In vivo subcellular localization of Mal de Río Cuarto virus (MRCV) non-structural proteins in insect cells reveals their putative functions

MARONICHE GA; MONGELLI, V. C.; LLAUGER, G.; ALFONSO, V.; TABOGA, O.; DEL VAS, M.

VIROLOGY

ACADEMIC PRESS INC ELSEVIER SCIENCE

Lugar: Amsterdam; Año: 2012 vol. 430 p. 81 - 89

0042-6822

To obtain insight into the function of Mal de Río Cuarto virus (MRCV, Fijivirus, Reoviridae) non-structural proteins, their in vivo subcellular localization was analyzed employing confocal microscopy. Our results showed that MRCV P5-2, P7-1 and P7-2 are able to enter the nucleus; MRCV P5-1 has a cytoplasmic vesicular-like distribution that might result from its interaction with cellular PDZ proteins; MRCV P6 localizes in the cytoplasm and in perinuclear cloud-like inclusions, it is driven to viroplasm-like structures formed by MRCV P9-1 and co-localizes with MRCV P7-2, with the major outer capsid protein MRCV P10 and with tubulin, supporting a possible role for MRCV P6 in the formation of viroplasms and intracellular movement of viral particles; MRCV P9-2 is a glycoprotein located at the plasma membrane in association with filopodia-like cell protrusions that contain actin and might be involved in virus cell-to-cell movement and spread.