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Family Potyviridae
Virion Properties
Morphology
Virions
are flexuous filaments with no envelope and are 11 - 15 nm in
diameter, with a helical pitch of about 3.4 nm (Fig. 1). Particle
lengths of members of some of the six genera differ. Members of the
genera Potyvirus, Ipomovirus, Macluravirus, Rymovirus,
Tritimovirus and the unassigned viruses are monopartite with
particle modal lengths of 650 - 900 nm; members of the genus Bymovirus
are bipartite with particles of two modal lengths of 250 - 300 and
500 - 600 nm.

Figure
1: (Left)
Schematic diagram of a potyvirus particle. The N-terminal ~ 30 amino
acids (large rectangle) and C-terminal ~ 19 amino acids (small
rectangle) of the capsid protein molecules are exposed on the
surface of the intact virus particle (from Shukla and Ward, 1989).
(Right) Negative contrast electron micrograph of particles of Plum
pox virus (PPV) stained with 1% PTA, pH 6.0. The bar represents
200 nm (from Scottish Crop Research Institute).
Physicochemical and
Physical Properties
Member
viruses of the genera Potyvirus and Rymovirus have a
density in CsCl of about 1.31 g/cm3 and an S20w
of 150 - 160S. Member viruses of the genus Bymovirus have a
density in CsCl of about 1.29 g/cm3.
Nucleic Acid
Member
viruses of the genera Potyvirus and Rymovirus have a
single molecule of positive sense, ssRNA, 8.5 - 10.0 kb in size (Mr
3.0 x 106). Virions are infectious. A protein (VPg Mr
about 24 x 103) is covalently linked to the 5'-terminal
nucleotide. A polyadenylate tract (20 to 160 adenosines) is present
at the 3' terminus. The complete nucleotide sequence is known for
nearly 30 members of the genus Potyvirus, for two members of
the genus Bymovirus, and one member of the genus Ipomovirus.
Member viruses of the bipartite genus Bymovirus have two
positive sense, ssRNA molecules; RNA1 is 7.5 - 8.0 kb in size (Mr
2.6 x 106) and RNA2 is 3.5 - 4.0 kb in size (Mr 1.5 x 106).
Both RNAs have 3' terminal polyadenylate tracts and a VPg is
probably present at the 5'-termini. The complete nucleotide sequence
of Barley yellow mosaic virus (BaYMV) RNAs has been
determined, and about 70% of Wheat streak mosaic virus (WSMV)
has been sequenced.
Proteins
The
genome-derived polyprotein is cleaved into several proteins, some of
which form inclusion bodies in the cell (see genus descriptions).
Virions contain one capsid protein (CP), Mr of 28.5 - 47 x 103.
N- and C-terminal residues are positioned on the exterior of the
virion. Mild trypsin treatment removes N- and C-terminal segments,
leaving a trypsin-resistant core of about Mr 24 x 103.
Plant proteases may degrade the CP in vivo as happens in
vitro during purification using some procedures or from certain
hosts. All potyvirus CPs display significant amino acid sequence
homology in the trypsin-resistant core, but little homology in their
N and C-terminal segments.
Lipids
None
reported.
Carbohydrates
None
reported.
Genome Organization and
Replication
Genetic
information encoded by the RNA genome is organized as a single ORF.
Genetic maps for the genus Potyvirus, and BaYMV, a member of
the genus Bymovirus, are presented in genera descriptions.
For members of the genus Potyvirus, the genome is expressed
initially as a polyprotein which undergoes co- and post-translational
proteolytic processing by three viral-encoded proteinases to form
individual gene products. Genomic RNA replicates via the production
of a full-length negative sense RNA.
Antigenic Properties
The
viral proteins are moderately immunogenic; there are serological
relationships between members. A conserved internal trypsin-resistant
core CP epitope has been identified, that is similar in most members
of the family.
Biological Properties
Inclusion Body
Formation
All
members of the family Potyviridae form cytoplasmic
cylindrical inclusion (CI) bodies during infection. The CI is an
array of a viral protein of an Mr 70 x 103 which
possesses ATPase and helicase activities. The viruses encode and
express the following proteins, but inclusion bodies composed of
these proteins are not formed in all instances (some potyviruses
induce nuclear inclusion bodies which are co-crystals of two
viral-encoded proteins present in equimolar amounts): The small
nuclear inclusion (NIa) protein (Mr 49 x 103) is a
polyprotein consisting of the VPg and proteinase. The large nuclear
inclusion (NIb) protein has amino acid motifs of RNA-dependent RNA-polymerases.
NIa and NIb are also found in the cytoplasm. Amorphous inclusion
bodies are also evident in the cytoplasm during certain potyvirus
infections and represent aggregations of the protein HC-Pro. This
protein has a helper component activity and a proteolytic activity
associated with it. Bymoviruses do not encode a protein analogous to
the helper component in length, but a protein with Mr 28 x 103
from RNA2 of BaYMV has amino acid domains with sequence similarities
to the potyvirus protein HC-Pro.
Host Range
Some
members have a narrow host range, most members infect an
intermediate number of plants, and a few members infect species in
up to 30 families. Transmission to most hosts is readily
accomplished by mechanical inoculation. Many viruses are widely
distributed. Distribution may be aided by seed transmission in some
cases.
Transmission
Potyviruses
are vectored by a variety of organisms. Members of the genus Potyvirus
and Macluravirus have aphid vectors that transmit in a
non-persistent, non-circulative manner. A helper component and a
particular CP amino acid triplet (i.e., DAG for some potyviruses)
are required for aphid transmission. Rymoviruses and tritimoviruses
are transmitted by mites, possibly in a persistent-circulative
manner. Bymoviruses are transmitted by a fungus vector. Ipomoviruses
appear to be transmitted by a whitefly.
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