Engagement of new castle disease virus (NDV) matrix (M) protein with charged multivesicular body protein (CHMP) 4 facilitates viral replication

Abstract

Newcastle disease virus (NDV) causes heavy economic losses to poultry industry across the globe every year. Although NDV matrix (M) protein is involved in virus budding and our previous data indicate that in ovo expression of M protein facilitates NDV replication, the underlying mechanism for the role of M protein in NDV replication is not clear. Using yeast two-hybrid system and immunoprecipitation approaches, we found that M protein interacted with host vacuolar sorting protein charged multivesicular body protein (CHMP) 4B and 4C. In addition, the colocalization of M protein and CHMP4B/C could be observed using a laser confocal scanning microscope. Knockdown of CHMP4B by siRNA or transient expression of CHMP4B/C dominant negative forms markedly inhibited NDV growth in DF-1 cells. Thus, cellular CHMP4s play a critical role in NDV replication.