being 125–150 nm. The particles have a helical structure with a pitch of 2–9 nm, break easily, and contain a single protein of apparent mol. wt. 21|400, slightly larger than that of PMTV (19 800). In serological tests assessed by electron microscopy, no relationship was detected between NVMV and PMTV, or barley stripe mosaic, beet necrotic yellow vein, soil-borne wheat mosaic, tobacco mosaic or tobacco rattle viruses. However, antiserum to soil-borne wheat mosaic virus reacted quite strongly with PMTV and weakly with tobacco mosaic virus. NVMV is considered to be a distinct member of the tobamovirus group; its frequent transmission through seed may be an adaptation to the arid environment where it was found. Its cryptogram is */*:*/*:E/E:S/*.     

Tobacco mosaic virus particle structure and the initiation of disassembly

The structure of an intact tobacco mosaic virus (TMV) particle was determined at 2.9 A resolution using fibre diffraction methods. All residues of the coat protein and the three nucleotides of RNA that are bound to each protein subunit were visible in the electron density map. Examination of the structures of TMV, cucumber green mottle mosaic virus and ribgrass mosaic virus, and site-directed mutagenesis experiments in which carboxylate groups were changed to the corresponding amides, showed that initial stages of disassembly are driven by complex electrostatic interactions involving at least seven carboxylate side-chains and a phosphate group. The locations of these interactions can drift during evolution, allowing the viruses to evade plant defensive responses that depend on recognition of the viral coat protein surface.