Vaccinia virus entry receptors and host factors

Olvi-Vec (olvimulogene nanivacirepvec) is an oncolytic virus derived from the Lister strain of vaccinia virus (VACV), engineered to selectively infect, replicate in, and lyse tumor cells. The entry of Olvi-Vec into host cells is a complex, multi-step process that does not rely on a single high-affinity receptor but instead exploits a broad range of host factors and attachment molecules (Schmidt et al., 2012, PLoS Pathogens). Primary attachment is typically mediated by glycosaminoglycans (GAGs) such as heparan sulfate and chondroitin sulfate, which are often abundant on the surface of cancer cells (Chung et al., 1998, J. Virol.). The virus also employs "apoptotic mimicry," where the viral envelope displays phosphatidylserine to engage host receptors like AXL, MERTK, or TIM-1, thereby triggering macropinocytosis for viral internalization (Mercer and Helenius, 2008, Science). Furthermore, host proteins such as integrin beta-1 (ITGB1) and CD98 have been implicated in facilitating the fusion of the viral envelope with the host cell membrane (Izmailyan et al., 2012, J. Virol.). Once inside the cell, Olvi-Vec relies on host intracellular machinery, including the actin cytoskeleton and various signaling kinases, to complete its replication cycle and spread to adjacent cells. In clinical oncology, the expression levels of these entry factors in the tumor microenvironment can influence the efficacy and selectivity of Olvi-Vec therapy.

Other names

Olvi-Vec entry factorsGL-ONC1 host factorsVaccinia virus attachment factorsVACV entry receptors

Olvi-Vec (GL-ONC1) utilizes a variety of host cell surface molecules, such as heparan sulfate and integrins, to facilitate viral attachment and membrane fusion or endocytosis, enabling the virus to enter and replicate within tumor cells.