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. 1986 Dec;60(3):1130–1133. doi: 10.1128/jvi.60.3.1130-1133.1986

Neutralization of herpes simplex virus ribonucleotide reductase activity by an oligopeptide-induced antiserum directed against subunit H2.

E A Cohen, P Gaudreau, P Brazeau, Y Langelier
PMCID: PMC253364  PMID: 2431161

Abstract

Herpes simplex virus type 1 ribonucleotide reductase is associated with two polypeptides of apparent molecular weights 136,000 and 38,000. The two polypeptides form a tight complex and, therefore, are often coprecipitated by monoclonal antibodies. We report here that immunoglobulins G purified from polyclonal rabbit antisera (P9) raised against a nonapeptide corresponding to the carboxy terminus of the 38,000-dalton polypeptide specifically neutralize the herpes simplex virus ribonucleotide reductase activity. We suggest that the P9 immunoglobulin G neutralizes the reductase activity by impairing the association of the two subunits (H1 and H2) of the enzyme.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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