BiP (grp78) is a chaperone protein which can also regulate the unfolded pro
tein response of the cell. Levels of BiP increased in cells infected by the
small plaque producing, cell associated, neuroinvasive strains of HSV-1 (S
P7, 490) but decreased in cells infected with KOS, a Barge plaque, attenuat
ed strain. BiP protein synthesis continued early in infection and BiP was s
equestered and its degradation was limited during SP7 infection. BiP protei
n synthesis stopped and the protein was degraded in KOS infected cells. The
se viral strain dependent differences in BiP concentration may influence ot
her aspects of the viral interaction with the target cell and its host. (C)
2001 Elsevier Science B.V. All rights reserved.