Kunlakanya JitoboamNarumon PhaonakropSirikwan LibsittikulChutima ThepparitSittiruk RoytrakulDuncan R. SmithMahidol UniversityThailand National Science and Technology Development Agency2018-12-112019-03-142018-12-112019-03-142016-03-01PLoS ONE. Vol.11, No.3 (2016)193262032-s2.0-84962106655https://repository.li.mahidol.ac.th/handle/20.500.14594/41092© 2016 Jitoboam et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Dengue virus (DENV) remains a significant public health problem in many tropical and subtropical countries worldwide. The DENV envelope (E) protein is the major antigenic determinant and the protein that mediates receptor binding and endosomal fusion. In contrast to some other DENV proteins, relatively few cellular interacting proteins have been identified. To address this issue a co-immuoprecipitation strategy was employed. The predominant co-immunoprecipitating proteins identified were actin and actin related proteins, however the results suggested that actin was the only bona fide interacting partner. Actin was shown to interact with the E protein of DENV 2 and 4, and the interaction between actin and DENV E protein was shown to occur in a truncated DENV consisting of only domains I and II. Actin was shown to decrease during infection, but this was not associated with a decrease in gene transcription. Actin-related proteins also showed a decrease in expression during infection that was not transcriptionally regulated. Cytoskeletal reorganization was not observed during infection, suggesting that the interaction between actin and E protein has a cell type specific component.Mahidol UniversityAgricultural and Biological SciencesBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1371/journal.pone.0151951