Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4

Showalter, Stephen D.; Zweig, M; Hampar, Berge

doi:10.1128/iai.34.3.684-692.1981

Cited by 420 publications

(188 citation statements)

References 17 publications

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“…MAb 53S recognizes a discontinuous epitope and strictly requires gL for reactivity. MAb 52S recognizes a gL-independent discontinuous epitope with critical residues at position 536 to 537 (43,47). All three gH mutants maintained the reactivity to MAb 52S, suggesting no major defect in proper folding (data not shown).…”

Section: Methodsmentioning

confidence: 93%

“…COS or BHK cells were grown on glass coverslips, transfected with the indicated plasmids by means of Polyfect (QIAGEN), and fixed 48 h later with 4% paraformaldehyde for 10 min at room temperature. Samples were incubated with monoclonal antibodies (MAbs) 52S and 53S to gH (43,47) and fluorescein isothiocyanate-conjugated anti-mouse IgG (Jackson Immunoresearch) and observed with a Zeiss microscope. Micrographs were taken with a Kodak DC290 digital camera, as described previously (19).…”

Section: Methodsmentioning

confidence: 99%

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Heptad Repeat 2 in Herpes Simplex Virus 1 gH Interacts with Heptad Repeat 1 and Is Critical for Virus Entry and Fusion

Gianni¹,

Piccoli

Bertucci

et al. 2006

J Virol

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Herpes simplex virus 1 (HSV-1) entry into cells and cell-cell fusion mediated by HSV-1 glycoproteins require four glycoproteins, gD, gB, gH, gL. Of these, gH is the only one that so far exhibits structural-functional features typical of viral fusion glycoproteins, i.e., a candidate fusion peptide and, downstream of it, a heptad repeat (HR) segment able to form a coiled coil, named HR-1. Here, we show that gH carries a functional HR-2 capable of physical interaction with HR-1. Specifically, mutational analysis of gH aimed at increasing or decreasing the ability of HR-2 to form a coiled coil resulted in an increase or decrease of fusion activity, respectively. HSV infection was modified accordingly. A mimetic peptide with the HR-2 sequence inhibited HSV-1 infection in a specific and dose-dependent manner. Circular dichroism spectroscopy showed that both HR-2 and HR-1 mimetic peptides adopt mainly random conformation in aqueous solution, while a decrease in peptide environmental polarity determines a conformational change, with a significant increase of the ␣-helical conformation content, in particular, for the HR-1 peptide. Furthermore, HR-1 and HR-2 mimetic peptides formed a stable complex, as revealed in nondenaturing electrophoresis and by circular dichroism. The mixture of HR-1 and HR-2 peptides reversed the inhibition of HSV infection exerted by the single peptides. Complex formation between HR-1 and HR-2 was independent of the presence of adjacent gH sequences and of additional glycoproteins involved in entry and fusion. Altogether, HR-2 adds to the features typical of class 1 fusion glycoproteins exhibited by HSV-1 gH.Viral fusion glycoproteins are responsible for execution of fusion between the viral envelope and cell membranes. Key structural elements of class 1 viral fusion glycoproteins (e.g., the influenza virus hemagglutinin, the paramyxovirus F protein, human immunodeficiency virus gp41, Ebola virus, and severe acute respiratory syndrome coronavirus [CoV] glycoproteins) are the fusion peptide and heptad repeat (HR) sequences (12, 23). The fusion peptide is a hydrophobic ␣-helix able to penetrate the membrane of the target cell and destabilize it. Through it, the fusion glycoproteins form a bridge between the virion envelope and the cell membrane, an event that initiates fusion pore formation (12, 23). Following receptor binding, or induced by low pH, the trimeric fusion glycoproteins undergo a series of conformational changes and switch from the fusion-inactive to the fusion-active state. Critical for these changes are the HRs, usually two, termed HR-1 and HR-2, located downstream of the fusion peptide and upstream of the transmembrane segment, respectively. HR-1 forms a three ␣-helical structure termed a coiled coil, which is further modified to form a trimer of hairpins, also designated a six-helix bundle. In this structure, three HR-1 helices form a central coiled coil surrounded by three HR-2 helices in an oblique antiparallel orientation (23).Entry of herpes simplex virus (HSV) into the cell req...

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Section: Methodsmentioning

confidence: 93%

Section: Methodsmentioning

confidence: 99%

Heptad Repeat 2 in Herpes Simplex Virus 1 gH Interacts with Heptad Repeat 1 and Is Critical for Virus Entry and Fusion

Gianni¹,

Piccoli

Bertucci

et al. 2006

J Virol

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“…Preparation of monoclonal antibodies against the gB1 glycoprotein has been described by several laboratories [Pereira et al, 1981;Showalter et al, 1981;Holland et al, 1983;Marlin et al, 19861. Where the virusspecificity of the monoclonals has been reported, the majority have been classified a s cross-reactive (with gB2). If the monoclonals isolated thus far are assumed to reflect a representative account of the immunogenic epitopes present on gB, then it would appear that the majority of epitopes on gB are cross-reactive in nature.…”

Section: Discussionmentioning

confidence: 99%

Topological distribution of virus‐specific and cross‐reactive antigenic determinants on the gB glycoprotein of the herpes simplex viruses

Eberle

Courtney

1989

Journal of Medical Virology

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The antigenic properties and relations between the herpes simplex virus type 1 and 2 (HSV1, HSV2) gB glycoproteins were investigated. Using several assay systems to analyze the virus-specific reactivity of polyclonal monospecific rabbit anti-gB sera, it was demonstrated that most of the antigenic determinants of the gB glycoproteins exposed at the surface of both virions and infected cells are virus-specific rather than cross-reactive. Comparative examination of the reactivity of human immune sera with HSV1 and HSV2 antigens by immunoblotting also revealed differences in the ability of HSV1 and HSV2 immune sera to recognize homologous vs. heterologous gB antigens. These results indicate that despite the high degree of amino acid sequence homology which exists between the HSV1 and HSV2 gB glycoproteins many of the immunologically relevant antigenic determinants of the gB glycoproteins probably reside in regions of the molecule which are not so highly conserved between the two HSV serotypes.

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“…HSV proteins are degraded differentially in different cell lines after acute infections in cell culture. 19 Therefore, redundant antigenic sites on the virus-specific proteins 9°-23 may be either exposed or lost during the degradation process in macroplmges or other phagocytic cells, such as some choriodecidual cells and the Hofbauer cells of the chorionic villi. Tiffs uncertainty may make identification of specific HSV protdins by imnumohistochemistry and/or isolation difficult in subacute or chronic infections in animal tissues.…”

Section: Discussionmentioning

confidence: 99%

Intrauterine latent herpes simplex virus infection

Robb¹,

Benirschke²,

Barmeyer³

1986

Human Pathology

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Herpes simplex virus (HSV, probably type 2) antigen was detected in nonpregnant and pregnant endometria, placentae, umbilical cords, and neonatal tissues (companion paper) by avidin-biotin complex immunohistochemical studies. HSV cytologic abnormalities were not detected in any of the 380 cases examined: included were specimens from therapeutic and spontaneous abortions (200 cases) and endometrial curettage (180 cases). The presence of inflammation was not correlated with HSV positivity. Endometrial HSV positivity was significantly correlated with normal late secretory phase (40 per cent of specimens positive), abnormal secretory phase (67 per cent positive), and therapeutic (33 per cent positive) versus spontaneous (26 per cent positive) abortions. Placental HSV positivity was significantly correlated with spontaneous (39 per cent positive) versus therapeutic (14 per cent positive) abortions and with blighted ova (67 per cent positive). No significant correlation was found between HSV positivity and a clinical history of oral or genital HSV infection in either the patient or the male partner. The data support the concept of a subclinical latent intrauterine endometrial HSV infection that is hormonally regulated and can produce transplacental infection of the embryo or fetus, with variable consequences.

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Monoclonal antibodies to herpes simplex virus type 1 proteins, including the immediate-early protein ICP 4

Cited by 420 publications

References 17 publications

Heptad Repeat 2 in Herpes Simplex Virus 1 gH Interacts with Heptad Repeat 1 and Is Critical for Virus Entry and Fusion

Heptad Repeat 2 in Herpes Simplex Virus 1 gH Interacts with Heptad Repeat 1 and Is Critical for Virus Entry and Fusion

Topological distribution of virus‐specific and cross‐reactive antigenic determinants on the gB glycoprotein of the herpes simplex viruses

Intrauterine latent herpes simplex virus infection

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