Tumor cell surface receptors mediating vaccinia viral entry

Tumor cell surface receptors mediating vaccinia viral entry comprise a diverse group of host molecules that the vaccinia virus (VACV) exploits to gain access to the cytoplasm. Unlike many viruses that rely on a single high-affinity receptor, VACV utilizes a multi-step entry process involving initial attachment to glycosaminoglycans, such as heparan sulfate and chondroitin sulfate, followed by interaction with protein receptors like integrin beta-1, CD98, and the epidermal growth factor receptor (EGFR). The virus often employs a strategy known as 'apoptotic mimicry,' where virion-associated phosphatidylserine engages host receptors like Axl and TIM-1 to trigger macropinocytosis. In the context of oncolytic virotherapy, these receptors are critical as they determine the tropism and efficacy of engineered vaccinia viruses, such as Pexa-Vec and CF33, which are designed to selectively infect and lyse cancer cells. Many tumors overexpress these entry factors, facilitating selective viral entry and subsequent oncolysis while inducing a systemic anti-tumor immune response. Understanding these complex interactions is essential for optimizing oncolytic agents and developing antiviral strategies to block poxvirus infection.

Other names

Vaccinia virus receptorsVACV entry factorsPoxvirus entry receptorsHost cell receptors for vaccinia virusVaccinia virus entry-mediating molecules

Oncolytic viral entry via receptor-mediated endocytosis or membrane fusion; Inhibition of viral entry and signaling pathways