A new memory space: The urology museum “Prof. Dr. Néstor Vigo“ from the Faculty of Medical Sciences of the UNLP

La Universidad Nacional de La Plata, desde la normalización, ha desarrollado una política de acercamiento a la comunidad local y nacional mediantela educación no formal. Para ello ha incentivado la generación de Museos Universitarios nucleados enuna Red cuya finalidad es mostrar cómo la ciencia, el arte, la tecnología y la educación han contribuido al mejoramiento de la calidad de vida. En la Facultad de Ciencias Médicas existen los Museos de Anatomíahumana normal Dr. “Alberto Leonardo Poli”, de Historia de la Medicina “Dr. Santiago Gorostiague” y el de Urología “Dr. Néstor J. Vigo”.Fil: Tobia Gonzalez, Sebastian Gregorio. Universidad Nacional de La Plata. Facultad de Ciencias Médicas; ArgentinaFil: Tobia González, Ignacio P.. Universidad Nacional de La Plata. Facultad de Ciencias Médicas; ArgentinaFil: Sempe, Maria Carlota. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Laboratorio de Análisis Cerámico; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentin

A new memory space: The urology museum “Prof. Dr. Néstor Vigo“ from the Faculty of Medical Sciences of the UNLP

La Universidad Nacional de La Plata, desde la normalización, ha desarrollado una política de acercamiento a la comunidad local y nacional mediantela educación no formal. Para ello ha incentivado la generación de Museos Universitarios nucleados enuna Red cuya finalidad es mostrar cómo la ciencia, el arte, la tecnología y la educación han contribuido al mejoramiento de la calidad de vida. En la Facultad de Ciencias Médicas existen los Museos de Anatomíahumana normal Dr. “Alberto Leonardo Poli”, de Historia de la Medicina “Dr. Santiago Gorostiague” y el de Urología “Dr. Néstor J. Vigo”.Fil: Tobia Gonzalez, Sebastian Gregorio. Universidad Nacional de La Plata. Facultad de Ciencias Médicas; ArgentinaFil: Tobia González, Ignacio P.. Universidad Nacional de La Plata. Facultad de Ciencias Médicas; ArgentinaFil: Sempe, Maria Carlota. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Laboratorio de Análisis Cerámico; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentin

A viral inhibitor of peptide transporters for antigen presentation

CYTOTOXIC T lymphocytes lyse target cells after T-cell-receptor-mediated recognition of class I major histocompatibility complex molecules presenting peptides(1). Antigenic peptides are generated in the cytoplasm by proteasomes(2) and translocated into the lumen of the endoplasmic reticulum (ER) by peptide transporters (TAP)3-6. Herpes simplex virus (HSV) expresses a cytoplasmic protein, ICP47, which seems to interfere with such immune surveillance by mediating retention of 'empty' class I molecules in the ER(7,8). BY expressing ICP47 in HeLa cells under an inducible promoter(9), we show that ICP47 efficiently inhibits peptide transport across the ER membrane such that nascent class I molecules fail to acquire antigenic peptides. This inhibition was overcome by transfecting murine TAP. Further, we demonstrate that ICP47 colocalizes and physically associates with TAP within the cell, Inhibition of peptide translocation by a viral protein indicates a previously undocumented potential mechanism for viral immune evasion. [References: 22

Molecular mechanism and species specificity of tap inhibition by herpes simplex virus protein icp47

The immediate early protein ICP47 of herpes simplex virus (HSV) inhibits the transporter for antigen processing (TAP)-mediated translocation of antigen-derived peptides across the endoplasmic reticulum (ER) membrane. This interference prevents assembly of peptides with class I MHC molecules in the ER and ultimately recognition of HSV-infected cells by cytotoxic T-lymphocytes, potentially leading to immune evasion of the virus. Here, we demonstrate that recombinant, purified ICP47 containing a hexahistidine tag inhibits peptide import into microsomes of insect cells expressing human TAP, whereas inhibition of peptide transport by murine TAP was much less effective. This finding indicates an intrinsic species-specificity of ICP47 and suggests that no additional proteins interacting specifically with either ICP47 or TAP are required for inhibition of peptide transport. Since neither purified nor induced ICP47 inhibited photocrosslinking of 8-azido-ATP to TAP1 and TAP2 it seems that ICP47 does not prevent ATP from binding to TAP. By contrast, peptide binding was completely blocked by ICP47 as shown both by photoaffinity crosslinking of peptides to TAP and peptide binding to microsomes from TAP-transfected insect cells. Competition experiments indicated that ICP47 binds to human TAP with a higher affinity (50 nM) than peptides whereas the affinity to murine TAP was 100-fold lower. Our data suggest that ICP47 prevents peptides from being translocated by blocking their binding to the substrate-binding site of TAP. [References: 47