SciELO - Scientific Electronic Library Online

 
vol.47 número3Hormiga argentina Linepithema humile Mayr, 1868 (Hymenoptera: Formicidae) y su rol como posible vector de contaminación microbiana en una lechería de cabras Capra hircus Linnaeus, 1758 (Artiodactyla: Bovidae)Evaluación de protocolos de sedación y analgesia con xilazina y dos tasas de infusión continua de morfina en caballos en estación sometidos a castración vía laparascópica índice de autoresíndice de materiabúsqueda de artículos
Home Pagelista alfabética de revistas  

Servicios Personalizados

Revista

Articulo

Indicadores

Links relacionados

  • En proceso de indezaciónCitado por Google
  • No hay articulos similaresSimilares en SciELO
  • En proceso de indezaciónSimilares en Google

Compartir


Archivos de medicina veterinaria

versión impresa ISSN 0301-732X

Resumen

VILLA-MANCERA, A et al. Identification of novel peptides of a phage display library with specific monoclonal antibody to the N protein of PRRS virus. Arch. med. vet. [online]. 2015, vol.47, n.3, pp.325-331. ISSN 0301-732X.  http://dx.doi.org/10.4067/S0301-732X2015000300009.

The aim of the present study was to select phage clones from a combinatorial library of filamentous phage that mimic the N protein of Porcine Reproductive and Respiratory Syndrome Virus (PRRS) using a monoclonal antibody (SDOW17). An combinatorial library of random peptide 7-mer cysteine-constrained fused to a minor coat protein (pIII) of the M13 phage was used. To determine the effect of enrichment after each round of selection, the eluted phage were titrated, bacteriophages increased from 4,8 x 103 plaque-forming units (pfu) in the first round to 3,2 x 105 pfu in the third round. After three rounds of panning 32 phage clones were randomly picked, each individual clone was amplified, purified and titred. The binding reactivity of phage clones with anti-PRRS antibodies was determined using a phage ELISA. Alignments of the selected clones with the published sequences of the N protein of PRRS virus were located at the amino terminal region and middle portion of the protein. The consensus amino acid residues of the 32 mimotopes sequenced was NYRYQ. Mimotope sequences were used to calculate the epitopes of the nucleocapsid protein by the web tool of Peptiope server with PepSurf algorithm. Two conformational epitopes against monoclonal antibody anti-protein N were identified, located in a different position and appeared mainly as an a-helix. The selected mimotopes and conformational epitopes could be regarded as informative for diagnosis of disease.

Palabras clave : N protein; PRRS; mimotopes; phage display.

        · resumen en Español     · texto en Español     · Español ( pdf )

 

Creative Commons License Todo el contenido de esta revista, excepto dónde está identificado, está bajo una Licencia Creative Commons