Las proteínas virales p49 y pB602L son esenciales para la construcción de la cápsida icosaédrica del virus de la peste porcina africana
Author
Epifano García, CarolinaEntity
UAM. Departamento de Biología Molecular; Centro de Biología Molecular Severo Ochoa (CBM)Date
2005-11-15Subjects
Virus de la peste porcina africana-Tesis doctorales; Proteínas virales-Tesis doctorales; Biología y Biomedicina / BiologíaNote
Tesis Doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departamento de Biología Molecular. Fecha de lectura : 15-11-2005Abstract
African swine fever virus (ASFV), the only member of the AsfawiMae family. is one
of the largest and more complex icosahedral virus which assemble in animal cells.
The ASFV particle is approximately 200 nm in diameter and is composed of the DNAcontaining
nucleoid surrounded by a thick protein layer denominated wre-shell,
which is enwrapped by an internal envelope and the icosahedral capsid. We have
approached the study of the viral morphogenesis by analyzing the effect of the
repression of key viral proteins on this process. To this end. we have constructed and
characterized two recombinant viruses which inducibly express protein p49 or protein
pB602L. Protein p49 is a structural componen! of the viral particle. while protein
pB602L has been proposed to function in the correct folding of the major capsid
protein p72. Although p49 does not possess any canonical membrane insertion
sequence, it associates with membranes during the infection, probably due to an
interaction with a viral protein located in the internal envelope of the virus particle. It
has been found that, in the absence of protein p49. the viral assembiy proms is
altered wlh the generation of tubular structures of a large size and containing an
aberrant capsid. On the other hand. the findings with the recombinant virus inducibly
expressing protein pBBO2L show that, in the absence of the non-structural protein
pB6021, aberrant "zipper-like" structures, which do not possess a capsid. are
accumulated in the virus assembly sites. Under restrictive condiitions, protein p72
translocates from the virus factory to the cytoplasm, probabiy due to an inwrrect
folding of the protein.
The results obtained with the two inducible viruses indicate that protein p49 and
protein pB602L are essential for the mrrect constniction of the virus icosahedral
capsid.
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