Investigation of the specificity of the herpes simplex virus type 1 protease by point mutagenesis of the autoproteolysis sites | Zendy

P.J. McCann | Zendy; Donald R. O’Boyle | Zendy; Ingrid C. Deckman | Zendy

Open Access

Investigation of the specificity of the herpes simplex virus type 1 protease by point mutagenesis of the autoproteolysis sites

Author(s) -

P.J. McCann,

Donald R. O’Boyle,

Ingrid C. Deckman

Publication year - 1994

Publication title -

journal of virology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.617

H-Index - 292

eISSN - 1070-6321

pISSN - 0022-538X

DOI - 10.1128/jvi.68.1.526-529.1994

Subject(s) - biology , herpes simplex virus , point mutation , virology , mutagenesis , protease , virus , cleavage (geology) , herpesviridae , capsid , mutation , genetics , microbiology and biotechnology , enzyme , biochemistry , gene , viral disease , paleontology , fracture (geology)

The herpes simplex virus type 1 (HSV-1) protease is cleaved at two autoprocessing sites during viral maturation, one of which shares amino acid identity with its substrate, ICP35. Similar autoprocessing sites have been observed within other members of the Herpesviridae. Introduction of point mutations within the autoprocessing sites of the HSV-1 protease indicated that specificity resides within the P4-P1' region of the cleavage sites.

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