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The 11 th International Workshop on KSHV & Related Agents, Birmingham, UK Poster Session Abstract P7 SUMO-MODIFICATION MODULATES THE SUBCELLULAR LOCALIZATION AND ACTIVITY OF THE KSHV LATENT PROTEIN LANA2 1 2 3 3 2 Laura Marcos-Villar, Pedro Gallego, Fernando Lopitz, Manuel S Rodriguez & Carmen Rivas 1Dpt Microbiologia II, Fac Farmacia, Universidad Complutense de Madrid, Madrid, Spain; 2 Dpt Biología Molecular y Celular, Centro Nacional de Biotecnología, CSIC, Madrid, Spain; 3 Ubiquitin-like proteins & Cancer Group, Proteomics Unit. CIC-BioGUNE, Derio, Spain. Abstract Small ubiquitin-related modifier (SUMO) family proteins function by becoming covalently attached to other proteins as post-translational modifications. SUMO modifies many proteins that participate in diverse processes, including transcriptional regulation, nuclear transport, maintenance of genome integrity, and signal transduction. The functional consequences of SUMO attachment vary greatly from substrate to substrate; however, two general modes of action have been suggested. Sumoylation may alter protein stability or may alter protein-protein interactions that could result in a variety of consequences, including changes in cellular localization. LANA2 is a multifunctional protein exclusively expressed in KSHV infected B cells that is required for the survival of KSHV-infected primary effusion lymphoma cells. Studies carried out in our laboratory demonstrate that LANA2 is covalently modified by SUMO. Sumoylation of LANA2 does not affect protein stability but modulates its subcellular localization and protein activity. Presenting author Email: lmarcos@cnb.csic.es 104
The 11 th International Workshop on KSHV & Related Agents, Birmingham, UK Poster Session Abstract P8 HHV8-ASSOCIATED K5/MIR2 EXPRESSION IN VIVO CORRELATES WITH REDUCED COEXPRESSION OF CD31, MHC-1, AND ®-CATENIN IN KAPOSI’S SARCOMA Liron Pantanowitz1, Mandana Mansouri2, Sharon Marconi1, Eric Bartee2, Ashlee V. Moses2, Klaus Früh2 1 Department of Pathology, Baystate Medical Center, Tufts University School of Medicine, Springfield, MA; 2 Vaccine and Gene Therapy Institute, Oregon Health & Science University, 505 NW185th Ave, Beaverton, OR, 97006, USA Abstract K5/MIR2 eliminates MHC-I, CD31 and the VE-Cadherin/β-catenin complex from KSHVinfected endothelial cells in vitro, thereby reducing their immune recognition, cell adhesion and migration. Expression of K5 in vivo and downregulation of K5-target proteins in Kaposi’s sarcoma (KS) has not been studied. Therefore, we investigated K5 in patient procured KS lesions, and sought to determine whether this expression correlated with loss of CD31, MHC-1, and β-Catenin. Immunohistochemistry was performed on biopsied KS lesions of various stages (patch 2, plaque 10, tumor 8) using novel antibodies to K5, as well as antibodies to CD31, CD34, MHC-I, β-Catenin, LNA-1, and D2- 40. All cases were immunoreactive with CD34, D2-40 and LNA-1. K5-specific staining was observed in 100% of tumor stage lesions and 40% of KS plaques. While only a few spindle cells were K5 positive (3+) in plaque lesions, up to 90% of lesional cells were K5 positive in KS tumors. In only 10% of cases with K5 staining was concomitant expression of K5-targeted molecules (CD31, MHC-1, and β-Catenin) noted, whereas 50% of K5negative cases stained for K5-targeted molecules. These data suggest that K5 expression in vivo is more wide-spread than currently assumed, particularly in advanced KS lesions. Moreover, K5 expression in KS tumors appears to be associated with an absence of the K5-targeted molecules CD31, MHC-1, and β-Catenin in KSHV-infected lymphatic endothelial lesional cells. This striking inverse correlation between K5 and CD31/MHC- 1/β-Catenin expression supports a crucial role for K5 in modulating tumor cell function in proliferating KS lesions. Presenting author Email: fruehk@ohsu.edu 105
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