Serological analysis of herpes simplex virus types 1 and 2 with monoclonal antibodies.

The purpose of this study was to evaluate the performance of a herpes simplex virus (HSV) type 1-specific anti-glycoprotein C-1 monoclonal antibody (MAb) and a type 2-specific anti-glycoprotein G-2 MAb for typing of 2,400 clinical HSV-1 isolates and 2,400 clinical HSV-2 isolates, respectively, using an enzyme immunoassay. The anti-HSV-1 MAb showed sensitivity and specificity of 100%, and the anti-HSV-2 MAb showed a sensitivity of 99.46% and 100% specificity, indicating that these MAbs are suitable for typing of clinical HSV isolates.

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Processing of Herpes Simplex Virus Type 1 Glycoproteins: Two-dimensional Gel Analysis Using Monoclonal Antibodies

Journal of General Virology ◽

10.1099/0022-1317-64-4-873 ◽

1983 ◽

Vol 64 (4) ◽

pp. 873-886 ◽

Cited By ~ 9

Author(s):

J. W. Palfreyman ◽

L. Haarr ◽

A. Cross ◽

R. G. Hope ◽

H. S. Marsden

Keyword(s):

Monoclonal Antibodies ◽

Herpes Simplex Virus ◽

Herpes Simplex ◽

Virus Type ◽

Herpes Simplex Virus Type ◽

Two Dimensional ◽

Simplex Virus

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Monoclonal antibodies and human sera directed to the secreted glycoprotein G of herpes simplex virus type 2 recognize type-specific antigenic determinants

Journal of General Virology ◽

10.1099/0022-1317-83-1-157 ◽

2002 ◽

Vol 83 (1) ◽

pp. 157-165 ◽

Cited By ~ 20

Author(s):

Jan-Åke Liljeqvist ◽

Edward Trybala ◽

Johan Hoebeke ◽

Bo Svennerholm ◽

Tomas Bergström

Keyword(s):

Monoclonal Antibodies ◽

Herpes Simplex Virus ◽

Herpes Simplex ◽

Terminal Portion ◽

Glycoprotein G ◽

Infected Cells ◽

Simplex Virus ◽

Carboxy Terminal ◽

Hsv 1

Glycoprotein G-2 (gG-2) of herpes simplex virus type 2 (HSV-2) is cleaved to a secreted amino-terminal portion (sgG-2) and to a cell-associated carboxy-terminal portion which is further O-glycosylated to constitute the mature gG-2 (mgG-2). In contrast to mgG-2, which is known to elicit a type-specific antibody response in the human host, information on the immunogenic properties of sgG-2 is lacking. Here the sgG-2 protein was purified on a heparin column and used for production of monoclonal antibodies (mAbs). Four anti-sgG-2 mAbs were mapped using a Pepscan technique and identified linear epitopes which localized to the carboxy-terminal part of the protein. One additional anti-sgG-2 mAb, recognizing a non-linear epitope, was reactive to three discrete peptide stretches where the most carboxy-terminally located stretch was constituted by the amino acids 320RRAL323. Although sgG-2 is rapidly secreted into the cell-culture medium after infection, the anti-sgG-2 mAbs identified substantial amounts of sgG-2 in the cytoplasm of HSV-2-infected cells. All of the anti-sgG-2 mAbs were HSV-2 specific showing no cross-reactivity to HSV-1 antigen or to HSV-1-infected cells. Similarly, sera from 50 HSV-2 isolation positive patients were all reactive to sgG-2 in an enzyme immunoassay whilst no reactivity was seen in 25 sera from HSV-1 isolation positive patients or in 25 serum samples from HSV-negative patients suggesting that sgG-2 is a novel antigen potentially suitable for type-discriminating serodiagnosis.

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