The U(L)17 protein (pU(L)17) of herpes simplex virus 1 (HSV-1) likely associates with the surfaces of DNA-containing capsids in a heterodimer with pU(L)25. pU(L)17 is also associated with viral light particles that lack capsid proteins, suggesting its presence in the tegument of the HSV-1 virion. To help determine how pU(L)17 becomes incorporated into virions and its functions therein, we identified pU(L)17-interacting proteins by immunoprecipitation with pU(L)17-specific IgY at 16 h postinfection, followed by mass spectrometry.
View Article and Find Full Text PDFLipophosphoglycan (LPG) is an abundant surface molecule that plays key roles in the infectious cycle of Leishmania major. The dominant feature of LPG is a polymer of phosphoglycan (PG) (6Galbeta1,4Manalpha1-PO(4)) repeating units. In L.
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