Evasión del sistema inmune por receptores solubles de citoquinas codificados por virus

Álvarez de Miranda Rodríguez, Francisco Javier (2019). Evasión del sistema inmune por receptores solubles de citoquinas codificados por virus. Proyecto Fin de Carrera / Trabajo Fin de Grado, E.T.S. de Ingeniería Agronómica, Alimentaria y de Biosistemas (UPM), Madrid.

Description

Title: Evasión del sistema inmune por receptores solubles de citoquinas codificados por virus
Author/s:
  • Álvarez de Miranda Rodríguez, Francisco Javier
Contributor/s:
  • Alcamí Pertejo, Antonio Javier
  • García-Arenal Rodríguez, Fernando
Item Type: Final Project
Degree: Grado en Biotecnología
Date: June 2019
Subjects:
Faculty: E.T.S. de Ingeniería Agronómica, Alimentaria y de Biosistemas (UPM)
Department: Biotecnología - Biología Vegetal
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

The Poxviridae family is remarkable for its many mechanisms to avoid the immune system of their hosts, which provide them with the ability to infect animals. Famous members of this family include Variola virus, the causing agent of smallpox, and Vaccinia virus, which was used for the eradication of smallpox. Among those mechanisms, we emphasise soluble type I interferon viral receptors, which are secreted by infected cells and can bind to this cytokine blocking the antiviral response. It has been discovered that most poxviruses encode a soluble type I interferon-binding protein, among which B18 protein from Vaccinia virus has been the most studied. Its importance on pathogenesis and infection is now clear, and it has been related to the effectiveness of specific vaccines against poxviruses. Recent studies have shown that B18 protein can additionally bind to the glycosaminoglycans on the cell surface to exert its function. While B18 is composed of three immunoglobulin-like domains, this ability relies exclusively on domain 1. On the other hand, it was previously demonstrated that domain 3 from B18 retained the ability to bind type I interferon, independently of the other two domains. The main aim of this work was the generation of a new recombinant protein in which domain three is fused to a small region within domain one, hypothetically responsible of binding to the cell surface. To this effect, we used the baculovirus expression system to express the protein and isolated it by affinity chromatography. Finally, the recombinant protein obtained was used in an interferon protection assay to evaluate its ability to block type I interferon biological effects. We could confirm that domain 3 from B18 retained the ability to bind and block type I interferon, even after fusion to the glycosaminoglycan-binding region. Following studies should explore whether this recombinant protein retained the ability to bind to the cellular surface, and should perform a comparative analysis between the effectiveness of the isolated domain 3 previously expressed in bacteria and the new recombinant protein expressed in baculovirus.

More information

Item ID: 57463
DC Identifier: http://oa.upm.es/57463/
OAI Identifier: oai:oa.upm.es:57463
Deposited by: Biblioteca ETSI Agrónomos
Deposited on: 10 Dec 2019 12:26
Last Modified: 10 Dec 2019 12:26
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