In silico prediction shows SARS-CoV-2 spike protein may interact with laminin (laminin β-1 and γ-1 subunits) because of spike protein’s mimicry of laminin, though the exact docking model is unpublished. [1] Experimental data seem to match with prediction in silico. Bamberger et al. (the paper you sent me) reported that immunoprecipitation using spike protein (especially S2) could pull down laminin β-3 and laminin γ-2. [2] Yapici-Eser et al. noted that “SARS-CoV-2 mimics various proteins that increase the vulnerability of thrombosis.” [1] I think spike S2 fusion coil probably mimics long helix on laminin and may engage in coiled-coil interaction with laminin β and γ. The HMI-Pred server predicts viral-human protein interaction by identifying interface mimicry. The algorithm performs two steps: 1) structural alignment (structural superposition) of viral protein with human protein at interface; 2) verification of binding by docking analysis at interface. Sadly, Yapici-Eser et al. didn’t publish a docking model of spike-laminin interaction. Maybe the post-fusion spike S2 mimics helical coil on laminin and engages trimeric coiled-coil interaction with laminin β and γ subunits. It would be helpful if Yapici-Eser et al. publish their docking model, but they didn’t. The exact binding mode is unknown. Their paper only showed a model of spike-fibrinogen interaction—the α-helical fusion coil of spike S2 appears to engage fibrinogen beta chain. [2] Look at the docking model between spike and fibrinogen. Although an intact spike protein probably won’t engage fibrinogen because S2 fusion coil is buried, binding may occur if the spike S2 fusion coil is exposed. In other words, the furin cleavage site may be the culprit. Large amounts of spike S2 fusion coil are surface-exposed after furin cleavage (post-fusion conformation), and perhaps this phenomenon leads to excess blood coagulation. According to Charles Rixley’s post, former vaccine researcher Philip Dormitzer said poly-basic cleavage motif [FCS] shouldn’t be included in influenza vaccines. I performed a structural superposition between laminin (PDB ID: 5XAU) and postfusion spike S2 (PDB ID: 6XRA) on Pymol. As shown in the attached picture, laminin α subunit is colored green, laminin β is colored cyan, laminin γ subunit is colored magenta, and spike monomer is colored orange. The postfusion spike S2 mimics laminin β in coil shape. By the way, nsp8 and nsp9 are predicted to bind glutamate receptor NMDAR by structural mimicry. [1] Maybe this is another factor in neurological impact of COVID. References: 1. Yapici-Eser H, Koroglu YE, Oztop-Cakmak O, Keskin O, Gursoy A, Gursoy-Ozdemir Y. Neuropsychiatric Symptoms of COVID-19 Explained by SARS-CoV-2 Proteins' Mimicry of Human Protein Interactions. Front Hum Neurosci. 2021 Mar 23;15:656313. doi: 10.3389/fnhum.2021.656313. PMID: 33833673; PMCID: PMC8021734. 2. Bamberger C, Pankow S, Martínez-Bartolomé S, Diedrich J, Park R, Yates J 3rd. The Host Interactome of Spike Expands the Tropism of SARS-CoV-2. bioRxiv [Preprint]. 2021 Feb 16:2021.02.16.431318. doi: 10.1101/2021.02.16.431318. Update in: J Proteome Res. 2023 Dec 1;22(12):3742-3753. doi: 10.1021/acs.jproteome.3c00387. PMID: 33619478; PMCID: PMC7899442.