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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/43093
Title: WSV399, a viral tegument protein, interacts with the shrimp protein PmVRP15 to facilitate viral trafficking and assembly
Authors: Phattarunda Jaree
Saengchan Senapin
Ikuo Hirono
Chu Fang Lo
Anchalee Tassanakajon
Kunlaya Somboonwiwat
Chulalongkorn University
Mahidol University
Thailand National Center for Genetic Engineering and Biotechnology
National University Corporation Tokyo University of Marine Science and Technology
National Cheng Kung University
Keywords: Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology
Issue Date: 1-Jun-2016
Citation: Developmental and Comparative Immunology. Vol.59, (2016), 177-185
Abstract: © 2016 Elsevier Ltd. Viral responsive protein 15 (PmVRP15) has been identified as a highly up-regulated gene in the hemocyte of white spot syndrome virus (WSSV)-infected shrimp Penaeus monodon. However, the function of PmVRP15 in host-viral interaction was still unclear. To elucidate PmVRP15 function, the interacting partner of PmVRP15 from WSSV was screened by yeast two-hybrid assay and then confirmed by co-immunoprecipitation (Co-IP). Only WSV399 protein was identified as a PmVRP15 binding protein; however, the function of WSV399 has not been characterized. Localization of WSV399 on the WSSV virion was revealed by immunoblotting analysis (in vitro) and immunoelectron microscopy (in vivo). The results showed that WSV399 is a structural protein of the WSSV virion and is particularly located on the tegument. Gene silencing of wsv399 in WSSV-infected shrimp reduced the percentage of cumulative mortality by 74%, although the expression level of a viral replication marker gene, vp28, was not changed suggesting that WSV399 might not involved in viral replication but viral assembly. Because it has already been known that tegument proteins function in capsid transport during viral trafficking and assembly, interaction between PmVRP15 on hemocyte nuclear membrane and the WSV399 viral tegument protein suggests that PmVRP15 might be required for trafficking and assembly of WSSV during infection.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84957892308&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/43093
ISSN: 18790089
0145305X
Appears in Collections:Scopus 2016-2017

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