The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.

Title:

The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.

Dataset

identifier:	1418773
description:	epitope description:VFTGVLAGVWGEGGKFVYPFDDKMSFLFA antigen name:DNA helicase/primase complex-associated protein host organism:Mus musculus antibody name:MAb 817, 818, 819
aggregation:	instance of dataset
availability:	available
primaryPublications:	9261356

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1004169
landingPage:	http://www.iedb.org/assay/1418773

Publication

type:	Literature
publicationVenue:	J Virol
dates:	1997

Dimension

study type:	b cell assays
subject species:	Human alphaherpesvirus 1

Person

fullName:	H S Marsden G W McLean E C Barnard G J Francis K MacEachran M Murphy G McVey A Cross A P Abbotts N D Stow

Data Type

method:	biological activity

Study

name:	The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.
description:	All three of the mAbs that recognized the epitope in the C-terminus of UL8 were capable of inhibiting the interaction between UL8 (helicase-primase protein) and the polymerase (POL). The epitope was also shown to inhibit the interaction of the UL8 helicase to the POL polymerase directly. This was detected by POL-specific mAb 13185 in a separate assay (IC50 = 66uM).

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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