Amino acids 143 to 150 of the herpes simplex virus type 1 scaffold protein are required for the formation of portal-containing capsids.

Journal of Virology
Jamie B HuffmanFred L Homa

Abstract

The herpes simplex virus type 1 (HSV-1) portal is composed of a dodecamer of UL6 protein molecules whose incorporation into the capsid is mediated by interaction with the HSV-1 UL26.5 scaffold protein. Previous results with an in vitro capsid assembly assay demonstrated that nine amino acids (amino acids 143 to 151) of the UL26.5 protein are required for its interaction with UL6 and for incorporation of the portal complex into capsids. In the present study an HSV-1 mutant, bvFH411, was isolated and contained a deletion that removed the codons for UL26.5 amino acids 143 to 150. The mutant virus failed to produce infectious virus in noncomplementing cells, and only B capsids that contained only minor amounts of portal protein were made. These data corroborate our previous in vitro studies and demonstrate that amino acids 143 to 150 of UL26.5 are required for the formation of portal-containing HSV-1 capsids.

References

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Citations

Sep 20, 2011·Current Opinion in Virology·Jay C Brown, William W Newcomb
Mar 25, 2018·Reviews in Medical Virology·Ellyn M Kornfeind, Robert J Visalli
Dec 19, 2019·Frontiers in Microbiology·Fatai S OladunniThomas M Chambers
Apr 7, 2018·Science·Shuai YuanXiangxi Wang
Sep 25, 2020·Journal of Virology·Alexis HuetFred L Homa

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