Senecavirus A capsid protein complex (SVV capsid) (SVV capsid)

The Senecavirus A capsid protein complex, commonly referred to as the Seneca Valley Virus (SVV) capsid, is the icosahedral protein shell of a non-enveloped, positive-strand RNA virus [Hales et al., 2008]. It is composed of 60 repeating protomers, each containing the structural proteins VP1, VP2, VP3, and VP4 [Cao et al., 2018]. The capsid is of significant therapeutic interest due to its highly selective tropism for Anthrax Toxin Receptor 1 (ANTXR1), also known as Tumor Endothelial Marker 8 (TEM8), which is frequently overexpressed in various solid tumors but has limited expression in normal tissues [Miles et al., 2017]. In the context of oncolytic virotherapy, the SVV capsid serves as the targeting mechanism for the therapeutic agent SVV-001, facilitating selective viral entry and subsequent destruction of malignant cells [Rudin et al., 2011]. Clinical development has demonstrated the capsid's efficacy in targeting neuroendocrine and pediatric tumors, though its use is challenged by the rapid induction of host neutralizing antibodies that can limit the effectiveness of repeated systemic administration [Burke et al., 2015; Liu et al., 2021]. Research continues into engineering the capsid surface to reduce immunogenicity and optimize tumor-specific binding [Cao et al., 2018].

Other names

Seneca Valley Virus capsidSVV-001 capsidSenecavirus A structural proteinsVP1-VP2-VP3-VP4 complex

The capsid mediates selective attachment to the ANTXR1 (TEM8) receptor on the surface of target cells, triggering receptor-mediated endocytosis and subsequent viral replication leading to cell death (oncolysis) [Miles et al., 2017; Cao et al., 2018].