Equine rhinovirus serotypes 1 and 2: relationship to each other and to aphthoviruses and cardioviruses

Wutz, Gordana; Auer, Herbert; Nowotny, Norbert; Grosse, B.; Skern, Tim; Kuechler, Ernst

doi:10.1099/0022-1317-77-8-1719

Cited by 92 publications

(118 citation statements)

References 30 publications

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“…As the initiation of protein synthesis can take place at one of two AUG codons in FMDV and ERV1 (Sangar et al, 1987 ;Wutz et al, 1996), two forms of the L protein can be synthesized, the longer Lab and the shorter Lb form. As there is evidence that the Lb form is the biologically relevant one (Cao et al, 1995), it is this form of FMDV and ERV1 which is used in these studies.…”

Section: Resultsmentioning

confidence: 99%

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A structural model of picornavirus leader proteinases based on papain and bleomycin hydrolase.

Skern

Fita

Guarné³

1998

Journal of General Virology

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The leader (L) proteinases of aphthoviruses (footand-mouth disease viruses) and equine rhinovirus serotypes 1 and 2 cleave themselves from the growing polyprotein. This cleavage occurs intramolecularly between the C terminus of the L proteinases and the N terminus of the subsequent protein VP4. The foot-and-mouth disease virus enzyme has been shown, in addition, to cleave at least one cellular protein, the eukaryotic initiation factor 4G. Mechanistically, inhibitor studies and sequence analysis have been used to classify the L proteinases as papain-like cysteine proteinases. However, sequence identity within the L proteinases themselves is low (between 18 % and 32 %) and only 14 % between the L proteinases and papain. Secondary structure predictions, sequence alignments that take into account the positions of the essential

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Section: Resultsmentioning

confidence: 99%

“…Recent investigation of the genome structure of ERV serotypes 1 and 2 revealed that these viruses also possess an L proteinase of the FMDV type. However, sequence identity between all three viral proteinases is only between 18 % and 32 % (Wutz et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

A structural model of picornavirus leader proteinases based on papain and bleomycin hydrolase.

Skern

Fita

Guarné³

1998

Journal of General Virology

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“…They are, therefore, also likely to elicit antibodies. Direct comparison of the known structure of FMDV VP1 with that predicted for ERAV VP1 (Wutz et al, 1996) shows that most of the predicted loops of ERAV VP1 are larger than those of FMDV. In particular, the bE-bF loop of ERAV, which contains a strong B cell epitope, is more than double the size of that in FMDV (32 compared to 14 aa in FMDV) and in the case of FMDV is not reported to contain any antigenic sites.…”

mentioning

confidence: 99%

mentioning

confidence: 99%

“…ERAV is classified with foot-and-mouth disease virus (FMDV), albeit as a separate cluster, in the genus Aphthovirus, family Picornaviridae. ERAV shares many physico-chemical and biological properties with FMDV and the genome structures and sequences of the two viruses are also similar (Li et al, 1996;Newman et al, 1973;Plummer, 1963;Studdert & Gleeson, 1978;Wutz et al, 1996).Picornavirus capsid proteins VP1, VP2 and VP3 share structural homology and are composed of wedge-shaped, eight-stranded, b-barrels, which differ in the size and conformation of the connecting loops between their strands and the extensions of their N-and C-termini (Rueckert, 2001). The amino acid sequences of the loops that connect the b-strands and the N-and C-terminal regions that extend from the b-barrel domain give each picornavirus its distinct morphology and antigenicity (Mateu, 1995;Rueckert, 2001).…”

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Mapping epitopes in equine rhinitis A virus VP1 recognized by antibodies elicited in response to infection of the natural host

Stevenson

Hartley

Huang

et al. 2003

Journal of General Virology

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Equine rhinitis A virus (ERAV) is an important respiratory pathogen of horses and is of additional interest because of its close relationship and common classification with foot-and-mouth disease virus (FMDV). As is the case with FMDV, the VP1 capsid protein of ERAV has been shown to be a target of neutralizing antibodies. In FMDV VP1, such antibodies commonly recognize linear epitopes present in the bG-bH loop region. To map linear B cell epitopes in ERAV VP1, overlapping fragments spanning its length were expressed in Escherichia coli as glutathione S-transferase (GST) fusion proteins. These fusion proteins were tested for reactivity with sera from ERAV-infected horses and with polyclonal sera from ERAV-immunized rabbits and mice. Regions at the N-and C-termini as well as the bE-bF and the bG-bH loop regions contained B cell epitopes that elicited antibodies in the natural host. GST fusion proteins of these regions also elicited antibodies following immunization of rabbits and mice, which, in general, strongly recognized native ERAV VP1 but which were non-neutralizing. It is concluded that the N-terminal region of ERAV VP1, in particular, contains strong B cell epitopes.Equine rhinitis A virus (ERAV) is an important respiratory pathogen of horses. Disease is characterized by fever (41±0?5˚C) and clinical signs that include nasal discharge, coughing, anorexia, pharyngitis and lymphadenitis (Plummer, 1962). ERAV is classified with foot-and-mouth disease virus (FMDV), albeit as a separate cluster, in the genus Aphthovirus, family Picornaviridae. ERAV shares many physico-chemical and biological properties with FMDV and the genome structures and sequences of the two viruses are also similar (Li et al., 1996;Newman et al., 1973;Plummer, 1963;Studdert & Gleeson, 1978;Wutz et al., 1996).Picornavirus capsid proteins VP1, VP2 and VP3 share structural homology and are composed of wedge-shaped, eight-stranded, b-barrels, which differ in the size and conformation of the connecting loops between their strands and the extensions of their N-and C-termini (Rueckert, 2001). The amino acid sequences of the loops that connect the b-strands and the N-and C-terminal regions that extend from the b-barrel domain give each picornavirus its distinct morphology and antigenicity (Mateu, 1995;Rueckert, 2001). For example, the surface loops of VP1, VP2 and VP3 of poliovirus type 1 (PV-1) and human rhinovirus type 14 capsid structures protrude from the virion surface to form the receptor-binding canyon, as well as the major antigenic sites of these viruses. In comparison, the VP1 protein within the relatively smooth surface of FMDV particles contains a linear peptide, the bG-bH loop, which is both the dominant neutralization epitope and is also involved in receptor binding to various integrins via an RGD motif (Berinstein et al., 1995;Danen et al., 1995;Jackson et al., 2000;Mateu et al., 1995;Stanway, 1990;Strohmaier et al., 1982).In marked contrast to FMDV and human rhinoviruses, the predicted amino acid sequence of ERAV P1 and, in particu...

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Picornaviruses

Rowlands¹

2010

Encyclopedia of Life Sciences

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The name picornavirus is derived from pico for small and ribonucleic acid (RNA), denoting the chemical nature of the genome. Virions are nonenveloped icosahedral particles approximately 30 nM in diameter. The capsid is constructed from 60 copies of each of four structural proteins which account for 70% of the particle mass and enclose the single‐strand genome of 7500–8500 nucleotides. The positive strand genome acts directly as a messenger RNA to template a single polyprotein product. This is subsequently processed by virally encoded proteases into mature active proteins. Several intermediate products have distinct functions to the final fully processed proteins. Replication of the genome is initiated by an uridylated peptide and proceeds via a negative strand intermediate template. Picornaviruses are among the smallest pathogens of vertebrates and are responsible for many important diseases in humans and animals. Key Concepts: There are effective vaccines against polio, hepatitis A and foot‐and‐mouth disease viruses. In addition, movement control and slaughter is used to control foot‐and‐mouth disease. There are no licensed drugs for picornavirus infections. Genome sequence comparisons have replaced biological and biophysical comparisons as the bases for classification within the family. Picornavirus particles comprise 60 copies each of 4 structural proteins, which form a quasi T1 icosohedral capsid encasing the single strand RNA genome. The picornavirus RNA genome functions as a messenger RNA to template the synthesis of a single polyprotein, which is posttranslationally processed by viral proteases. Picornaviruses bind to cell specific surface receptors and this interaction is an important factor in determining host and tissue specificity of each virus. Picornaviruses cannot gain entry to cells by membrane fusion, as is the case for enveloped viruses, and require special mechanisms to breach cellular membranes and safely deliver the genome into the host cell. Genome replication occurs in association with virus modified cellular membranes. Viral RNA templates complementary negative strand molecules which in turn template multiple positive strand copies. The synthesis of all RNA molecules is initiated by an uridylated peptide primer. The mechanisms of transmission of infection play key roles in the epidemiology of picornavirus infections. Picornaviruses are responsible for a wide range of clinical diseases resulting from multiple factors such as receptor specificity, tissue‐specific susceptibility, virulence and the mechanisms of transmission.

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Equine rhinovirus serotypes 1 and 2: relationship to each other and to aphthoviruses and cardioviruses

Cited by 92 publications

References 30 publications

A structural model of picornavirus leader proteinases based on papain and bleomycin hydrolase.

A structural model of picornavirus leader proteinases based on papain and bleomycin hydrolase.

Mapping epitopes in equine rhinitis A virus VP1 recognized by antibodies elicited in response to infection of the natural host

Picornaviruses

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