Page 95 - CIBERES-2015-eng

Most relevant scientific articles
Research Groups
Falcon A., Cuevas M.T., Rodríguez-Frandsen A., Reyes N., Pozo F., Moreno S. et al. CCR5 deficiency predisposes to fatal outcome in influenza virus infection. Journal of Gen- eral Virology. 2015;96(8):2074-2078.
Ortin J., Martín-Benito J.. The RNA synthesis machinery of negative-stranded RNA viruses. Virology. 2015;479- 480:532-544.
Gilman M.S.A., Moin S.M., Mas V., Chen M., Patel N.K., Kramer K. et al. Characterization of a Prefusion-Specific Antibody That Recognizes a Quaternary, Cleavage-De- pendent Epitope on the RSV Fusion Glycoprotein. PLoS Pathogens. 2015;11(7).
Highlights
Influenza virus establishes a complex network of in- teractions with the host cell, accordingly it is known that its pathogenicity depends on a large number of virus-host interactions. This suggests that efficient replication of influenza viruses is based on a set of virus-host cell interactions in which there are two factors involved; the viral pathogenicity determi- nants and the genetic determinants of the host.
We have characterized some cellular factors that interact with influenza virus proteins and modulate its replicative cycle such as the cellular factor NXP2 / MORC3, which is a positive modulator of viral replication in cultured cells. On the other hand we have characterized a risk factor for the human pop- ulation, the chemokine receptor CCR5, whose pres- ence in homozygous of a deleted form, increases very significantly the fatality rate by influenza virus infection.
Ver LS, Marcos-Villar L, Landeras-Bueno S, Nieto A, Ortín J. The Cellular Factor NXP2/MORC3 Is a Positive Regu- lator of Influenza Virus Multiplication.Journal of virology. 2015;89(19):10023-30.
Trento A, Ábrego L, Rodríguez-Fernández R, González- Sánchez MI, González-Martínez F, Delfraro A et al. Conser- vation of G-Protein Epitopes in Respiratory Syncytial Virus (Group A) Despite Broad Genetic Diversity: Is Antibody Selection Involved in Virus Evolution?. Journal of virology. 2015;89(15):7776-85.
Progress has also been attained in understanding of the F glycoprotein of human respiratory syncytial virus (hRSV) and human metapneumovirus (hMPV), two highly related viruses at the clinic and genetic level. The hMPV F protein was purified to homoge- neity in its postfusion conformation, allowing crys- tallization and determination of its atomic structure. Comparison of this structure with those of other paramyxovirus F proteins revealed many similarities with that of hRSV F but more differences with its counterparts of two other paramyxoviruses (PIV3 and NDV).
Despite crossreactivity of hRSV and hMPV F gly- coproteins with a monoclonal antibody, polyclonal sera raised against either protein failed to exhibit crossreactivity. This prompted us the design of chi- meric F proteins that could be used as “universal” vaccine against the Pneumovirinae.
Institution: Agencia Estatal Consejo Superior de Investigaciones Científicas · C. Nacional de Biotecnología Contact: c/ Darwin, 3. Universidad Autónoma de Madrid. Cantoblanco. Dpto de Biología Molecular y Celular. 28049 Madrid · Tel.: 91 585 45 57 · E.mail: [email protected]
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