Recombinant vaccine for canine parvovirus in dogs

Turiso, J A López de; Cortes, Elena; Martínez, Concepción; Ybanez, Rocto Ruiz De; Simarro, I.; Vela, Carmen; Casal, J. Ignacio

doi:10.1128/jvi.66.5.2748-2753.1992

Cited by 81 publications

(21 citation statements)

References 23 publications

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“…The membrane was incubated for 1 h at room temperature in blocking buffer (3% skim milk in phosphate-buffered saline [PBS]). A mixture of CPV VP2-specific MAbs (14) was added and incubated for 2 h at room temperature. After washing, bound antibody was detected with alkaline phosphatase-conjugated goat antimouse immunoglobulin G antibodies (1:10,000 dilution in PBS) (Sigma).…”

Section: Methodsmentioning

confidence: 99%

“…We have developed a system that allows us to study the effects of different domains and residues of VP2 in the interactions necessary for the assembly of the capsid. Expression of CPV VP2 in insect cells results in the assembly of virus-like particles (VLPs), which indicates that VP2 alone is sufficient for capsid assembly (14,18). Our studies on CPV VP2 have involved the synthesis of a series of mutants with internal deletions in the four major loops of the surface of the capsid.…”

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confidence: 99%

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Identification of domains in canine parvovirus VP2 essential for the assembly of virus-like particles

Hurtado

Rueda

Nowicky

et al. 1996

J Virol

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Canine parvovirus capsids are composed of 60 copies of VP2 and 6 to 10 copies of VP1. To locate essential sites of interaction between VP2 monomers, we have analyzed the effects of a number of VP2 deletion mutants representing the amino terminus and the four major loops of the surface, using as an assay the formation of virus-like particles (VLPs) expressed by recombinant baculoviruses. For the amino terminus we constructed three mutants with progressively larger deletions, i.e., 9, 14, and 24 amino acids. Deletions of 9 and 14 amino acids did not affect the morphology and assembly capabilities of the mutants. However, the mutant with the 24-amino-acid deletion did not show hemagglutination properties or correct VLP morphology, stressing again the relevance of the RNER domain in canine parvovirus functionality. Three of the four mutants with deletions in the loops failed to make correct VLPs, indicating that these regions are essential for correct capsid assembly and morphology. Only the mutant with the deletion in loop 2 was able to assemble in regular VLPs, suggesting that this loop has little or no effect in capsid morphogenesis. Further research has demonstrated that this region can tolerate the insertion of foreign epitopes that are correctly exposed in the surface of the capsid. This result opens the door to the use of these VLPs for antigen delivery.

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Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

Identification of domains in canine parvovirus VP2 essential for the assembly of virus-like particles

Hurtado

Rueda

Nowicky

et al. 1996

J Virol

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“…Both tested VLPs were able to elicit neutralizing antibodies, sufficient to render all the immunized dogs protected against the viral challenge. 66,67…”

Section: Swine Viruses and Parvoviridaementioning

confidence: 99%

Virus-like particle-based vaccines for animal viral infections

Crisci

Bárcena²,

Montoya

2013

Inmunología

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i n m u n o l o g í a . 2 0 1 3;3 2(3):102-116 103Por lo general son antigénicamente indistinguibles de los virus de los que proceden y su empleo como inmunógenos presenta importantes ventajas en términos de seguridad. Las VLPs pueden inducir una fuerte respuesta inmune, tanto humoral como celular, y se ha demostrado que poseen capacidad de actuar como adyuvantes (self-adjuvanting). Además de su idoneidad como vacunas frente al virus homólogo del cual proceden, las VLPs también se pueden utilizar como vectores para la presentación multimérica de antígenos heterólogos. Las VLPs han mostrado una elevada eficacia como candidatos vacunales, sin embargo, hasta el momento sólo una vacuna basada en VLPs ha sido autorizada y comercializada en el campo veterinario. En este trabajo se revisa el estado actual de las VLP empleadas como nuevas estrategias vacunales en el campo de la veterinaria, analizando las potenciales ventajas y desafíos que enfrenta esta tecnología.

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“…The BEVS has been used to produce a variety of parvovirusspecific proteins. Among these, virus-like particles (VLPs) have been produced for adeno-associated virus [25], Aleutian mink disease parvovirus [26], muscovy duck parvovirus [27], human parvovirus B19, porcine parvovirus [28][29][30], and canine parvovirus [31][32][33][34][35]. Recently, baculoviral vectors have also been used to efficiently mediate gene transfer and expression in various mammalian cell lines both in vitro [36][37][38][39][40][41][42][43][44][45] and in vivo [46][47][48][49].…”

Section: Introductionmentioning

confidence: 99%

Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus‐transduced NLFK cells

et al. 2004

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A mammalian baculovirus delivery system was developed to study targeting in Norden Laboratories feline kidney (NLFK) cells of the capsid proteins of canine parvovirus (CPV), VP1 and VP2, or corresponding counterparts fused to EGFP. VP1 and VP2, when expressed alone, both had equal nuclear and cytoplasmic distribution. However, assembled form of VP2 had a predominantly cytoplasmic localization. When VP1 and VP2 were simultaneously present in cells, their nuclear localization increased. Thus, confocal immunofluorescence analysis of cells transduced with the different baculovirus constructs or combinations thereof in the absence or presence of infecting CPV revealed that the VP1 protein is a prerequisite for efficient targeting of VP2 to the nucleus. The baculovirus vectors were functional and the genes of interest efficiently introduced to this CPV susceptible mammalian cell line. Thus, we show evidence that the system could be utilized to study targeting of the CPV capsid proteins.

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Recombinant vaccine for canine parvovirus in dogs

Cited by 81 publications

References 23 publications

Identification of domains in canine parvovirus VP2 essential for the assembly of virus-like particles

Identification of domains in canine parvovirus VP2 essential for the assembly of virus-like particles

Virus-like particle-based vaccines for animal viral infections

Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus‐transduced NLFK cells

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