The in vivo behaviour of twenty-four strains of alfalfa mosaic virus

Hull, Roger; Hills, G. J.; Plaskitt, A.

doi:10.1016/0042-6822(70)90321-1

Cited by 33 publications

(19 citation statements)

References 32 publications

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“…Particles of nepoviruses are usually found within double-walled tubes The observations above show that, although the virus isolates examined have similar host ranges and are serologically indistinguishable, there are differences in their in vivo behavior. This situation is also found with AMV which has several aggregation forms [15] specific to strains which are sero-logicaliy indistinguishable [H u ll and van R egenm ortel, unpublished data]. Preliminary investigations have shown that the tryptic peptide maps of NRSV differ from those of BBWV and PRSV [T. R. D oel, personal commun.].…”

Section: Discussionmentioning

confidence: 81%

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The <i>in vivo </i>Behavior osf Broad Bean Wilt Virus and Three of its Strains

Hull¹,

Plaskitt²

1973

Intervirology

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The particles of broad bean wilt virus and three of its strains aggregated in different ways in infected cells of Chenopodium amaranticolor, C.quinoa and Nicotiana clevelandii. Most aggregates were crystals, interlocking networks of partides and sheets of particles rolled into different tubular forms or lying between adjacent mitochondria. One strain induces the formation of tubules consisting of a membrane around a file of particles. These structures are discussed with regard to the current ideas on the relationships between the virus strains.

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Section: Discussionmentioning

confidence: 81%

“…I). These resemble in some respects the type 3 aggregates of alfalfa mosaic virus (AMV) [9,15]. However, the particles of BBWV and PRSV did not appear to be arranged so definitely and were not packed into interlocking rings of 6 as were those of AMV.…”

Section: Discussionmentioning

confidence: 94%

The <i>in vivo </i>Behavior osf Broad Bean Wilt Virus and Three of its Strains

Hull¹,

Plaskitt²

1973

Intervirology

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“…For details see [I31 Quite a number of different AMV strains have been described in the past [14,15]. Exceptionally long particles occur in preparations of the strain VRU [16] shown in Fig.…”

Section: Isolation Modification and Cyanogen Bromide Cleavage Ojalfamentioning

confidence: 99%

The Primary Structure of the Coat Protein of Alfalfa Mosaic Virus Strain VRU. A Hypothesis on the Occurrence of Two Conformations in the Assembly of the Protein Shell

Castel¹,

Kraal²,

Graaf³

et al. 1979

Eur J Biochem

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The complete primary structure of the coat protein of strain VRU of alfalfa mosaic virus (AMV) is reported. The strain is morphologically different from all other AMV strains as it contains large amounts of unusually long virus particles. This is caused by structural differences in the coat protein chain. The amino acid sequence has mainly been established by the characterization of peptides obtained after cleavage with cyanogen bromide and digestion with trypsin, chymotrypsin, thermolysin or Staphylococcus aureus protease. The major sequencing technique used was the dansyl-Edman procedure. The VRU coat protein consists of 219 amino acid residues corresponding to a molecular weight of 24056. Compared to the coat protein of strain 425 [Van Beynum et al. (1977) Eur. J. Biochem. 72,[63][64][65][66][67][68][69][70][71][72][73][74][75][76][77][78], 15 amino acid substitutions were localized. Most of them have a conservative character and may be explained by single-point mutations. A correction is given for the AMV 425 coat protein: Asn-216 was shown to be Asp-216.The prediction of the secondary structure for the two viral coat proteins was not significantly influenced by the various amino acid substitutions except for the region containing residues 65 -100. This led us to the hypothesis that the AMV coat protein may occur in two different conformations favouring its incorporation into either a pentagonal or hexagonal quasi-equivalent position in the lattice of the protein shell. The substitutions in the above-mentioned region of the VRU coat protein may have caused a strong preference for the hexagonal lattice conformation. The model is supported by preliminary sequence data of the same coat protein region in AMV 15/64, a strain morphologically intermediate between 425 and VRU Alfalfa mosaic virus (AMV) is an interesting virus from both a biological and a structural point of view. This small plant virus belongs to the group of viruses with a tripartite single-stranded RNA genome encapsidated by one single type of coat protein subunits into rods of different but discrete lengths. Like the other heterocapsidic viruses within this group, AMV needs a small amount of coat protein to start an infection cycle (see [l -31 for a review). This remarkable biological activity of the coat protein was already discovered in 1971 [4], but the underlying mechanism is not known as yet.In our group we have established the complete primary structure of the coat protein of AMV strain 425, which consists of 220 amino acids [5]. Knowledge of the primary structure appeared to be of great help in several other lines of investigation concerning this plant virus. It was possible to make a precise comparison between the authentic coat protein and the biosynthetic products synthesized in various cell-free systems programmed with the subgenomic AMV RNA 4 [6-91. The amino acid sequence data greatly facilitated the nucleotide sequence determination of the coat protein cistron in the monocistronic AMV RNA 4 [lo, 1 I]. Furthermore, this knowledge is ...

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“…Some individual viruses can be distinguished by the inclusions they induce (Edwardson & Christie, 1978;Martelli & Russo, 1977;Maramorosch, 1977). Viruses within nine groups induce distinctive inclusions which are diagnostic for infections at the group level (Table 2) and individual viruses within a group may sometimes produce distinctive effects (Hull et al, 1970;Christie & Edwardson, 1977;Lesemann, 1977, Gill & Chong, 1979Shalla et al, 1980;Hatta & Francki, 1981 a, b).…”

Section: Cytopathology By Light and Electron Microscopymentioning

confidence: 99%