Comoviridae: Plant Picorna-like Viruses

Olivier Le Gall, INRA, Bordeaux-Aquitaine, France Joan Wellink, Wageningen Agricultural University, Wageningen, The Netherlands
The Comoviridae are plant viruses that share many structural and functional features with animal and human viruses of the family Picornaviridae.

Secondary article
Article Contents
. Introduction . Classification, Including Prominent Members . Historical Perspective . Structure of Virus Particles . Structure of the Virus Genome and Function of Genome-encoded Proteins . Relationships with Other Families . Pathogenesis

Introduction
Virtually all prokaryotic and eukaryotic organisms can be infected by viruses, obligatory parasites that rely on the cellular metabolism and metabolites to accomplish their replication cycle, often (but not always) at the expense of their host. Viruses are generally composed of a relatively small-sized genome, from a few thousands to a few hundred thousand nucleotides, packed in a protein shell, the capsid, itself sometimes enveloped in membranous structures. Viruses have been typied according to their general properties (host, properties of host invasion, etc.), their structure and the nature of their genome (deoxyribonucleic acid (DNA) or ribonucleic acid (RNA), singleor double-stranded, mono- or multipartite, terminal structures, size, etc.). Plants and animals share important features of their metabolism but also dier by characteristics to which their respective viruses have adapted. The usual result is that plant viruses cannot multiply in animal cells, and vice versa. However some plant and animal virus families share many structural and functional characteristics, like the animal Picornaviridae and the plant Comoviridae. The aim of this article is to underline the similarities between viruses belonging to these two families, while describing more precisely the properties of the Comoviridae.

. Transmission and Epidemiology . Control

and the economically very important Arabis mosaic virus (ArMV), Grapevine fanleaf virus (GFLV) and Raspberry ringspot virus (RRSV). Subgroup B contains nine members, including Tomato black ring virus (TBRV). Subgroup C contains 13 members, including Tomato ringspot virus (ToRSV) and Cherry leafroll virus (CLRV). In addition, several other virus species have been tentatively placed in the genus Nepovirus, but recent sequence data indicate that they might represent the rst characterized representatives of new genera.

Historical Perspective
The family Comoviridae was introduced in the sixth report of the International Committee on Taxonomy of Viruses (ICTV) in 1995 to account for the similarities of the three virus genera Comovirus, Nepovirus and Fabavirus. The nepoviruses were among the rst plant viruses to be recognized as a group, when Cadman, in 1963, proposed to dierentiate two types of nematode-transmitted viruses, the polyhedral ones (the nepoviruses) and the tubular ones (the netuviruses, now known as tobraviruses). The nepoviruses thus derive their name from their Nematode vectors and their polyhedral virions. In 1963, only six dierent nepoviruses were known, of which one, Strawberry latent ringspot virus (SLRSV), is now considered as a tentative member of the genus (Table 1). The comoviruses were described as a group in 1971, when the plant virus subcommittee of the ICTV, then chaired by Brian Harrisson, issued the rst classication of plant viruses, comprising 16 groups. Comoviruses derive their name from their type member, Cowpea mosaic virus. The fabavirus group is more recent, created in 1987 to group three virus species previously recognized as atypical comoviruses. The name Fabavirus derives from one of the major hosts of these viruses, the broad bean Vicia faba.

Classification, Including Prominent Members

Table 1 lists all the Comoviridae members characterized so far. There are three genera (Comovirus, Nepovirus and Fabavirus) within the family Comoviridae The genus Comovirus contains 15 members. The type member of comoviruses is Cowpea mosaic virus (CPMV). The genus Fabavirus contains four members. The type member of fabaviruses is Broad bean wilt virus 1 (BBWV1). There are three subgroups within the genus Nepovirus, dened according to structural and biological criteria. Subgroup A contains eight members, including the Nepovirus type member Tobacco ringspot virus (TRSV)

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Comoviridae: Plant Picorna-like Viruses

Table 1 All known members of the Comoviridae English vernacular name Genus Comovirus Andean potato mottle virus Bean pod mottle virus Bean rugose mosaic virus Broad bean stain virus Broad bean true mosaic virus Cowpea mosaic virusa Cowpea severe mosaic virus Glycine mosaic virus Pea green mottle virus Pea mild mosaic virus Quail pea mosaic virus Radish mosaic virus Red clover mottle virus Squash mosaic virus Ullucus virus C Genus Fabavirus Broad bean wilt virus 1a Broad bean wilt virus 2 Abbreviation APMV BPMV BRMV BBSV BBTMV CPMV CPSMV GMV PGMV PMiMV QPMV RMV RCMV SMV UVC CMI/AABb 203 108 246 126 20 47, 197 209 RNA1c [M84806, M84483] U70866 (5983 nt) RNA2c L16239 (3671 nts) M62738 (3862 nts)

X00206 (5889 nt) M83830 (5957 nt)

X00729 (3481 nts) M83309 (3732 nts)

238 121 74 43 277

X64886 (6033 nt)

M14913 (3453 nts) AF059533 (3356 nts) AF059532 (3369 nts)

BBWV1 BBWV2

81

[AB018702-703] AB013615 (5957 nt)

U65985 (3182 nts) AB013616 (3589 nts) AB018698 (3569 nts) AF104335 (3588 nts) AB011007 (3591 nts)

Lamium mild mosaic virus Patchouli mild mosaic virus Genus Nepovirus (subgroup A) Arabis mosaic virus Arracacha virus A Artichoke Aegean ringspot virus Cassava American latent virus Grapevine fanleaf virus Potato black ringspot virus Raspberry ringspot virus Tobacco ringspot virusa Genus Nepovirus (subgroup B) Artichoke Italian latent virus Beet ringspot virus Cacao necrosis virus Crimson clover latent virus Cycas necrotic stunt virus Grapevine chrome mosaic virus Mulberry ringspot virus Olive latent ringspot virus Tomato black ring virus

LMMV PaMMV

ArMV AVA AARSV CsALV GFLV PBRSV RRSV TRSV

16 216

X81814 (3852 nts) X81815 (3711 nts)

28 206 6, 198 17, 309

D00915 (7342 nt)

X16907 (3774 nts) S46011 (3928 nts) [L09205] [X87254]

U50869 (7514 nt)

AILV BRSV CoNV CCLV CNSV GCMV MRSV OLRSV TBRV

176 138 173

D00322 (7362 nt)

X04062 (4662 nts)

103 142 301 138

X15346 (7212 nt)

X15163 (4441 nts)

X80831 (4618 nts) continued

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Comoviridae: Plant Picorna-like Viruses

Table 1 continued English vernacular name Genus Nepovirus (subgroup C) Artichoke yellow ringspot virus Blackcurrant reversion virus Blueberry leaf mottle virus Cassava green mottle virus Cherry leafroll virus Chicory yellow mottle virus Grapevine Bulgarian latent virus Hibiscus latent ringspot virus Lucerne Australian latent virus Myrobalan latent ringspot virus Peach rosette mosaic virus Potato virus U Tomato ringspot virus Tentative Genus Nepovirus Arracacha virus B Artichoke vein banding virus Cherry rasp leaf virus Cherry rosette virus Lucerne Australian symptomless virus Rubus Chinese seed-borne virus Satsuma dwarf virus Strawberry latent ringspot virus Tomato top necrosis virus
a b

Abbreviation AYRSV BRV BLMV CGMV CLRV ChYMV GBLV HLRSV LALV MLRSV PRMV PVU ToRSV

CMI/AABb 271 267 80, 306 132 186 233 225 160 150 18, 290

RNA1c

RNA2c

[U20622]

[AF020051] [U20621]

AF016626 (7977 nt) L19655 (8214 nt) D12477 (7273 nts)

AVB AVBV CRLV CRV LASV RCSV SDV SLRSV ToTNV

270 285 159

208 126

AB009958 (6795 nt)

AB009959 (5345 nts) X77466 (3824 nts) [X75165]

Type member of each genus. Number of the species description by the Association of Applied Biologists (AAB). c Sequence accession numbers for the two genomic segments; complete sequences are given with their number of nucleotides, and partial sequences of significant length between brackets.

Structure of Virus Particles

The nonenveloped capsid of Comoviridae is icosahedral, with a diameter of about 2530 nm (Table 2). It is composed of 60 subunits each made of a single coat protein (CP) subunit of about 5055 kDa in most nepoviruses, and of a large subunit (LCP) of around 3540 kDa, and a small one (SCP), of around 2025 kDa, in comoviruses and fabaviruses. However, the tridimensional fold of the capsid subunits are similar in Comoviridae and Picornaviridae, with three b-barrels, proteolytically processed or not in Comoviridae (Chen et al., 1989; Le Gall et al., 1995a; Chandrasekar and Johnson, 1998) (Figure 1). A fourth protein found inside the picornavirus capsid and encoded as the N-terminal part of the structural genes, VP4 (Figure 2), has apparently no counterpart in Comoviridae. However the N-terminus of the CP domain of Comoviridae is also folded inside the virion.

Structure of the Virus Genome and Function of Genome-encoded Proteins

The genome of Comoviridae is made of two single-stranded RNA molecules encapsidated separately (Figure 2). In addition, a proportion of the virus particles found in infected plants is usually empty. The largest RNA, RNA1, contains 60008000 nucleotides, and the smallest one, RNA2, 40007000. Both genomic RNAs are polyadenylated at their 3 end, covalently linked at their 5 end to a small (less than 5 kDa) virus-encoded protein (VPg), and translated into polyproteins processed by an RNA1encoded proteinase. The 5 noncoding region often contains a terminal stemloop, followed by a pyrimidinerich region upstream of the translation initiation codon. In some nepoviruses and fabaviruses, direct nucleotide sequence repeats are found in the 5 noncoding region.

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Comoviridae: Plant Picorna-like Viruses

Table 2 Structural features of Comoviridae, compared to those of the three related families, Picornaviridae, Potyviridae and Sequiviridae Property Virion structure Virion size (nm) Virion enveloped? Number of subunits Coat protein per subunit Subunit structure Genome nature Number of genomic segments 5 structure (kDa) 3 structure Expression strategy Genetic organisation: Structural genes Nonstructural genes Picornaviridae Icosahedral 2530 nm in diameter no 60 3 (+VP4) 3 -barrels ssRNA 1 VPg (35 kDa) Polyadenylate Polyprotein Comoviridae Icosahedral 2530 nm in diameter no 60 1 or 2 3 -barrels ssRNA 2 VPg (35 kDa) Polyadenylate Polyprotein Sequiviridae Icosahedral 2530 nm in diameter no 60 3 3 -barrels? ssRNA 1 VPg (35 kDa) Stemloop Polyprotein Potyviridae Helical 1115 5001000 nm no About 2000 1 Unknown ssRNA 12 VPg (2025 kDa) Polyadenylate Polyprotein

5 of genome 3 of RNA-2 5 of genome 3 of genome Cluster Helicase-VPg- Cluster Helicase-VPg- Cluster Helicase-VPg- Cluster Helicase-VPgProteinase-Polymerase Proteinase-Polymerase Proteinase-Polymerase Proteinase-Polymerase

In addition, some isolates of nepoviruses and of SLRSV also amplify a third RNA species, called satellite RNA, dispensable for genomic RNA replication and sharing no or very limited sequence homology with the genomic RNAs. There are two very dierent types of satellite RNAs associated with nepoviruses. Large satellite RNAs, about 1500 nucleotides in length, with a 5-VPg and a 3polyadenylate, are translated into a single peptide of about 4550 kDa, with no identied role other than allowing the replication of the satellite RNA itself (Hemmer et al., 1993). The second type consists of small molecules (about 300 nucleotides, with neither a VPg nor a polyadenylate), apparently noncoding and probably replicated using a rolling circle mechanism (for a review see Bruening, 1990). Satellite RNAs seem to be opportunistic entities taxonomically independent from their helper virus but using their replication and encapsidation functions to spread. The genomic RNAs are infectious to plants or protoplasts when mixed together. RNA1 is infectious independently of RNA2 in protoplasts but not in entire plants, and thus does encode all the virus-encoded replication proteins, but not the proteins allowing the movement of the virus throughout the infected plant. RNA2 encodes these proteins, among which is the CP. Except for Fabavirus RNA1 and subgroup C Nepovirus RNA1 and RNA2, several genomic sequences are available for both genomic RNAs of each genus or subgroup (Table 1). The complete nucleotide sequence of SLRSV RNA2 and Satsuma dwarf virus (SDV) RNA1 and RNA2, have also been determined and give some clues as to the
4

future classication of these tentative nepoviruses. The genomic organization of Comoviridae is summarized in Figure 2. The genetic structure of RNA1 is conserved among the three genera included in the Comoviridae. In regard to the RNA1-encoded P1 polyprotein (Figure 2), the domain at the N-terminus of polyprotein P1 functions as a proteinase cofactor in CPMV (Peters et al., 1992) but its function has not been determined in nepoviruses and fabaviruses. This P1a protein is poorly conserved among Comoviridae even within the same genus, but small regions of homology are present in nepoviruses and comoviruses. The next domain (P1b) represents a protein of about 60 kDa, with a conserved nucleotide-binding site and, near its C-terminus, a hydrophobic region (potential membrane-binding site). It is hypothesized to be a helicase involved in unwinding the template RNA in front of the replicase. Then follows the VPg domain (P1c, c. 35 kDa), and a proteinase domain (P1d, c. 25 kDa) responsible for the proteolytic maturation of the polyproteins. The catalytic residue of the proteinase is a cysteine, but the fold of the protein is similar to that of serine proteinases such as trypsin, with a cysteine replacing the catalytic serine. The C-terminal domain of P1 (P1e) contains sequence motifs conserved in RNA-dependent RNA-polymerases (Goldbach, 1986). The expression strategy and genetic structure of RNA2 dier slightly between the dierent genera. In comoviruses and SLRSV, RNA2 translation is initiated at two successive initiation codons in the same ribosomal reading frame, resulting in two polyproteins largely identical but diering by the presence of an N-terminal extension (P2a

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Comoviridae: Plant Picorna-like Viruses

VP

VP1
2 VP

VP1

VP1 VP3 VP2

VP3
VP2
VP3

VP1

VP1

VP2

VP

VP1

VP3

2 VP

VP1

VP3

H E F (COOH)

S L

L
L
L
S

S L S S
L

CP

CP

(NH2)

CP

CP

CP

CP

CP

CP CP

Figure 1 Compared architecture of the capsids of Picornaviridae and Comoviridae. In Picornaviridae (top), the capsid (right) is formed of 60 subunits each made of three proteins, VP1 to VP3, each folded as a single b barrel (left). In comoviruses and probably Strawberry latent ringspot virus (SLRSV) (middle), the domains corresponding to VP2 and VP3 are fused into a single protein folded in two b barrels (Chen et al., 1989; Le Gall et al., 1995a). In nepoviruses (bottom), the three domains are fused into a single coat protein (CP) folded in three b barrels (Le Gall et al., 1995a; Chandrasekar and Johnson, 1998).

and P2b for comovirus in Figure 2). In nepoviruses, there is only one polyprotein encoded by RNA2. This translational feature has not been determined for fabaviruses and SDV. The CP domain is at the C-terminal end of the P2 polyprotein in all Comoviridae, unlike the N-terminal location in the Picornaviridae polyprotein (Table 2 and Figure 2). Immediately upstream of CP is the putative movement protein domain. Where it has been investigated, the corresponding viral protein, P2b, forms tubules supposed to be involved in virus cell-to-cell movement. Another protein, P2a, is encoded by RNA2. It is produced by proteolytic cleavage from P2b in nepoviruses, and from the CP domain within the largest polyprotein in comoviruses (Figure 2). P2a is believed to be involved in RNA2 replication, perhaps by allowing the recruitment of the replication complex (van Bokhoven et al., 1993).

Processing of the polyproteins occurs at Gln-Xaa dipeptides in comoviruses, fabaviruses and SLRSV (where Xaa is a Gly, Ser, Met, Thr and sometimes Ala or other residues), a situation essentially similar to that found in Picornaviridae (Figure 3). In nepoviruses the situation is more complex: in subgroup C nepoviruses conventional Gln-Xaa dipeptides are cleaved. In subgroups A and B, as well as in SDV, the proteinase cleaves at less predictable sites, although a basic amino acid (Lys or Arg) is often, but not always, found immediately upstream of the cleavage dipeptide (Lys-Ala, Lys-Ser, Arg-Ala, Arg-Gly, but also Cys-Ala, Cys-Ser or Gly-Glu, for instance). These types of specicities correlate with the identity of a particular amino acid within the substrate-binding pocket of the proteinase, which has been identied as important for substrate recognition in Picornaviridae (Bazan and Fletterick, 1988). This amino acid is a histidine in Picornaviridae, comoviruses and subgroup C nepoviruses, as well as
5

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G D

C
L

CP

VP1

CP

VP3

VP3

CP
CP
CP
CP

VP

VP

VP1

VP2

VP

VP

CP

VP3

VP

VP3

VP2
VP3
VP2

VP1

VP3

VP2

VP1

VP2

2 VP

VP 3
VP2

VP1

VP 1
1 VP

L CP

S
L
S

S
L

CP

CP
CP

Comoviridae: Plant Picorna-like Viruses

VP3 VP1 VP4 VP2 P2a P2b Picornavirus P2a Comovirus P2bMP Fabavirus ? L S

P2c

P3bVPg P3a P3cPro

P3dPol

P1bHel P1a ?

P1cVPg P1dPro

P1ePol

SLRSV

(No data available)

SDV

A Nepovirus

C P2a P2bMP CP Structural protein(s) P1a P1bHel P1dPro P1cVPg P1ePol

Movement protein

Replication proteins

Figure 2 Genomic organization of Comoviridae, compared with that of a typical Picornavirus. The regions showing homology between the different genera and species are boxed, and the conserved nucleoside triphosphate (NTP)-binding (Helicase), Proteinase and Polymerase motifs are shown by diamonds. The VPg is indicated by a dot at the 5 end of the RNAs, and the polyadenylate by an arrowhead at the 3 end. The terminal regions conserved between both RNAs of a given virus are circled. SDV, Satsuma dwarf virus; SLRSV, Strawberry latent ringspot virus.

in Potyviridae, which all have a Gln-Xaa specicity (Figure 3). It is a leucine or a valine in subgroup A and B nepoviruses, a cysteine in SDV and a leucine in the Sequivirus Parsnip yellow eck virus (PYFV), which have other types of specicities. The exception is the proteinase of the Fabavirus BBWV2, where a tyrosine is present at this position but which cleaves Gln-Xaa dipeptides (Figure 3). As shown in Figure 2, the terminal noncoding regions show sequence similarity between the two genomic RNAs of a given virus. In subgroup B nepoviruses, the 3 noncoding regions of the genomic RNAs are identical, probably due to a template switch during RNA2 replication (Le Gall et al., 1995b). In the subgroup C nepovirus, ToRSV, both the 5 and 3 termini are strongly conserved between the two genomic RNAs, and the size of the regions involved is larger, 1140 nucleotides at the 5 end and 1546 at the 3 end (Rott et al., 1991). These conserved terminal regions extend into the 5 part of the open reading frame, so that the amino acid sequences of the N-termini of P1a and P2a are strongly conserved (Figure 2). No data is available at the 5 end for other subgroup C nepoviruses, but the extended 3 conservation has also been observed where it has been investigated, for Blueberry leaf mottle virus (BLMV) (1390 nucleotides conserved) and CLRV (about
6

1500 nucleotides conserved). Such long conserved nontranslated regions at the 3 end account for the longer RNA2 of subgroup C nepoviruses as compared with other subgroups (Table 1 and Figure 2). In SDV, a tentatively classied nepovirus (Table 1), only the 5 terminus is duplicated, over about 1000 nucleotides including the 5 part of the open reading frame (Iwanami et al., 1999) (Figure 2). These dierent patterns of conservation of the genomic RNA terminal sequences between the genera and subgroups of Comoviridae probably reect slightly dierent properties of their replication machineries.

Relationships with Other Families

The Comoviridae, the Potyviridae and the Picornaviridae share similarities in their genomic organizations, with a 3polyadenylate, a 5-VPg, a unique open reading frame cleaved by a viral proteinase, with functional domains of genome-encoded polyproteins organized in the same order (nucleoside triphosphate (NTP)-binding/helicase-VPgproteinase-polymerase) and with sequence homologies (Figure 2 for Comoviridae and Picornaviridae). These

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Comoviridae: Plant Picorna-like Viruses

Virus Picornaviridae PV2 Potyviridae PVY Sequiviridae PYFV Comovirus BPMV CPMV RCMV CPSMV Fabavirus BBWV2 Nepovirus A GFLV TRSV Nepovirus B GCMV BRSV Nepovirus C ToRSV PRMV

Substrate binding pocket M Y N F P T R A G Q C G G V I T C T G K V I GMH V G G N G S H G F K HW I E T DNG H C G L P V V S T A D G C I V G I H S L A NN A H T T N S S P F K T E DGQCG S C L V S T S D K L DG K V F C S L V A G T Y D R V T G E E R Q Y Y Y Y D E E D A A A V C P P S T T T T I P ND I P E D VMS D K A E D C C C C G G G G S S S S L V L V M I L I V I I I A A T A K H N T V I V I GNH GGK GGK DGR KQ HK T K K K I I I I V V V I G G G G F V I I H H H H V V V T A A A A G G G G S I R R KG QG DN AN R K K R L I I S G Y GC GM G F

Cleavage Gln-Xaa Gln-Xaa other Gln-Xaa Gln-Xaa Gln-Xaa Gln-Xaa Gln-Xaa other other other other Gln-Xaa Gln-Xaa other

S Y E A S T V A G D C G S L I L A E I D G K F K L V GMY V A F N G R E G S V Y A H E A K K Y DCG A L A V A V I QG I P K V I AML V S GN R G V T Y Q Y G R P DQ L HDCG A I C V A K I GGQH R I V G L V I S T D K HN T G V V F H Y E S R NN D C GM L L T C Q L S G K M K V V GM L V A G K D K T S W T F H Y E S R N D D C GM I I L C Q I K G K M R V V GM L V A G K D K T S W I S E Y V N S P E D C G A L L V A H L E G G Y K I I GMH V A G S S Y P V E V T S S Y A A G V HDCGG L I S I L HQG R R K V V G L H V A G T R V GH L F

Tentative Nepovirus SDV Y A D G P A L N G H C G R L L C A N L A G HW R V I GMC A G E G K N R A G V

Figure 3 Alignment of the amino acid sequences around the catalytic cysteine of the proteinase of various Comoviridae, of the picornavirus poliovirus 2 (PV2), of the potyvirus potato virus Y (PVY) and of the sequivirus Parsnip yellow fleck virus (PYFV). The one-letter amino acid code is used in the alignment. The catalytic cysteine is shown in bold and red, as is a conserved histidine found 18 amino acids downstream in some Comoviridae and 14 and 16 amino acids downstream for PV2 and PVY, respectively. The cleavage specificity is indicated at the right (Gln-Xaa or Other when other types of dipeptides are cleaved, as described in the text). BBWV2, Broad bean wilt virus 2; BPMV, Bean pod mottle virus; BRSV, Beet ringspot virus; CPMV, Cowpea mosaic virus; CPSMV, Cowpea severe mosaic virus; GCMV, Grapevine chrome mosaic virus; GFLV, Grapevine fanleaf virus; PRMV, Peach rosette mosaic virus; RCMV, Red clover mottle virus; SDV, Satsuma dwarf virus; ToRSV, Tomato ringspot virus; TRSV, Tobacco ringspot virus.

observations have led Goldbach (1986) to propose the creation of the supergroup of plant Picorna-like viruses. More recently, the genetic organization of Sequiviridae has been elucidated and found to be similar (Turnbull-Ross et al., 1993). Table 2 lists the similarities and dissimilarities between Picornaviridae, Comoviridae, Sequiviridae and Potyviridae. As compared to a general scheme, Comoviridae dier essentially in having a divided genome, Sequiviridae in having a stemloop structure rather than a polyadenylate at the 3 end of their genome, and Potyviridae in having a helical virion symmetry and a somewhat larger VPg. The position of the structural protein(s) along the polyprotein varies according to these dierent families, either at the Nor at the C-terminus of the polyprotein.

Pathogenesis
Comoviruses usually have a relatively narrow host range, often within the family Fabacae. Fabaviruses have a wider

host range, including both monocotyledons and dicotyledons. The width of the host range of nepoviruses diers from very narrow to wide according to the individual species considered. In the eld, the range of plants infected by nepoviruses is often restricted by the host range of their nematode vector, as in the case of the subgroup A member, GFLV (Table 1). This virus is transmitted by a nematode, Xiphinema index, that is restricted to grapevine, Vitis sp., and g tree, Ficus sp., but GFLV does not infect the g tree. Comoviridae often induce mottle, mosaic, distortion and apical necrosis. Ringspots are characteristic of nepoviruses and fabaviruses, but not of comoviruses. Plants infected with nepoviruses often show a recovery phenomenon: the newly developing leaves cease, within a few weeks after inoculation, to display any symptoms, and accumulate lower amounts of virus than earlier developing leaves did. This long-known phenomenon has recently been correlated with a silencing-based host defence mechanism (Ratcli et al., 1997).

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Comoviridae: Plant Picorna-like Viruses

Transmission and Epidemiology

Many members of the family Comoviridae are seedtransmitted. Comoviruses are transmitted by coleoptera, mostly of the family Chrysomelidae. Fabaviruses are transmitted by aphids. Some nepoviruses have no known animal vector, but are pollen-transmitted. Of the nepoviruses transmitted by vectors, most are transmitted by soil nematodes of the family Longidoridae (Longidorus spp. or Xiphinema spp.), often with a very tight specicity. Some cases of transmission of nepoviruses by arthropods have been described: besides the nematode Xiphinema americanum, TRSV can be transmitted by Thrips tabaci and grasshoppers (Messieha, 1969, and references therein), and the natural vector of Blackcurrent reversion virus (BRV) is the eriophyid mite Cecidophyopsis ribis (Lemetty et al., 1997). The mode of virus transmission has a direct eect on distribution of diseased plants in the environment. Nematode-transmitted viruses often occur as clusters of diseased plants in the eld, corresponding to an area where viruliferous nematodes are present. These clusters sometimes slide year after year down the natural slopes, reecting the eect of the rain waters on the otherwise relatively poorly mobile soil nematodes. In any case, plant contamination by the soil occurs between neighbours, but cannot cross obstacles such as ditches or other soil discontinuities. In contrast, viruses transmitted by insect or pollen contaminate plants at larger distances. Seedtransmitted viruses, and those infecting woody plants propagated vegetatively, are prone to extremely longdistance transport, aided by human economic exchanges of planting material.

References
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Control
The control of seed-transmitted Comoviridae is mostly performed by control of the commercial seed lots and certication. The same is true for viruses infecting vegetatively propagated crops. The detection is currently based on graft-inoculation of control plants, or on immunological techniques such as enzyme-linked immunosorbent assay (ELISA). Nematode-transmitted nepoviruses can also be controlled by nematicidal soil treatments. However, the negative impact of the use of chemicals as toxic as methyl bromide in complex ecosystems is now a very strong concern, and this practice is rapidly becoming less and less acceptable as well as increasingly regulated. Biotechnologies (transgenic plants, most of them expressing the viral CP) have recently been developed to control several nepoviruses. These approaches could help controlling nepoviruses when soil fumigations are no longer authorized.
8

Further Reading
Adams MJ, Antoniw JF, Barker H et al. (1998) Description of Plant Viruses on CD-ROM. Wellesbourne, Warwick, UK: Association of Applied Biologists. Goldbach RW, Martelli GP and Milne RG (1995) Comoviridae. In: Murphy FA, Fauquet CM, Bishop DHL et al. (eds) Virus Taxonomy: the Classication and Nomenclature of Viruses. The Sixth Report of the International Committee on Taxonomy of Viruses, pp. 341347. Vienna: Springer.

ENCYCLOPEDIA OF LIFE SCIENCES / & 2001 Nature Publishing Group / www.els.net

Comoviridae: Plant Picorna-like Viruses

Virology Division of the International Union of Microbiological Societies (1999) International Committee for the Taxonomy of Viruses. [http://www.ncbi.nlm.nih.gov/ICTV/] Bu chen-Osmond C (1999) Virus databases on-line. Canberra, Australia: Research School of Biological Sciences (RSBS), Australian National University. [http://life.anu.edu.au/viruses/welcome.htm]

Bu chen-Osmond C (1998) Comoviridae. Canberra, Australia: Research School of Biological Sciences (RSBS), Australian National University. [http://life.anu.edu.au/viruses/ICTVdB/18000000.htm]

ENCYCLOPEDIA OF LIFE SCIENCES / & 2001 Nature Publishing Group / www.els.net