The early activation of FLIP suggests that it would also be induced by VLPs. We therefore anticipate that like SV40 vectors, VLPs might also be non-immunogenic, allowing repeated treatments. Of note, FLIP activation by SV40 may be another anti-apoptotic renal protective mechanism, in addition to AKT activation and Hsp70 upregulation. In this proof-of-principle therapeutic study we showed that VLP administration conferred protection BEZ235 against HgCl2-induced AKI, presumably via activation of the Akt-1 survival pathway and chaperones. Production of VLPs is a simple, low cost procedure, and the absence of genetic material circumvents inherent risks of gene therapy. Thus this strategy may potentially be developed as a preventative medical measure against AKI. VLPs protected human HEK293 and monkey CV-1 cells also against etoposide-induced apoptosis, suggesting wide range applicability of VLPs for cell and tissue survival. SV40-based vectors were shown to reach many targets in vivo. Numerous reports suggest that Akt survival pathway and chaperones are involved in many types of organ failure, not just the kidney. Thus the findings described here may be extended to additional clinical conditions. Furthermore, viruses have evolved to enter cells by a variety of mechanisms, inducing a wide array of cellular responses. One may predict that virus-induced host signaling would by applicable as novel medical modalities to a large spectrum of diseases. Herpes simplex virus type-1 is a worldwide health problem that causes a wide range of diseases. It is a leading cause of infectious corneal blindness in the developed world and sporadic, fatal encephalitis worldwide. The virus also causes asymptomatic life-long infections in a majority of adult human population and uses a clever way of spreading from cell-to-cell to avoid detection by the host immune system. Absence of an effective vaccine or ICI 182780 microbicide against latent or recurrent HSV, and the fast emerging drug-resistant virus isolates highlight the need for developing new antivirals for HSV-1. Therefore, characterizing the molecular basis of HSV-1 entry into host cells and the viral-cellular interactions involved in viral spread are crucial for the development of new approaches to prevent the infection. HSV-1 follows different entry routes depending on the type of the cell it infects. It can fuse at the plasma membrane, enter via endocytosis, or get captured by cells in a phagocytosis-like manner and fuse with the phagosomal membrane. Five HSV-1 glycoproteins are known to be involved in HSV-1 entry, and these are HSV-1 glycoproteins gB, gC, gD, gH, and gL. The glycoprotein gC is not essential for entry, and in its absence the virus can still enter the host cell.