• Coxsackievirus;
  • HUVEC;
  • F-actin;
  • ZO-1;
  • p38 MAPK


Tight junction (TJ) plays a pivotal role in preventing the invasion of pathogens from the blood to extracellular environment. However, the mechanisms by which Group B coxsackievirus 3 (CVB3) can get through TJ from the apical surface still remain obscure. In the present study, the human umbilical vein endothelial cell (HUVEC) was utilized to investigate the alterations in F-actin and ZO-1 status, permeability as well as p38 mitogen-activated protein kinase (MAPK) activity in response to CVB3 by means of fluorescence labeling, flow cytometry, and macromolecule permeability assay. We found that CVB3 was able to induce reorganization of F-actin and redistribution of ZO-1, increase the level of F-actin, and elevate the permeability of FITC-albumin. Moreover, CVB3-mediated the above effects involve in P38 MAPK activation. Our preliminary study indicates that CVB3-induced alteration in permeability may be attributed to disruption of F-actin and ZO-1 organizations and that SB203580, a specific P38 MAPK inhibitor, can reverse these effects. The precise mechanisms underlying the CVB3-mediated effects on HUVECs need to be studied further.