Previously we have reported the capacity of the fusion protein PD3, composed of the P64k protein and the envelope (E) fragment from amino acids (aa) 286-426 of dengue-2 virus (DEN-2), to induce a functional immune response in mice against the homologous virus. In that case, the E fragment was inserted within the lipoyl-binding domain of the meningococcal P64k protein. In the present study, to test the functionality of the same E region from dengue-1 (DEN-1), a similar construct was made. Furthermore, another alternative of fusion protein was also constructed where the same E fragment from DEN-1 was fused to the C-terminus of the P64k protein. The recombinant proteins obtained (PD11 and PD10) were semi-purified and analysed for their antigenicity, immunogenicity and the ability to protect mice against lethal challenge. Both molecules exhibited the same recognition patterns against anti-DEN-1 polyclonal antibodies. In addition, when administered to mice, they elicited high levels of neutralizing antibodies and induced significant protection against lethal challenge with DEN-1 after intracerebral inoculation. These results reveal the availability of two sites within the P64k for the further insertion of DEN fragments, enabling a construct carrying two fragments from heterologous serotypes within the same molecule of this protein carrier.

A fragment of the envelope protein from dengue-1 virus, fused in two different sites of the meningococcal P64k protein carrier, induces a functional immune response in mice / L. Hermida, R. Rodríguez, L. Lazo, L. Bernardo, R. Silva, A. Zulueta, C. López, J. Martín, I. Valdés, D. del Rosario, G. Guillén, M.G. Guzmán. - In: BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY. - ISSN 0885-4513. - 39(2004 Feb), pp. 107-114.

A fragment of the envelope protein from dengue-1 virus, fused in two different sites of the meningococcal P64k protein carrier, induces a functional immune response in mice

A. Zulueta;
2004-02

Abstract

Previously we have reported the capacity of the fusion protein PD3, composed of the P64k protein and the envelope (E) fragment from amino acids (aa) 286-426 of dengue-2 virus (DEN-2), to induce a functional immune response in mice against the homologous virus. In that case, the E fragment was inserted within the lipoyl-binding domain of the meningococcal P64k protein. In the present study, to test the functionality of the same E region from dengue-1 (DEN-1), a similar construct was made. Furthermore, another alternative of fusion protein was also constructed where the same E fragment from DEN-1 was fused to the C-terminus of the P64k protein. The recombinant proteins obtained (PD11 and PD10) were semi-purified and analysed for their antigenicity, immunogenicity and the ability to protect mice against lethal challenge. Both molecules exhibited the same recognition patterns against anti-DEN-1 polyclonal antibodies. In addition, when administered to mice, they elicited high levels of neutralizing antibodies and induced significant protection against lethal challenge with DEN-1 after intracerebral inoculation. These results reveal the availability of two sites within the P64k for the further insertion of DEN fragments, enabling a construct carrying two fragments from heterologous serotypes within the same molecule of this protein carrier.
dengue-1; fusion; neutralization; P64k carrier; protection
Settore BIO/10 - Biochimica
Settore BIO/11 - Biologia Molecolare
Settore MED/07 - Microbiologia e Microbiologia Clinica
Article (author)
File in questo prodotto:
File Dimensione Formato  
Hermida_et_al-2004-Biotechnology_and_Applied_Biochemistry.pdf

non disponibili

Tipologia: Publisher's version/PDF
Dimensione 120.02 kB
Formato Adobe PDF
120.02 kB Adobe PDF   Visualizza/Apri   Richiedi una copia
Pubblicazioni consigliate

Caricamento pubblicazioni consigliate

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/491336
Citazioni
  • ???jsp.display-item.citation.pmc??? 6
  • Scopus 33
  • ???jsp.display-item.citation.isi??? 27
social impact