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Articles by Felix Alvarez
Total Records ( 2 ) for Felix Alvarez
  Nelson Acosta-Rivero , Yaraima Aguilera , Viviana Falcon , Joanna Poutou , Alexis Musacchio , Liz Alvarez-Lajonchere , Ivis Guerra , Julio C. Alvarez-Obregon , Yalena Amador-Canizares , Gillian Martinez-Donato , Jeny Marante , Julio C. Aguilar , Yordanka Soria , Felix Alvarez , Angel Perez , Maria C. de la Rosa , Juan Morales , Juan B. Kouri and Santiago Duenas-Carrera
  Recently, it has been shown that a truncated HCV core (HCcAg) variant, covering the first 120 aa (HCcAg.120), interacts with plasmid DNA vaccine (pIDKE2), encoding the HCV structural proteins (HCcAg, E1 and E2). In the present work, HCcAg.120-pIDKE2 complexes, forming heterogeneous packaged structures, were visualized using a negative stain/rotary shadow technique. Interestingly, 72 hours after intramuscular injection of HCcAg.120-pIDKE2 complexes in Balb/c mice, E2 protein was immunolabeled in muscle cells. In fact, HCcAg.120-pIDKE2 complexes induced anti-HCV humoral and cellular immune responses in mice when inoculated by both, parenteral or mucosal routes, although intranasal administration generally rendered weaker results. On the other hand, data demonstrated that Alum enhanced the HCV-specific IgG antibody production. However, the analysis of the HCV-specific cellular immune response showed that HCcAg.120-pIDKE2 delivered in PBS by the intramuscular route induced the strongest HCV-specific lymphoproliferative response, especially against E1 and induced viremia control in a vaccinia virus surrogate challenge model. These results support the use of HCcAg.120-pIDKE2 complexes in the rational design of therapeutic or preventive vaccine strategies against HCV infection.
  Viviana Falcon , Ivon Menendez , Nelson Acosta-Rivero , Mineko Shibayama , Marlia-C de la Rosa , Jose Luna- Munoz , Magdalena Miranda-Sanchez , Jorge V. Gavilondo , Deliana Lopez , Santiago Duenas-Carrera , Bienvenido Gra , Glay Chinea , Luisa Tamayo Garcia , Waldo Garcia , Eduardo Vidal , Enrique Arus-Soler , Jose Silva , Felix Alvarez , Emilio F. Acosta , Jesus Seoane , Juan Morales-Grillo , Eduardo Penton , Juan Kouri and Victor Tsutsumi
  Despite of recent advances on acknowledge of hepatitis B virus (HBV) structure and biology, little is known about the morphogenesis and release of virions. In this study, the ultrastructural analysis of HBV components in liver biopsies from chronically HBV-infected patients disclosed complex assembly and morphogenesis pathways for HBV. HBV core (HBcAg) and surface (HBsAg) antigens were specifically identified in all liver biopsies from HVB-infected patients. HBcAg containing core-like particles 24-28 nm in diameter were observed both in nucleus and cytoplasm of hepatocytes. Dane’s-like particles were detected either budding to or into the lumen of ER close to HBsAg containing tubular structures. Besides, Dane’s-like particles were detected in different vesicular compartments resembling multivesicular endosomes. Other kind of enveloped HBV-like particles similar to the previously described cobra-shaped and horn-shaped particles were also observed in hepatocytes. Some of these particles were connected to the vesicle membrane through a stalk 20-22 nm in diameter. On the other hand, spherical subviral particles (SVP) were frequently observed in cytoplasmic vesicles. Moreover, a minor proportion of enveloped HBV-like particles budding through the plasma membrane to the extracellular space and bile canaliculi were detected. Interestingly, Dane’s-like particles in the bile canaliculi and entering into ductular-like cells were shown. Strikingly, Dane’s-like particles close to tubular structures and specific immunolabeling for HBcAg both in cytoplasm and nuclei of stellate-like cells were detected. Remarkably, HVB-like particles appeared entering hepatocytes from large cytoplasmic processes of fibrocytes raising the interesting possibility of a cell to cell passage of HBV through direct transcellular migration.
 
 
 
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