Interaction between hantaviral nucleocapsid protein and the cytoplasmic tail of surface glycoprotein Gn.

Hantaviral N and Gn proteins were shown to interact, thus providing the long-awaited evidence for one of the crucial steps in the virus replication at which RNPs are directed to the site of the virus assembly. Using pull-down assay and point mutagenesis it was demonstrated that intact, properly folded zinc fingers in the Gn protein cytoplasmic tail as well as the middle domain of the N protein (that includes aa residues 80-248) are essential for the interaction.

Oligomerization of hantaviral nucleocapsid protein: charged residues in the N-terminal coiled-coil domain contribute to intermolecular interactions.

The nucleocapsid (N) protein of hantaviruses (family Bunyaviridae) is the most abundant component of the virion; it encapsidates genomic RNA segments and participates in viral genome transcription and replication, as well as in virus assembly. During RNA encapsidation, the N protein forms intermediate trimers and then oligomers via 'head-to-head, tail-to-tail' interactions. In previous work, using Tula hantavirus (TULV) N protein as a model, it was demonstrated that an intact coiled-coil structure of the N terminus is crucial for the oligomerization capacity of the N protein and that the hydrophobic 'a' residues from the second alpha-helix are especially important.

Oligomerization of hantavirus nucleocapsid protein: analysis of the N-terminal coiled-coil domain.

Hantaviruses constitute a genus in the family Bunyaviridae. They are enveloped negative-strand RNA viruses with a tripartite genome encoding the nucleocapsid (N) protein, the two surface glycoproteins Gn and Gc, and an RNA-dependent RNA polymerase. The N protein is the most abundant component of the virion; it encapsidates genomic RNA segments forming ribonucleoproteins and participates in genome transcription and replication as well as virus assembly.

A novel insertion site inside the potyvirus P1 cistron allows expression of heterologous proteins and suggests some P1 functions.

The P1 cistron encodes the first and most variable part of the polyprotein of potyviruses. A site tolerant to a pentapeptide insertion at the N-terminus of Potato virus A P1 (Genome Res. 12, 584-594) was used to express heterologous proteins (insertions up to 783 nucleotides) with or without flanking new proteolytic sites.

Strains of Peru tomato virus infecting cocona (Solanum sessiliflorum), tomato and pepper in Peru with reference to genome evolution in genus Potyvirus.

Two isolates (SL1 and SL6) of Peru tomato virus (PTV, genus Potyvirus) were obtained from cocona plants (Solanum sessiliflorum) growing in Tingo María, the jungle of the Amazon basin in Peru. One PTV isolate (TM) was isolated from a tomato plant (Lycopersicon esculentum) growing in Huaral at the Peruvian coast. The three PTV isolates were readily transmissible by Myzus persicae.