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Arch Virol (2008) 153:17771781 DOI 10.1007/s00705-008-0183-x
BRIEF REPORT
Vimentin is required for dengue virus serotype 2 infection but microtubules are not necessary for this process
Wei Chen Na Gao Jia-li Wang Yan-ping Tian Zong-tao Chen Jing An
Received: 4 March 2008 / Accepted: 25 July 2008 / Published online: 10 August 2008 Springer-Verlag 2008
Abstract The present study investigated the effect of microtubules (MTs) and vimentin during dengue virus serotype 2 (DV2) infection. Immunostaining showed that DV2 infection induced MT and vimentin reorganization. Colocalization of DV2 antigens with MTs or vimentin were often observed in ECV304 cells. MT-disrupting agents could enhance DV2 release but did not affect other steps of virus replication. In contrast, disruption of vimentin inhibited DV2 infection. Our results suggest that an MT-dependent mechanism may not be necessary for DV2 infection, and MT disruption may promote DV2 release. However, vimentin is required for DV2 infection.
Dengue virus (DV) belongs to the family Flaviviridae, and there are four serotypes (DV1-4). They cause a mild-to-debilitating febrile illness (classical dengue fever, DF) or life-threatening syndrome (dengue haemorrhagic fever/ dengue shock syndrome, DHF/DSS). In recent years, the geographical range of DV infection in tropical and
subtropical regions of the world has extended, and DHF/ DSS is occurring in new areas and with increased incidence [11, 14].
Viruses are obligate intracellular parasites and therefore depend on the host cellular machinery to facilitate entry, replication, transport, and release of progeny virions [5]. The intricate structural system referred to as the cytoskeletal network is composed of actin, microtubules (MTs), intermediate laments (IFs), their motor protein and other elements [10]. Actin laments are exible structures which are organized into a variety of linear bundles and arrays, two-dimensional networks or three-dimensional gels. Myosins mediate translocation along actin laments. MTs are long, hollow cylinders assembled from heterodimers of a- and b-tubulin and MT-associated proteins (MAPs). Directional movement along MT is mediated by the motor proteins kinesin and cytoplasmic dynein [4, 17]. IFs with a diameter of 810 nm are found in nearly all eukaryotic cells and show a characteristic tripartite domain organization. Unlike actin and MTs, IFs do not participate in cell motility.
It has been reported that many viruses interact with cytoskeletal elements, which is considered to be critical at each...