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- W2020796632 abstract "Herpes simplex virus type 1 (HSV-1) UL37 is a 1123 amino acid tegument protein that self-associates and binds to the tegument protein UL36 (VP1/2). Studies were undertaken to identify regions of UL37 involved in these protein-protein interactions. Coimmunoprecipitation assays showed that residues within the carboxy-terminal half of UL37, amino acids 568-1123, are important for interaction with UL36. Coimmunoprecipitation assays also revealed that amino acids 1-300 and 568-1123 of UL37 are capable of self-association. UL37 appears to self-associate only under conditions when UL36 is not present or is present in low amounts, suggesting UL36 and UL37 may compete for binding. Transfection-infection experiments were performed to identify domains of UL37 that complement the UL37 deletion virus, K∆UL37. The carboxy-terminal region of UL37 (residues 568-1123) partially rescues the K∆UL37 infection. These results suggest the C-terminus of UL37 may contribute to its essential functional role within the virus-infected cell." @default.
- W2020796632 created "2016-06-24" @default.
- W2020796632 creator A5013543863 @default.
- W2020796632 creator A5031999472 @default.
- W2020796632 creator A5075640001 @default.
- W2020796632 creator A5080949633 @default.
- W2020796632 date "2011-07-01" @default.
- W2020796632 modified "2023-10-10" @default.
- W2020796632 title "Identification of interaction domains within the UL37 tegument protein of herpes simplex virus type 1" @default.
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- W2020796632 doi "https://doi.org/10.1016/j.virol.2011.04.018" @default.
- W2020796632 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3617580" @default.
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