Richard J. Courtney

Pennsylvania State University

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Priscilla A. Schaffer

Baylor College of Medicine

Matilda Benyésh-Melnick

Baylor College of Medicine

John W. Wills

Pennsylvania State University

R. Eberle

Oklahoma State University

Kevin J. O’Regan

Fox Chase Cancer Center

Michelle A. Bucks

Pennsylvania State University

Gordon R. Dreesman

Texas Biomedical Research Institute

Joseph L. Melnick

Baylor College of Medicine

Michael A. Murphy

University of Houston

Kenneth L. Powell

Stevenage Bioscience Catalyst

Cooperative Institutions

Baylor College of Medicine

Pennsylvania State University

National Institutes of Health

Harvard University

University of Tennessee at Knoxville

University Medical Center

University of Pennsylvania

Institute of Virology of the Slovak Academy of Sciences

National Cancer Institute

Cancer Research Center

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Endo-beta-N-acetylglucosaminidase H sensitivity of precursors to herpes simplex virus type 1 glycoproteins gB and gC

Journal of Virology (1982)

E A Wenske M W Bratton Richard J. Courtney

The endoglycosidase endo-beta-N-acetylglucominidase H (endo H) was used to examine the nature of the oligosaccharides associated with the herpes simplex virus type 1 glycoproteins gA, gB, and gC. Immunoprecipitates from detergent extracts of infected cells, using monospecific antisera to gAB and gC, were treated with endo H. The low-molecular-weight precursor to gC, pgC(105), was found to be sensitive to endo H. Removal of the endo H-sensitive oligosaccharide chains from pgC(105) resulted in a protein with an apparent molecular weight of 75,000. In contrast, the fully glycosylated gC was not sensitive to endo H treatment. These results suggested that the oligosaccharide chains of pgC(105) were primarily of the simple high-mannose type. Both gA and gB were sensitive to endo H treatment; however, gB appeared to be only partially susceptible, whereas [3H]mannose-labeled gA was not detectable after endo H treatment. These results that gB contained both complex- and simple-type oligosaccharides, and gA contained only simple-type oligosaccharides. An accumulation of the high-mannose glycoproteins pgC(105) and gA was observed in monensin-treated infected cells with a concomitant inhibition of gB and gC. Glycoproteins gA and pgC(105) synthesized in the presence of monensin were also sensitive to endo H treatment.

Monensin

Endoglycosidase

Endoglycosidase H

Oligosaccharide

10.1128/jvi.44.1.241-248.1982

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Citations (94)

Antibody to Herpes Simplex Virus Type 2-Induced Nonstructural Proteins in Women With Cervical Cancer and in Control Groups<xref ref-type="fn" rid="fn2"><sup>2</sup></xref>

JNCI Journal of the National Cancer Institute (1975)

Takashi Anzai Gordon R. Dreesman Richard J. Courtney E Adám William E. Rawls

Sera obtained from 15 patients with cervical cancer, 10 patients with breast cancer, and 15 control women, individually matched with the cervical cancer patients, were examined for antibodies to early proteins synthesized in herpes simplex virus type 2 (HSV-2)-infected cells. The method used was an indirect radioimmune precipitation test followed by polyacrylamide gel electrophoretic analysis of immune precipitates. The relative reactivity to a major early nonstructural protein (VP134) was used to compare these selected sera. The results obtained suggest that cervical cancer patients possess sera with a higher reactivity to VP134 than breast cancer patients or matched healthy women,and that serum reactivity is independent of the level of neutralizing antibodies to HSV-2.

10.1093/jnci/54.5.1051

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Citations (33)

Thymidine Kinase Activity of Herpes Simplex Virus Temperature-Sensitive Mutants

Intervirology (1973)

Gary M. Aron Priscilla A. Schaffer Richard J. Courtney Matilda Benyésh-Melnick Saul Kit

Eighteen temperature-sensitive (ts) mutants of herpes simplex virus type 1 were studied with regard to their ability to synthesize virus-induced thymidine kinase (TK) at permissive (34°) and nonpermissive (39°) temperatures. Five mutants were TK– at both temperatures (TK– mutants), 10 were TK+ at both temperatures (TK+ mutants) and 3 showed reduced TK activity at 39° but not at 34° (TK± mutants). Two of the 3 TK± mutants were ts in the production of TK at 39° while the third mutant synthesized a ts TK at both temperatures. Polyacrylamide gel electrophoresis of extracts of both uninfected and TK-mutant-infected cells exhibited one major and one minor peak of TK activity, whereas extracts of wild-type (WT) virus-infected cells revealed at least one additional major peak of TK activity. Gel patterns of TK± mutants were similar to those of the WT virus in 34 and 39° extracts; however, a reduction in TK activity of the viral peaks was observed in 39° extracts.

Thymidine kinase

Thymidine

Wild type

10.1159/000148836

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Citations (32)

Glycosylation of herpes simplex virus type 1 gC in the presence of tunicamycin

Journal of Virology (1983)

E A Wenske Richard J. Courtney

The presence of O-glycosidic linkages on herpes simplex virus type 1 (HSV-1) glycoproteins was indicated by the synthesis and glycosylation of HSV-1 glycoproteins in the presence of tunicamycin. Monospecific antiserum to HSV-1 gC immunoprecipitated a 92,000-molecular-weight protein synthesized in the presence of tunicamycin and isotopically labeled with glucosamine or galactose. Anti-gAB did not immunoprecipitate a carbohydrate-labeled HSV-1 protein synthesized in the presence of tunicamycin. The purified glucosamine-labeled 92,000-molecular-weight protein synthesized in the presence of tunicamycin and the fully glycosylated forms of gAB and gC were tested for their sensitivity to mild alkaline hydrolysis. Purified gAB was resistant to mild alkaline hydrolysis, whereas gC and the 92,000-molecular-weight protein were both sensitive to mild alkaline hydrolysis. These results suggest that O-glycosidic linkages are associated with the HSV-1 gC glycoprotein.

Tunicamycin

Immunoprecipitation

Glycosidic bond

10.1128/jvi.46.1.297-301.1983

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Citations (33)

Herpes simplex virus type 1-specific cytotoxic T lymphocytes recognize virus nonstructural proteins

Journal of Virology (1988)

Stephen J. Martin Richard J. Courtney Gerissa Fowler Barry T. Rouse

The specificity of herpes simplex virus type 1-specific cytotoxic T cells was examined with target cells expressing either input viral structural antigens or antigens resulting from permissive infection or cells from an interrupted infection in which they expressed predominantly nonstructural immediate-early proteins. These studies indicated that only an insignificant minority of cytotoxic T cells recognized the input viral antigens, whereas a significant proportion (20 to 35%) recognized target cells that expressed the immediate-early proteins despite the absence of serologically detectable viral antigens upon the infected cell surface. The finding that a significant proportion of cytotoxic T-cell populations obtained from the draining lymph nodes of mice acutely infected with herpes simplex virus type 1 also recognized immediately-early gene-expressing target cells indicates the importance of nonstructural herpes simplex virus proteins to antiviral immunity in vivo.

10.1128/jvi.62.7.2265-2273.1988

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Citations (78)

Varia

Intervirology (1979)

Howard L. Bachrach Donald O. Morgan Douglas M. Moore Eng‐Chun Mar Eng‐Shang Huang

10.1159/000149080

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Citations (1)

Synthesis of the gB and gC glycoproteins of herpes simplex virus type 1 in the absence of viral DNA synthesis

Virus Research (1984)

Teresa Compton Richard J. Courtney

Herpesvirus glycoprotein B

Simplexvirus

10.1016/0168-1702(84)90050-9

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Structural Proteins of Pichinde Virus

Journal of Virology (1972)

Blanca Arellano Ramos Richard J. Courtney William E. Rawls

Pichinde virus, a member of the arenovirus group, was found to have four polypeptides by polyacrylamide gel electrophoresis. Two components, V(I) and V(II), had molecular weights of about 72,000, whereas V(III) had a molecular weight of 34,000. A minor component, V(IV), had a molecular weight of about 12,000. Glucosamine was incorporated into V(II) and V(III), suggesting that these components were glycopeptides whereas V(I) and V(IV) were polypeptides. Treatment of the virus with Nonidet P-40 removed V(III), but V(I) and V(II) remained associated with the virus nucleic acid. This suggests a functional role of a ribonucleoprotein for V(I) and an envelope glycoprotein for V(III). V(II), the major glycopeptide, could function both as a membrane component and as a nucleoprotein.

Nucleoprotein

Molecular mass

Arenavirus

10.1128/jvi.10.4.661-667.1972

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Citations (39)

Characterization of the large tegument protein (ICP1/2) of herpes simplex virus type 1

Virology (1992)

David S. McNabb Richard J. Courtney

Viral tegument

Immunofluorescence

Cell fractionation

Polyclonal antibodies

10.1016/0042-6822(92)91208-c

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Citations (89)

Viral Gene Functions Expressed and Detected by Temperature-sensitive Mutants of Herpes Simplex Virus

Cold Spring Harbor Symposia on Quantitative Biology (1974)

Matilda Benyésh-Melnick P A Schaffer Richard J. Courtney José Esparza Shoji Kimura

Herpes simplex virus (HSV) is a member of a widespread group of relatively large DNA viruses, some of which have been associated recently with malignancies in man and animals (Klein 1972). Two types of HSV are recognized, type 1 (HSV-1) and type 2 (HSV-2), which share many properties in common but differ in certain biologic, immunologic and biochemical properties (Ejercito et al. 1968; Nahmias et al. 1968; Figueroa and Rawls 1969; Plummer et al. 1970; Roizman et al. 1972). Epidemiologic and virologic evidence has indicated a close association between HSV-2 and cervical cancer (Rawls et al. 1969; Nahmias et al. 1970; Royston and Aurelian 1970; Frenkel et al. 1972). Transformation of cultured mammalian cells has been accomplished with HSV-2 (Duff and Rapp 1971; Kutinova et al. 1973) and with HSV-1 (Munyon et al. 1971; Davidson et al. 1973; Duff and Rapp 1973; Garfinkle and McAuslan 1974).

10.1101/sqb.1974.039.01.086

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Citations (26)