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1.
Viral Immunol ; 15(4): 549-56, 2002.
Artículo en Inglés | MEDLINE | ID: mdl-12513926

RESUMEN

An experimental model was used to investigate mRNA cytokine profiles in bronchoalvolar cells (BALC) from piglets, infected in utero with porcine reproductive and respiratory syndrome virus (PRRSV). The BALC's were analyzed for the cytokines TNF-alpha, IFN-gamma, IL-8, IL-10, and IL-12(p40) by real-time TaqMan polymerase chain reaction in 2-, 4-, and 6-week-old piglets, respectively. High levels of IFN-gamma mRNA was detected in all piglets, while IL-10 was upregulated in 2-week-old piglets, was at normal levels in 4-week-old piglets, and elevated again in 6-week-old piglets. IL-12 was weakly elevated in all three age groups. Virus was reduced by 50% in 4-week-old piglets and cleared by 6 weeks of age. The sustained expression of IFNgamma and reduction of IL-10 production indicate an important role for these cytokines in immunity to PRRSV.


Asunto(s)
Líquido del Lavado Bronquioalveolar/citología , Citocinas/metabolismo , Síndrome Respiratorio y de la Reproducción Porcina/inmunología , Virus del Síndrome Respiratorio y Reproductivo Porcino/inmunología , ARN Mensajero/metabolismo , Animales , Femenino , Transmisión Vertical de Enfermedad Infecciosa , Interferón gamma/metabolismo , Interleucina-10/metabolismo , Síndrome Respiratorio y de la Reproducción Porcina/transmisión , Síndrome Respiratorio y de la Reproducción Porcina/virología , Embarazo , Porcinos
2.
Vaccine ; 19(27): 3661-70, 2001 Jun 14.
Artículo en Inglés | MEDLINE | ID: mdl-11395200

RESUMEN

A vaccine based upon a recombinant plant virus (CPMV-PARVO1), displaying a peptide derived from the VP2 capsid protein of canine parvovirus (CPV), has previously been described. To date, studies with the vaccine have utilized viable plant chimaeric particles (CVPs). In this study, CPMV-PARVO1 was inactivated by UV treatment to remove the possibility of replication of the recombinant plant virus in a plant host after manufacture of the vaccine. We show that the inactivated CVP is able to protect dogs from a lethal challenge with CPV following parenteral immunization with the vaccine. Dogs immunized with the inactivated CPMV-PARVO1 in adjuvant displayed no clinical signs of disease and shedding of CPV in faeces was limited following CPV challenge. All immunized dogs elicited high titres of peptide-specific antibody, which neutralized CPV in vitro. Levels of protection, virus shedding and VP2-specific antibody were comparable to those seen in dogs immunized with the same VP2- peptide coupled to keyhole limpet hemocyanin (KLH). Since plant virus-derived vaccines have the potential for cost-effective manufacture and are not known to replicate in mammalian cells, they represent a viable alternative to current replicating vaccine vectors for development of both human and veterinary vaccines.


Asunto(s)
Comovirus/inmunología , Infecciones por Parvoviridae/prevención & control , Parvovirus Canino/inmunología , Proteínas Recombinantes/uso terapéutico , Proteínas Virales/uso terapéutico , Vacunas Virales/uso terapéutico , Secuencia de Aminoácidos , Animales , Cápside/uso terapéutico , Proteínas de la Cápside , Comovirus/efectos de la radiación , Enfermedades de los Perros/prevención & control , Enfermedades de los Perros/virología , Perros , Esquemas de Inmunización , Datos de Secuencia Molecular , Infecciones por Parvoviridae/mortalidad , Infecciones por Parvoviridae/veterinaria , Parvovirus Canino/efectos de la radiación , Rayos Ultravioleta , Vacunas de Productos Inactivados/uso terapéutico , Vacunas Sintéticas/uso terapéutico
3.
Vet Microbiol ; 78(4): 353-62, 2001 Feb 26.
Artículo en Inglés | MEDLINE | ID: mdl-11182501

RESUMEN

Exposure to bacterial DNA generates a "danger signal" that stimulates cellular elements of the mammalian immune system to proliferate and/or secrete cytokines. Stimulation is critically dependent on hexameric motifs that contain an unmethylated CpG dinucleotide: these are commonly found in bacterial but not vertebrate DNA. Different motifs are optimally stimulatory in different species. This work examines whether oligodeoxynucleotides (ODNs) containing CpG motifs stimulate peripheral blood mononuclear cells from pigs. Results show that pigs respond to CpG ODN by proliferating and secreting IL-6, IL-12 and TNF-alpha. By screening a large panel (>100) of ODNs, the palindromic hexamer 'ATCGAT' was identified as being optimally active in all animals examined (N=10). These findings are the first to establish the immunostimulatory activity of CpG ODN in pigs, and suggest that the therapeutic uses envisioned for these ODNs (as vaccine adjuvants and immunoprotective agents) may be applicable to husbandry animals.


Asunto(s)
Islas de CpG/inmunología , Leucocitos Mononucleares/inmunología , Oligonucleótidos/inmunología , Porcinos Enanos/inmunología , Adyuvantes Inmunológicos/genética , Adyuvantes Inmunológicos/farmacología , Animales , Citocinas/biosíntesis , Citocinas/genética , Metilación de ADN , Repeticiones de Dinucleótido/inmunología , Oligonucleótidos/farmacología , ARN Mensajero/biosíntesis , ARN Mensajero/genética , Porcinos , Porcinos Enanos/sangre
5.
Vaccine ; 18(21): 2244-9, 2000 Apr 28.
Artículo en Inglés | MEDLINE | ID: mdl-10717344

RESUMEN

Immunisation against pathogens remains one of the most effective ways of preventing or reducing losses due to infectious diseases in animal husbandry. When inactivated vaccines are used, adjuvants are most often required to obtain satisfactory immune responses. One such type of adjuvant is saponin derived from the bark of Quillaja saponaria Molina, a tree of the rose family. A few different commercial sources exist, but due to the structural complexity and heterogeneity of these saponin preparations, it has been difficult to establish exactly which components are responsible for the adjuvant activity. By carefully selecting the bark source, we have succeeded in preparing a much less heterogeneous preparation of quillaja saponin. In this report we describe the preparation, in terms of structural complexity, hemolytic activity, adjuvant activity, and its ability to form ISCOM matrix. This new preparation could have implications for use per se, or as starting material for more effective preparation of pure substances.


Asunto(s)
Adyuvantes Inmunológicos/aislamiento & purificación , Plantas Medicinales/química , Saponinas/aislamiento & purificación , Animales , Cromatografía Líquida de Alta Presión , ISCOMs/aislamiento & purificación , ISCOMs/farmacología , Ratones , Saponinas de Quillaja , Saponinas/farmacología , Ovinos
6.
Virology ; 267(2): 135-40, 2000 Feb 15.
Artículo en Inglés | MEDLINE | ID: mdl-10662609

RESUMEN

By using porcine immune sera to select a library of phage-displayed random peptides, we identified an antigenic sequence (RKASLSTS) in the C-terminus of the ORF 3 structural glycoprotein of European-type porcine reproductive and respiratory syndrome virus (PRRSV). Through the use of overlapping reading frames, the same PRRSV genetic locus codes for the ORF 3 "RKASLSTS" sequence, and a previously described ORF 4 epitope (Meulenberg, J. J. M., Van Nieuwstadt, A. P., Van Essen-Zandbergen, A., and Langeveld, J. P. M., 1997, J. Virol. 71, 6061-6067). Sequence analysis identified naturally occurring deletion mutants at this ORF 34 site. Phylogenetic analysis showed the presence of a highly accurate ORF 3 molecular clock, according to which deletion mutants and nondeleted viruses evolved at differing speeds. Furthermore, deletion mutants and nondeleted viruses evolved as separate lineages. These distinctions suggested that deletion mutants were a hitherto unrecognized subtype of European-type PRRSV. Currently, deletion mutants appear to be outcompeting nondeleted viruses in the field, highlighting the importance of the porcine antibody response against the minor structural glycoproteins of European-type PRRSV for viral evolution.


Asunto(s)
Virus del Síndrome Respiratorio y Reproductivo Porcino/genética , Secuencia de Aminoácidos , Animales , Anticuerpos Antivirales/inmunología , Epítopos , Datos de Secuencia Molecular , Mutación , Sistemas de Lectura Abierta/genética , Sistemas de Lectura Abierta/inmunología , Filogenia , Virus del Síndrome Respiratorio y Reproductivo Porcino/química , Virus del Síndrome Respiratorio y Reproductivo Porcino/inmunología , Alineación de Secuencia , Análisis de Secuencia de ADN , Eliminación de Secuencia , Homología de Secuencia de Aminoácido , Porcinos , Proteínas Estructurales Virales/genética , Proteínas Estructurales Virales/inmunología
7.
Dev Biol (Basel) ; 104: 45-51, 2000.
Artículo en Inglés | MEDLINE | ID: mdl-11713823

RESUMEN

DNA technology has facilitated the development of plasmid-based vaccines designed to prevent viral, bacterial and parasitic infections. The rapid transition of these novel vaccines from the laboratory to the clinic raises important safety concerns. Our review examines whether DNA vaccines (i) are likely to induce systemic or organ-specific auto-immune disease and (ii) have the potential to induce tolerance rather than immunity.


Asunto(s)
Autoinmunidad , Tolerancia Inmunológica , Vacunas de ADN/inmunología , Vacunas de ADN/farmacología , Animales , Animales Recién Nacidos , Anticuerpos Antinucleares/biosíntesis , Linfocitos B/inmunología , Infecciones Bacterianas/inmunología , Infecciones Bacterianas/prevención & control , Humanos , Activación de Linfocitos , Ratones , Especificidad de Órganos , Enfermedades Parasitarias/inmunología , Enfermedades Parasitarias/prevención & control , Seguridad , Virosis/inmunología , Virosis/prevención & control
8.
Virology ; 263(1): 89-99, 1999 Oct 10.
Artículo en Inglés | MEDLINE | ID: mdl-10544085

RESUMEN

An antigen-delivery system based on hybrid virus-like particles (VLPs) formed by the self-assembly of the capsid VP2 protein of canine parvovirus (CPV) and expressing foreign peptides was investigated. In this report, we have studied the effects of inserting the poliovirus C3:B epitope in the four loops and the C terminus of the CPV VP2 on the particle structure and immunogenicity. Epitope insertions in the four loops allowed the recovery of capsids in all of the mutants. However, only insertions of the C3:B epitope in VP2 residue 225 of the loop 2 were able to elicit a significant anti-peptide antibody response, but not poliovirus-neutralizing antibodies, probably because residue 225 is located in an small depression of the surface. To fine modulate the insertion site in loop 2, a cassette-mutagenesis was carried out to insert the epitope in adjacent positions 226, 227, and 228. The epitope C3:B inserted into these positions was well recognized by the specific monoclonal antibody C3 by immunoelectron microscopy. BALB/c mice immunized with these chimeric C3:B CPV:VLPs were able to elicit an strong neutralizing antibody response (>3 log(10) units) against poliovirus type 1 (Mahoney strain). Therefore, minor displacements in the insertion place cause dramatic changes in the accessibility of the epitope and the induction of antibody responses.


Asunto(s)
Anticuerpos Antivirales/sangre , Antígenos Virales/inmunología , Parvovirus Canino/genética , Proteínas Recombinantes de Fusión/inmunología , Virión/inmunología , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Cápside/genética , Cápside/metabolismo , Perros , Epítopos/genética , Epítopos/inmunología , Ratones , Ratones Endogámicos BALB C , Datos de Secuencia Molecular , Mutagénesis , Parvovirus Canino/metabolismo , Poliovirus/genética , Poliovirus/inmunología , Poliovirus/metabolismo , Proteínas Recombinantes de Fusión/metabolismo , Virión/genética
9.
Vaccine ; 17(9-10): 1057-64, 1999 Mar 05.
Artículo en Inglés | MEDLINE | ID: mdl-10195615

RESUMEN

Bovine Viral Diarrhea Virus (BVDV) is a major pathogen of cattle in most countries. The main reservoir of virus in herds are BVDV persistently infected animals, which arise as a result of infection of the bovine fetus early in gestation. The spread of virus to the unborn fetus may be prevented by vaccination of the dam. We describe in this report the production and initial testing of an inactivated subunit vaccine against BVDV. The vaccine is based on production of antigen in primary bovine cell cultures, extraction of antigens from infected cells with detergent, chromatographic purification, concentration, and insertion of antigens into immune stimulating complexes (ISCOMs). Vaccines based on two different Danish strains of BVDV were injected into calves and the antisera produced were tested for neutralising activity against a panel of Danish BVDV strains. The two vaccines induced different neutralisation responses, which seem to partly complement each other. The implication of these observations for successful vaccination against BVDV is discussed.


Asunto(s)
Adyuvantes Inmunológicos/síntesis química , Diarrea Mucosa Bovina Viral/prevención & control , Virus de la Diarrea Viral Bovina/inmunología , ISCOMs/inmunología , Animales , Anticuerpos Antivirales/biosíntesis , Bovinos , Células Cultivadas , Reacciones Cruzadas , Electroforesis en Gel de Poliacrilamida
10.
J Virol ; 73(2): 930-8, 1999 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-9882293

RESUMEN

The humoral immune responses to the D2 peptide of fibronectin-binding protein B (FnBP) of Staphylococcus aureus, expressed on the plant virus cowpea mosaic virus (CPMV), were evaluated after mucosal delivery to mice. Intranasal immunization of these chimeric virus particles (CVPs), either alone or in the presence of ISCOM matrix, primed CPMV-specific T cells and generated high titers of CPMV- and FnBP-specific immunoglobulin G (IgG) in sera. Furthermore, CPMV- and FnBP-specific IgA and IgG could also be detected in the bronchial, intestinal, and vaginal lavage fluids, highlighting the ability of CVPs to generate antibody at distant mucosal sites. IgG2a and IgG2b were the dominant IgG subclasses in sera to both CPMV and FnBP, demonstrating a bias in the response toward the T helper 1 type. The sera completely inhibited the binding of human fibronectin to the S. aureus FnBP. Oral immunization of the CVPs also generated CPMV- and FnBP-specific serum IgG; however, these titers were significantly lower and more variable than those generated by the intranasal route, and FnBP-specific intestinal IgA was undetectable. Neither the ISCOM matrix nor cholera toxin enhanced these responses. These studies demonstrate for the first time that recombinant plant viruses have potential as mucosal vaccines without the requirement for adjuvant and that the nasal route is most effective for the delivery of these nonreplicating particles.


Asunto(s)
Adhesinas Bacterianas , Proteínas Bacterianas/inmunología , Vacunas Bacterianas/inmunología , Proteínas Portadoras/inmunología , Comovirus/inmunología , Fibronectinas/metabolismo , Inmunidad Mucosa , Staphylococcus aureus/inmunología , Adyuvantes Inmunológicos , Administración Intranasal , Administración Oral , Secuencia de Aminoácidos , Animales , Anticuerpos Antibacterianos/inmunología , Proteínas Bacterianas/genética , Vacunas Bacterianas/genética , Proteínas Portadoras/genética , Toxina del Cólera/inmunología , Comovirus/genética , Femenino , Humanos , ISCOMs/inmunología , Inmunoglobulina G/sangre , Inmunoglobulina G/clasificación , Inmunoglobulina G/inmunología , Intestinos/inmunología , Pulmón/inmunología , Ratones , Ratones Endogámicos C57BL , Datos de Secuencia Molecular , Staphylococcus aureus/genética , Linfocitos T/inmunología , Vacunas Sintéticas/genética , Vacunas Sintéticas/inmunología , Vagina/inmunología , Virión
11.
Virus Res ; 53(2): 163-73, 1998 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-9620208

RESUMEN

The antigenic structure of the capsid proteins of porcine parvovirus (PPV) was investigated. A total of nine linear epitopes were identified by Pepscan using porcine or rabbit anti-PPV antisera. No sites were identified with a panel of neutralising monoclonal antibodies (MAbs). All epitopes were located in the region corresponding to the major capsid protein VP2. Based on this information, and on analogy to other autonomous parvoviruses, 24 different peptides were synthesised, coupled to keyhole limpet haemocyanin (KLH) and used to immunise rabbits. Most antisera were able to bind viral protein. Only peptides from the N-terminal part of VP2 were able to induce virus-neutralising antibodies, although at low levels. A similar neutralising activity could be obtained in pigs. The exposure of the N-terminus was shown in full virions, both by immunoelectron microscopy and absorption experiments. It is concluded that in PPV, the VP2 N-terminus is involved in virus neutralisation (VN) and peptides from this region are therefore primary targets for developing peptide-based vaccines against this virus.


Asunto(s)
Cápside/inmunología , Mapeo Epitopo , Parvovirus/inmunología , Péptidos/inmunología , Porcinos/virología , Secuencia de Aminoácidos , Animales , Anticuerpos Antivirales/inmunología , Antígenos Virales/inmunología , Proteínas de la Cápside , Ensayo de Inmunoadsorción Enzimática , Inmunización , Datos de Secuencia Molecular , Péptidos/síntesis química , Conejos
12.
J Pept Res ; 50(5): 357-64, 1997 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-9401920

RESUMEN

Synthetic peptides have frequently been used to immunize animals. However, peptides less than about 20 to 30 amino acids long are poor immunogens. In general, to increase its immunogenicity, the presentation of the peptide should be improved, and molecular weight needs to be increased. Many attempts have been made to couple peptide immunogens to different carrier proteins [e.g. keyhole limpet haemocyanin (KLH) or ovalbumin]. This leads to very complex structures, however. We used a controlled conjugation of a peptide to a single long-chain fatty acid like palmitic acid by a thioester or an amide bond. It was found that these S-palmitoylated peptides were much more immunogenic than N-palmitoylated peptides and at least similar to KLH-conjugated peptides with respect to appearance and magnitude of induced antibodies (canine parvovirus) or immunocastration effect (gonadotropin-releasing hormone). For chemical synthesis of thioesters, we established conditions for solution and solid-phase synthesis. In both phases, Cys(SBut) could only be deprotected efficiently using phosphines, and S-acylation was accomplished using standard coupling at pH 5. We speculate that, in vivo, the presence of an appropriate fatty acid chain, chemically linked through a labile thioester bond, greatly enhances immunogenicity, because it represents a favourable substrate for cleavage by cellular thioesterases in cells of the immune system.


Asunto(s)
Antígenos/inmunología , Ácido Palmítico/metabolismo , Péptidos/inmunología , Compuestos de Sulfhidrilo/metabolismo , Vacunas Sintéticas/inmunología , Secuencia de Aminoácidos , Animales , Ésteres , Cobayas , Inmunización , Masculino , Datos de Secuencia Molecular , Péptidos/síntesis química , Porcinos
13.
Clin Diagn Lab Immunol ; 4(5): 504-8, 1997 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-9302195

RESUMEN

In order to compare protocols for inactivation of viruses potentially present in biological specimens, three different model viruses were treated in bovine serum by two different inactivation methods: samples were subjected either to chemical inactivation with ethylenimine (El) at concentrations of 5 and 10 mM at 37 degrees C for periods up to 72 h or to electron-beam irradiation in frozen and liquid form with doses varying between 11 and 46 kGy. The chemical inactivation resulted in nonlinear tailing curves in a semilogarithmic plot of virus titer versus inactivation time showing non-first-order kinetics with respect to virus titer. The time for inactivation of 7 log10 units of porcine parvovirus (PPV) was about 24 h for both El concentrations, whereas 5 log10 units of bovine viral diarrhea virus (BVDV) was inactivated in 2 h for both El concentrations and 6 log10 units of porcine enterovirus (PEV) was inactivated within 3 h. The inactivation with electron-beam irradiation resulted in almost linear curves in a semilogarithmic plot of virus titer versus irradiation dose, reflecting a first-order inactivation. The rate of inactivation was almost twice as fast in the liquid samples compared to the rate in frozen ones, giving values of the doses needed to reduce virus infectivity 1 log10 unit for inactivation of PPV of 11.8 and 7.7 kGy for frozen and liquid samples, respectively, whereas the corresponding values for BVDV were 4.9 and 2.5 kGy, respectively, and those for PEV were 6.4 and 4.4 kGy, respectively. The nonlinear inactivation with El makes it impossible to extrapolate the curves beyond the virus detection limit and thereby predict the necessary time for complete inactivation, i.e., to a level beyond the detection limit, of virus in a given sample. The first-order inactivation obtained with electron-beam irradiation makes such a prediction possible and justifiable. The two methods are discussed with respect to their different kinetics and applicability under different circumstances and criteria for inactivation, and considerations for choice of method are discussed.


Asunto(s)
Aziridinas/farmacología , Radiación Ionizante , Virología/métodos , Virus/efectos de los fármacos , Virus/efectos de la radiación , Animales , Bovinos , Medios de Cultivo , Virus de la Diarrea Viral Bovina/efectos de los fármacos , Virus de la Diarrea Viral Bovina/efectos de la radiación , Cinética , Modelos Biológicos , Parvovirus/efectos de los fármacos , Parvovirus/efectos de la radiación
14.
Nat Biotechnol ; 15(3): 248-52, 1997 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-9062924

RESUMEN

The successful expression of animal or human virus epitopes on the surface of plant viruses has recently been demonstrated. These chimeric virus particles (CVPs) could represent a cost-effective and safe alternative to conventional animal cell-based vaccines. We report the insertion of oligonucleotides coding for a short linear epitope from the VP2 capsid protein of mink enteritis virus (MEV) into an infectious cDNA clone of cowpea mosaic virus and the successful expression of the epitope on the surface of CVPs when propagated in the black-eyed bean, Vigna unguiculata. The efficacy of the CVPs was established by the demonstration that one subcutaneous injection of 1 mg of the CVPs in mink conferred protection against clinical disease and virtually abolished shedding of virus after challenge with virulent MEV, demonstrating the potential utility of plant CVPs as the basis for vaccine development. The epitope used occurs in three different virus species-MEV, canine parvovirus, and feline panleukopenia virus- and thus the same vaccine could be used in three economically important viral hosts-mink, dogs, and cats, respectively.


Asunto(s)
Infecciones por Parvoviridae/prevención & control , Vacunas Sintéticas/inmunología , Vacunas Virales/inmunología , Secuencia de Aminoácidos , Animales , Clonación Molecular , ADN Complementario , Virus de la Panleucopenia Felina , Microscopía Electrónica , Visón , Datos de Secuencia Molecular , Vacunas Sintéticas/genética , Vacunas Virales/genética
15.
Clin Diagn Lab Immunol ; 3(6): 628-34, 1996 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-8914750

RESUMEN

Viral contamination of biological material may constitute a risk when samples are exchanged between countries, and it may be necessary to subject the material to an inactivation treatment. The present study investigated possible adverse effects on antibody activity subsequent to either electron beam irradiation or binary ethylenimine (BEI) treatment. The treatments were performed with sera obtained from pigs or cattle. For each treatment level, the posttreatment activity was plotted against the pretreatment activity, and regression analyses were carried out. The slope of the regression line was used as an estimate for the relative posttreatment activity. For a Toxoplasma gondii indirect enzyme-linked immunosorbent assay (ELISA) and agglutination assay as well as for a Salmonella dublin indirect ELISA, the posttreatment activity was more than 89% of the pretreatment activity when the samples were irradiated in the frozen state (on dry ice) with up to 46. kGy or when they were treated with 5 or 10 mM BEI for up to 48 h. The samples were more sensitive to irradiation in the liquid state. Thus, samples irradiated with 22.6 kGy retained 98% of their activity in the indirect ELISA when they were irradiated in the frozen state on dry ice but only 35% of their activity when they were irradiated in the liquid state at 0 degrees C. The patterns seen in an S. dublin blocking ELISA and an Actinobacillus pleuropneumoniae complement fixation assay differed in that samples with a low level of pretreatment activity were subject to a relatively greater decrease in activity than samples with a high level of pretreatment activity. The complement fixation assay was particularly sensitive to irradiation of serum. It is concluded that serum samples retain sufficient activity by both methods of virus inactivation, especially when used in indirect ELISA or in the T. gondii agglutination assay.


Asunto(s)
Actinobacillus pleuropneumoniae/inmunología , Anticuerpos Antibacterianos/efectos de los fármacos , Anticuerpos Antibacterianos/efectos de la radiación , Anticuerpos Antiprotozoarios/efectos de los fármacos , Anticuerpos Antiprotozoarios/efectos de la radiación , Aziridinas/farmacología , Salmonella/inmunología , Toxoplasma/inmunología , Animales , Anticuerpos Antibacterianos/sangre , Anticuerpos Antiprotozoarios/sangre , Especificidad de Anticuerpos/efectos de los fármacos , Especificidad de Anticuerpos/efectos de la radiación , Bovinos , Ensayo de Inmunoadsorción Enzimática/veterinaria , Aceleradores de Partículas , Análisis de Regresión , Porcinos
16.
J Virol ; 69(11): 7274-7, 1995 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-7474152

RESUMEN

The N-terminal domain of the major capsid protein VP2 of canine parvovirus was shown to be an excellent target for development of a synthetic peptide vaccine, but detailed information about number of epitopes, optimal length, sequence choice, and site of coupling to the carrier protein was lacking. Therefore, several overlapping peptides based on this N terminus were synthesized to establish conditions for optimal and reproducible induction of neutralizing antibodies in rabbits. The specificity and neutralizing ability of the antibody response for these peptides were determined. Within the N-terminal 23 residues of VP2, two subsites able to induce neutralizing antibodies and which overlapped by only two glycine residues at positions 10 and 11 could be discriminated. The shortest sequence sufficient for neutralization induction was nine residues. Peptides longer than 13 residues consistently induced neutralization, provided that their N termini were located between positions 1 and 11 of VP2. The orientation of the peptides at the carrier protein was also of importance, being more effective when coupled through the N terminus than through the C terminus to keyhole limpet hemocyanin. The results suggest that the presence of amino acid residues 2 to 21 (and probably 3 to 17) of VP2 in a single peptide is preferable for a synthetic peptide vaccine.


Asunto(s)
Formación de Anticuerpos , Cápside/inmunología , Parvovirus Canino/inmunología , Vacunas Virales/inmunología , Secuencia de Aminoácidos , Animales , Anticuerpos Antivirales/biosíntesis , Proteínas de la Cápside , Secuencia de Consenso , Perros , Ensayo de Inmunoadsorción Enzimática , Ratones , Datos de Secuencia Molecular , Pruebas de Neutralización , Fragmentos de Péptidos/inmunología , Conejos/inmunología , Homología de Secuencia de Aminoácido , Relación Estructura-Actividad
17.
Vaccine ; 13(11): 1033-7, 1995 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-8525686

RESUMEN

Two recently developed vaccine--one based on synthetic peptide and one based on recombinant capsid protein--fully protected dogs against heavy experimental canine parvovirus (CPV) infection. The high sequence homology ( > 98%) and antigenic similarity between CPV and mink enteritis virus (MEV), feline panleukopenia virus, and raccoon parvovirus, suggest that both vaccines could protect mink, cats and raccoons against these respective host range variants. This was tested in mink and turned out to be the case. The two vaccines were fully protective and as effective as a conventional commercial vaccine based on inactivated virus. Surprisingly, this protection was obtained after only a single injection. Furthermore, the vaccinal dose of 150 micrograms of conjugated peptide or 3 micrograms of recombinant VP2 particles per animal, are sufficiently low to be cost-effective and applicable on a large scale.


Asunto(s)
Proteínas de la Cápside , Virus de la Panleucopenia Felina/inmunología , Visón/virología , Infecciones por Parvoviridae/prevención & control , Infecciones por Parvoviridae/veterinaria , Parvovirus Canino/inmunología , Vacunas Sintéticas/inmunología , Vacunas Virales/inmunología , Secuencia de Aminoácidos , Animales , Anticuerpos Antivirales/biosíntesis , Anticuerpos Antivirales/sangre , Cápside/genética , Cápside/inmunología , Datos de Secuencia Molecular , Pruebas de Neutralización , Péptidos/inmunología , Proteínas Recombinantes/inmunología , Vacunas Sintéticas/administración & dosificación , Vacunas Virales/administración & dosificación
19.
Rev Sci Tech ; 11(3): 873-7, 1992 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-1335308

RESUMEN

The preparation and preliminary testing of a subunit ISCOM (immunostimulating complex) vaccine against bovine virus diarrhoea virus (BVDV) is described. Vaccination of calves with this vaccine yields high neutralising titres against a panel of Danish BVDV field isolates. The serological difference between virus isolates and vaccine strain selection is discussed.


Asunto(s)
Diarrea Mucosa Bovina Viral/prevención & control , Virus de la Diarrea Viral Bovina/inmunología , ISCOMs , Vacunación/veterinaria , Vacunas Virales , Animales , Anticuerpos Antivirales/sangre , Bovinos , Vacunas Virales/inmunología
20.
Vet Microbiol ; 29(1): 1-13, 1991 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-1659027

RESUMEN

The pestiviruses are small enveloped RNA viruses and are causative agents of economically important animal diseases in cattle, swine, sheep and goats worldwide. We used the polymerase chain reaction to amplify one common fragment of several different strains of both hog cholera virus and bovine virus diarrhea virus (BVDV). The fragment is located at the 5'-end of the genome immediately upstream of the open reading frame. This is a highly conserved region among the different published pestivirus sequences. An internal restriction digest of the amplified fragment with XhoI and PstI was performed in order to confirm specificity of the amplified fragment. The fragment was sequenced for a number of different BVDV strains, and the sequences obtained were compared to those published and used to deduce genetic relationships between strains. Apart from this common fragment we have amplified several other fragments of the Danish BVDV strain Ug59 and obtained specific amplification fragments of the expected size.


Asunto(s)
Virus de la Fiebre Porcina Clásica/genética , Virus de la Diarrea Viral Bovina/genética , ARN Viral/química , Animales , Secuencia de Bases , Bovinos , Electroforesis en Gel de Agar , Datos de Secuencia Molecular , Sondas de Oligonucleótidos/química , Reacción en Cadena de la Polimerasa , Mapeo Restrictivo , Porcinos , Transcripción Genética
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