Antigenic regions of poliovirus type 3/sabin capsid proteins recognized by human sera in the peptide scanning technique

Roivainen, Merja; Närvänen, Ale; Korkolainen, Mirja; Huhtala, Marja-Liisa; Hovi, Tapani

doi:10.1016/0042-6822(91)90013-2

Cited by 64 publications

(49 citation statements)

References 16 publications

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“…B-cell epitopes of picornaviruses have been studied by using synthetic peptides, peptide scanning, and neutralization escape mutants. In polioviruses, coxsackie A virus type 9 and CBV4, and human rhinovirus type 14, the major antigenic regions are mostly concentrated in the capsid protein VP1, whereas VP2 and VP3 are less involved in the antigenic structures (15,16,17,18,20). In this light, the VP1 protein of HPEV1 was surprisingly poorly immunogenic in immunoblotting and in EIA, although it induced neutralizing antibodies in rabbits.…”

Section: Discussionmentioning

confidence: 99%

Diagnostic Potential of Parechovirus Capsid Proteins

et al. 2003

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To study humoral and cellular immunity against human parechovirus type 1 (HPEV1), the viral capsid proteins VP0, VP1, and VP3 were expressed and purified as glutathione S-transferase (GST)-tagged recombinant proteins. The fusion proteins were used to raise antisera in rabbits. VP0 and VP1 antisera specifically detected HPEV1-infected cells in culture by immunoperoxidase staining and immunofluorescence. Furthermore, antisera against the VP0 and VP1 proteins had neutralizing effects against HPEV1 infection. When the HPEV1 antibody titers of 20 adults and 55 children were determined by a microneutralization test, the prevalence of HPEV1 antibodies in the adult population was 96%, while 50% of children were seropositive. Selected sera were used to evaluate HPEV1 fusion proteins as antigens in an enzyme immunoassay. The VP3 capsid protein appeared to be suitable for the purpose, with specificity of 100% and sensitivity of 96% compared to the neutralization test. Furthermore, T-cell responses to the purified HPEV1 and HPEV1 capsid fusion proteins were studied in 20 adults. Sixty percent of the subjects had T-cell proliferation responses to purified HPEV1, and 90% of the subjects also had positive T-cell responses to at least one of the GST capsid proteins.Human parechovirus type 1 (HPEV1), the type member of the genus Parechovirus, is a common pathogen with a worldwide distribution (5, 9). Infections occur early in life, and seropositivity increases rapidly after 1 year of age. The most common clinical manifestations are gastroenteritis and respiratory infections, while central nervous system symptoms are more rare than in enterovirus infections. Parechoviruses form one of the nine genera in the family Picornaviridae and include two human pathogens, HPEV1 and HPEV2, and a rodent virus, Ljungan virus (12). Like other picornaviruses, parechoviruses are small nonenveloped particles containing an RNA genome with positive polarity and a protein capsid consisting of 60 copies of each of the capsid proteins VP1 to VP4 (8). However, parechoviruses have distinctive molecular properties compared to other picornaviruses, including differences in capsid protein processing (VP0 is not cleaved to VP2 and VP4) and functions of the nonstructural proteins (3,7,21).B-cell antigenic epitopes of some picornaviruses, like polioviruses and rhinoviruses, are relatively well known (22). The major antigenic sites in polioviruses exist in VP1 and, to a lesser extent, in VP2 and VP3 (15). There is a linear epitope in VP1, while amino acids participating in two conformational epitopes are scattered along the capsid proteins. It has been shown by using rabbit antibodies and synthetic peptides that in HPEV1 one immunogenic region resides in VP0 and another resides at the C terminus of VP1 (10). The latter region contains an RGD motif which participates in recognition of ␣V␤3 integrin on the host cell surface (21).Cellular immunity and T-cell epitopes of enteroviruses, like coxsackie B viruses (CBV) and polioviruses, have been studied by proliferat...

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Section: Discussionmentioning

confidence: 99%

Diagnostic Potential of Parechovirus Capsid Proteins

et al. 2003

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“…Entero-and adenovirus antibody analyses. IgG and IgA class antibodies against purified Coxackievirus B4 (CVB4), purified echovirus 11 (EV11), and a synthetic enterovirus peptide antigen (sequence KEVPALTAVETGAT-C derived from an immunodominant region of capsid protein VP1 [12], which is a common epitope for several enteroviruses [13]) were measured using enzyme immunoassay (EIA) as described (3,14). The purified CVB4 and EV11 were incubated at 56°C for 15 min to expose antigenic determinants common for various enterovirus serotypes.…”

Section: Lönnrot and Associatesmentioning

confidence: 99%

Enterovirus infection as a risk factor for beta-cell autoimmunity in a prospectively observed birth cohort: the Finnish Diabetes Prediction and Prevention Study.

et al. 2000

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Previous studies suggest that enterovirus infections may initiate and accelerate ␤-cell damage years before the clinical manifestation of type 1 diabetes. We have now analyzed the role of enterovirus infections in the initiation of autoimmunity in children who have tested positive for diabetes-associated autoantibodies in a prospective study starting at birth (the Finnish Diabetes Prediction and Prevention Study). The frequency of enterovirus infections was studied using both serology and testing for the presence of enterovirus RNA in the sera of 21 children who developed and retained autoantibodies and in 104 control subjects chosen from the same study cohort and matched for the time of birth, sex, and HLA alleles determining genetic diabetes susceptibility. Sample intervals were taken as basic units of follow-up, to which the observed number of infections was adjusted. Enterovirus infections were detected in 26% of sample intervals in the case subjects and in 18% of the sample intervals in the control children (P = 0.03). A temporal relationship between enterovirus infections and the induction of autoimmunity was found; enterovirus infections were detected in 57% of the case subjects during a 6-month follow-up period preceding the first appearance of autoantibodies compared with 31% of the matched control children in the same agegroup (odds ratio 3.7, 95% CI 1.2-11.4). The frequency of adenovirus infections did not differ between the patient and control groups. Our data imply that enterovirus infections are associated with the development of ␤-cell autoimmunity and provide evidence for the role of enteroviruses in the initiation of ␤-cell destruction. Diabetes 49:1314-1318, 2000 T he etiology of type 1 diabetes comprises both genetic and environmental components. Enterovirus infections have long been suspected as potential environmental factors playing a role in the pathogenesis of type 1 diabetes (1,2). Recent prospective studies, based on enterovirus serology (3-5) and detection of enterovirus RNA in sera of prediabetic children (6), suggest that enterovirus infections may initiate and accelerate the ␤-cell-damaging process years before the clinical manifestation of type 1 diabetes. Enterovirus RNA has also been detected more frequently in patients with newly diagnosed type 1 diabetes than in healthy control subjects (7-9).Clear signs of ␤-cell damage often appear months or years before the manifestation of clinical diabetes (10), suggesting that prospective studies starting before the appearance of autoantibodies may be helpful in studying the etiology of the disease. In addition, early recognition of the individuals with ongoing ␤-cell damage may make it possibile to delay or halt ␤-cell destruction. The Finnish Diabetes Prediction and Prevention (DIPP) Study is a prospective population-based birth-cohort study in which Finnish children with increased genetic risk for type 1 diabetes are studied for the appearance of diabetes-associated autoantibodies at 3-to 12-month intervals from birth. We have now stud...

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“…The relevance of the immune response to the VP1 N terminus for host protection against poliovirus has been pointed out by in vitro studies of viral neutralization using synthetic peptides (9). In addition, this region is immunogenic in humans vaccinated with an attenuated (Sabin) poliovirus vaccine (43), in rabbits inoculated with CVA9 (42), and in SVDV infected pigs (24). The substituted residue S1045 maps to this region (Table 2).…”

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confidence: 99%

Structure of Swine Vesicular Disease Virus: Mapping of Changes Occurring during Adaptation of Human Coxsackie B5 Virus To Infect Swine

Verdaguer

Jiménez‐Clavero

Fita

et al. 2003

J Virol

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The structure of swine vesicular disease virus (SVDV) was solved and refined at a 3.0-Å resolution by X-ray crystallography to gain information about the role of sequence changes that occurred as this virus evolved from the parental human pathogen coxsackievirus B5 (CVB5). These amino acid substitutions can be clustered in five distinct regions: (i) the antigenic sites, (ii) the hydrophobic pocket of the VP1 ␤-sandwich, (iii) the putative CAR binding site, (iv) the putative heparan sulfate binding site, and (v) the fivefold axis. The VP1 pocket is occupied by a branched pocket factor, apparently different from that present in the closely related virus CVB3 and in other picornaviruses. This finding may be relevant for the design of new antiviral compounds against this site. Density consistent with the presence of ions was observed on the fivefold and threefold axes. The structure also provided an accurate description of the putative receptor binding sites.

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Antigenic regions of poliovirus type 3/sabin capsid proteins recognized by human sera in the peptide scanning technique

Cited by 64 publications

References 16 publications

Diagnostic Potential of Parechovirus Capsid Proteins

Diagnostic Potential of Parechovirus Capsid Proteins

Enterovirus infection as a risk factor for beta-cell autoimmunity in a prospectively observed birth cohort: the Finnish Diabetes Prediction and Prevention Study.

Structure of Swine Vesicular Disease Virus: Mapping of Changes Occurring during Adaptation of Human Coxsackie B5 Virus To Infect Swine

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