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Cell entry of most alphaherpesviruses is mediated by the binding of glycoprotein D (gD) to different cell surface receptors. Equine herpesvirus type 1 (EHV-1) and EHV-4 gDs interact with equine major histocompatibility complex I (MHC-I) to initiate entry into equine cells. We have characterized the gD-MHC-I interaction by solving the crystal structures of EHV-1 and EHV-4 gDs (gD1, gD4), performing protein-protein docking simulations, surface plasmon resonance (SPR) analysis, and biological assays. The structures of gD1 and gD4 revealed the existence of a common V-set immunoglobulin-like (IgV-like) core comparable to those of other gD homologs. Molecular modeling yielded plausible binding hypotheses and identified key residues (F213 and D261) that are important for virus binding. Altering the key residues resulted in impaired virus growth in cells, which highlights the important role of these residues in the gD-MHC-I interaction. Taken together, our results add to our understanding of t ....
WASHINGTON (dpa-AFX) - Analytical instruments and software provider Waters Corp. (WAT), while reporting higher fourth-quarter profit and revenues, on Wednesday issued forecast for the first quarter ....
Waters Corp. in Milford plans to acquire light scattering technology company Wyatt Technology Corp. for $1.36 billion in cash. The deal is expected to close in the second quarter of 2023. ....
Global Label-free Detection (LFD) Market 2022-2026 The analyst has been monitoring the label-free detection (LFD) market and it is poised to grow by $362.. ....