The herpes simplex virus type 1(HSV-1) VP22,is one of the most abundant HSV-1 tegument proteins with an average stoichiometry of 2 400 copies per virion and conserved among alphaherpesvirinae. Many functions are attributed to VP22,including nuclear localization,chromatin binding,microtubule binding,induction of microtubule reorganization,intercellular transport,interaction with cellular proteins,such as template activating factor I(TAF-I) and nonmuscle myosin II A(NMIIA) ,and viral proteins including tegument protein VP16,pUS9 and pUL46,glycoprotein E(gE) and gD. Recently,many novel functions performed by the HSV-1 VP22 protein have been shown,including promotion of protein synthesis at late times in infection,accumulation of a subset of viral mRNAs at early times in infection and possible transcriptional regulation function.
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