Herpes simplex virus protein UL11 but not UL51 is associated with lipid rafts.
The UL11 and UL51 gene products of herpes simplex virus (HSV) are membrane-associated tegument proteins that are incorporated into the HSV virion. UL11 and UL51 are conserved throughout the herpesvirus family. Both UL11 and UL51, either singly or in combination, are involved in virion envelopment and/or egress. Both proteins are fatty acylated: UL11 is both acylated by myristoic and palmitoic acids and UL51 is monoacylated by palmitoic acid. Using confocal microscopy and sucrose gradient fractionations in transfected or HSV-infected cells, we found that HSV-2 UL11 but not UL51 was associated with lipid rafts. The dual acylation of UL11 was necessary for lipid raft association, as mutations in the myristoylation or palmitoylation sites prevented lipid raft association. These differences in lipid raft association may contribute to the functional differences between UL11 and UL51.
Koshizuka
Tetsuo
T
Department of Virology, Nagoya University Graduate School of Medicine, Showa-ku, Nagoya 466-8550, Japan.
Kawaguchi
Yasushi
Y
Nozawa
Naoki
N
Mori
Isamu
I
Nishiyama
Yukihiro
Y
D000215:Acylation; D000818:Animals; D002458:Cell Fractionation; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D002522:Chlorocebus aethiops; D004285:Dogs; D006801:Humans; D021962:Membrane Microdomains / Q000737:chemistry*; D018613:Microscopy, Confocal; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D018139:Simplexvirus / Q000502:physiology*; D015678:Viral Structural Proteins / Q000032:analysis*
C073414:UL11 protein, herpesviridae; C525998:UL51 protein, HSV-2; D015678:Viral Structural Proteins
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