Fig. 7: Visual abstract of the interaction between laminins and H-1PV.
From: Oncolytic H-1 parvovirus binds to sialic acid on laminins for cell attachment and entry
Laminin γ1 chains form various heterotrimer complexes with α (1–5) chains and β (1–4) chains. In this study, we discovered that laminins are required for the attachment of H-1PV at the cell surface. H-1PV binding to laminins occurs via sialic acid moieties; neuraminidase (NA), which cleaves sialic acid, inhibits the interaction. Although heparin (H) is unable to bind directly to the H-1PV capsid (not illustrated), it prevents H-1PV from binding to laminins, probably by competing with the virus for the heparin-binding domains (HBD) present on laminins. The model was created by using Biorender.com.
