ArticleInternational journal of molecular sciences2026
In Silico Modeling of Structural Compatibility and Alignment Between Viral Class I Fusion Cores and Human TLR4/MD-2.
Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The SARS-CoV-2 spike protein has been shown to activate Toll-like receptor 4 (TLR4), yet the precise molecular structures driving recognition and subsequent activation remain poorly defined. Here, we present in silico structural alignments and molecular docking simulations indicating potential spatial compatibility between the wild-type SARS-CoV-2 HR1HR2 fusion core and the human TLR4/MD-2 heterodimer. The computational models project candidate interfaces involving salt bridges, as well as polar and non-polar interactions, with both TLR4 and MD-2 dimerization partners, suggesting a theoretical topology compatible with the dimerization of two TLR4/MD-2 heterocomplexes. Notably, similar structural compatibility was modeled for related class I fusion proteins from other highly pathogenic viruses, including SARS-CoV, MERS-CoV, influenza viruses A, B, and C, respiratory syncytial virus (RSV), and partially Ebola virus. These findings offer an exploratory computational hypothesis regarding viral-host interactions with the host innate immune system, which can trigger immune recognition or detrimental hyperactivation.
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