Modified FGF4 Signal Peptide Inhibits Entry of Herpes Simplex Virus Type 1

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Published in	Journal of Virology Vol. 75; no. 6; pp. 2634 - 2645
Main Authors	Bultmann, H, Busse, J S, Brandt, C R
Format	Journal Article
Language	English
Published	United States American Society for Microbiology 01.03.2001 American Society for Microbiology (ASM)
Subjects	Animals Chlorocebus aethiops Fibroblast Growth Factors Herpes Simplex - virology Herpes simplex virus 1 Herpesvirus 1, Human - drug effects Herpesvirus 1, Human - pathogenicity Herpesvirus 1, Human - physiology Peptides - chemical synthesis Peptides - chemistry Peptides - metabolism Peptides - pharmacology Protein Sorting Signals Vero Cells Viral Plaque Assay Virion - metabolism Virus-Cell Interactions
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Abstract	Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: JVI
AbstractList	Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue JVI About JVI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JVI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0022-538X Online ISSN: 1098-5514 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JVI .asm.org, visit: JVI Entry of herpes simplex virus type 1 (HSV-1) into host cells occurs through fusion of the viral envelope with the plasma membrane and involves complex and poorly understood interactions between several viral and cellular proteins. One strategy for dissecting the function of this fusion machine is through the use of specific inhibitors. We identified a peptide with antiviral activity that blocks HSV-1 infection at the entry stage and during cell-to-cell spreading. This peptide (called EB for "entry blocker") consists of the FGF4 signal sequence with an RRKK tetramer at the amino terminus to improve solubility. The activity of EB depends exclusively but not canonically on the signal sequence. Inhibition of virus entry (hrR3) and plaque formation (KOS) strongly depend on virus concentrations and serum addition, with 50% inhibitory concentrations typically ranging from 1 to 10 microM. Blocking preadsorbed virus requires higher EB concentrations. Cytotoxic effects (trypan blue exclusion) are first noted at 50 microM EB in serum-free medium and at > or = 200 microM in the presence of serum. EB does not affect gC-dependent mechanisms of virus attachment and does not block virus attachment at 4 degrees C. Instead, EB directly interacts with virions and inactivates them irreversibly without, however, disrupting their physical integrity as judged by electron microscopy. At subvirucidal concentrations, EB changes the adhesive properties of virions, causing aggregation at high virus concentrations. This peptide may be a useful tool for studying viral entry mechanisms. Entry of herpes simplex virus type 1 (HSV-1) into host cells occurs through fusion of the viral envelope with the plasma membrane and involves complex and poorly understood interactions between several viral and cellular proteins. One strategy for dissecting the function of this fusion machine is through the use of specific inhibitors. We identified a peptide with antiviral activity that blocks HSV-1 infection at the entry stage and during cell-to-cell spreading. This peptide (called EB for “entry blocker”) consists of the FGF4 signal sequence with an RRKK tetramer at the amino terminus to improve solubility. The activity of EB depends exclusively but not canonically on the signal sequence. Inhibition of virus entry ( hr R3) and plaque formation (KOS) strongly depend on virus concentrations and serum addition, with 50% inhibitory concentrations typically ranging from 1 to 10 μM. Blocking preadsorbed virus requires higher EB concentrations. Cytotoxic effects (trypan blue exclusion) are first noted at 50 μM EB in serum-free medium and at ≥200 μM in the presence of serum. EB does not affect gC-dependent mechanisms of virus attachment and does not block virus attachment at 4°C. Instead, EB directly interacts with virions and inactivates them irreversibly without, however, disrupting their physical integrity as judged by electron microscopy. At subvirucidal concentrations, EB changes the adhesive properties of virions, causing aggregation at high virus concentrations. This peptide may be a useful tool for studying viral entry mechanisms. ABSTRACT Entry of herpes simplex virus type 1 (HSV-1) into host cells occurs through fusion of the viral envelope with the plasma membrane and involves complex and poorly understood interactions between several viral and cellular proteins. One strategy for dissecting the function of this fusion machine is through the use of specific inhibitors. We identified a peptide with antiviral activity that blocks HSV-1 infection at the entry stage and during cell-to-cell spreading. This peptide (called EB for “entry blocker”) consists of the FGF4 signal sequence with an RRKK tetramer at the amino terminus to improve solubility. The activity of EB depends exclusively but not canonically on the signal sequence. Inhibition of virus entry ( hr R3) and plaque formation (KOS) strongly depend on virus concentrations and serum addition, with 50% inhibitory concentrations typically ranging from 1 to 10 μM. Blocking preadsorbed virus requires higher EB concentrations. Cytotoxic effects (trypan blue exclusion) are first noted at 50 μM EB in serum-free medium and at ≥200 μM in the presence of serum. EB does not affect gC-dependent mechanisms of virus attachment and does not block virus attachment at 4°C. Instead, EB directly interacts with virions and inactivates them irreversibly without, however, disrupting their physical integrity as judged by electron microscopy. At subvirucidal concentrations, EB changes the adhesive properties of virions, causing aggregation at high virus concentrations. This peptide may be a useful tool for studying viral entry mechanisms. Entry of herpes simplex virus type 1 (HSV-1) into host cells occurs through fusion of the viral envelope with the plasma membrane and involves complex and poorly understood interactions between several viral and cellular proteins. One strategy for dissecting the function of this fusion machine is through the use of specific inhibitors. We identified a peptide with antiviral activity that blocks HSV-1 infection at the entry stage and during cell-to-cell spreading. This peptide (called EB for "entry blocker") consists of the FGF4 signal sequence with an RRKK tetramer at the amino terminus to improve solubility. The activity of EB depends exclusively but not canonically on the signal sequence. Inhibition of virus entry (hrR3) and plaque formation (KOS) strongly depend on virus concentrations and serum addition, with 50% inhibitory concentrations typically ranging from 1 to 10 mu M. Blocking preadsorbed virus requires higher EB concentrations. Cytotoxic effects (trypan blue exclusion) are first noted at 50 mu M EB in serum-free medium and at greater than or equal to 200 mu M in the presence of serum. EB does not affect gC-dependent mechanisms of virus attachment and does not block virus attachment at 4 degree C. Instead, EB directly interacts with virions and inactivates them irreversibly without, however, disrupting their physical integrity as judged by electron microscopy. At subvirucidal concentrations, EB changes the adhesive properties of virions, causing aggregation at high virus concentrations. This peptide may be a useful tool for studying viral entry mechanisms.
Author	Curtis R. Brandt James S. Busse Hermann Bultmann
AuthorAffiliation	Department of Ophthalmology and Visual Sciences 1 and Department of Medical Microbiology and Immunology, 3 Medical School, and Department of Biochemistry, College of Agriculture and Life Sciences, 2 University of Wisconsin—Madison, Madison, Wisconsin
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BackLink	https://www.ncbi.nlm.nih.gov/pubmed/11222686$$D View this record in MEDLINE/PubMed
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Cites_doi	10.1016/S0021-9258(19)50546-4 10.1099/0022-1317-72-5-1131 10.1126/science.285.5433.1569 10.1074/jbc.274.39.27875 10.1073/pnas.84.15.5454 10.1073/pnas.82.23.7969 10.1128/jvi.63.6.2874-2876.1989 10.1073/pnas.91.2.664 10.1128/jvi.65.3.1090-1098.1991 10.1038/3293 10.1128/jvi.49.1.236-247.1984 10.1006/smvy.1993.1012 10.1016/S0021-9258(17)34080-2 10.1128/jvi.68.2.1224-1228.1994 10.1006/viro.1995.1184 10.1128/jvi.68.9.5825-5834.1994 10.1099/0022-1317-67-6-1001 10.1126/science.280.5369.1618 10.1128/jvi.66.4.2240-2250.1992 10.1128/jvi.71.3.2285-2291.1997 10.1021/ja00897a025 10.2174/092986650306221101121141 10.1093/nar/26.21.4910 10.1128/jvi.70.9.6076-6082.1996 10.1128/JVI.72.5.4430-4433.1998 10.1074/jbc.272.25.16010 10.1126/science.1439803 10.1128/jvi.63.2.819-827.1989 10.1016/0006-2952(90)90138-B 10.1016/0042-6822(90)90396-9 10.1099/0022-1317-69-6-1147 10.1128/jvi.71.5.3872-3878.1997 10.1523/JNEUROSCI.15-11-07158.1995 10.1128/JVI.72.1.873-875.1998 10.1016/S0092-8674(00)81363-X 10.1074/jbc.270.24.14255 10.1083/jcb.116.5.1273 10.1128/JVI.72.2.986-993.1998 10.1128/jvi.63.1.52-58.1989 10.1111/j.1399-3011.1979.tb01847.x 10.1073/pnas.89.21.10537 10.1128/jvi.62.8.2596-2604.1988 10.1128/jvi.70.6.3815-3822.1996 10.1099/0022-1317-68-5-1429 10.1073/pnas.74.9.3913 10.1099/0022-1317-75-6-1211 10.1128/JVI.72.5.3595-3601.1998 10.1073/pnas.88.12.5087 10.1096/fsb2fasebj.12.1.67 10.1016/S0014-5793(97)01123-X 10.1128/jvi.61.11.3356-3364.1987 10.1016/0166-3542(93)90001-Y 10.1016/0042-6822(90)90229-K 10.1128/jvi.67.4.2285-2297.1993 10.1016/0168-1702(93)90057-T 10.1128/jvi.70.6.3461-3469.1996 10.1128/JVI.72.9.7064-7074.1998 10.1128/jvi.71.8.6083-6093.1997 10.1128/jvi.62.5.1486-1494.1988 10.1128/jvi.69.7.4471-4483.1995 10.1006/viro.1996.0459 10.1128/jvi.66.8.5002-5012.1992 10.1128/JVI.72.7.6119-6130.1998
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Notes	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 Corresponding author. Mailing address: Department of Ophthalmology and Visual Sciences, University of Wisconsin, 1300 University Ave., 6630 MSC, Madison, WI 53706-1532. Phone: (608) 262-8054. Fax: (608) 262-0479. E-mail: crbrandt@facstaff.wisc.edu.
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References	e_1_3_2_26_2 e_1_3_2_49_2 e_1_3_2_28_2 e_1_3_2_41_2 e_1_3_2_64_2 e_1_3_2_20_2 e_1_3_2_43_2 e_1_3_2_62_2 e_1_3_2_22_2 e_1_3_2_45_2 e_1_3_2_68_2 e_1_3_2_24_2 e_1_3_2_47_2 Fields C. G. (e_1_3_2_13_2) 1991; 4 e_1_3_2_60_2 e_1_3_2_9_2 e_1_3_2_16_2 e_1_3_2_37_2 Grau D. R. (e_1_3_2_18_2) 1989; 30 e_1_3_2_39_2 e_1_3_2_54_2 e_1_3_2_10_2 e_1_3_2_31_2 e_1_3_2_52_2 e_1_3_2_5_2 e_1_3_2_12_2 e_1_3_2_33_2 e_1_3_2_58_2 e_1_3_2_3_2 e_1_3_2_14_2 e_1_3_2_35_2 e_1_3_2_56_2 e_1_3_2_50_2 e_1_3_2_27_2 e_1_3_2_48_2 e_1_3_2_29_2 e_1_3_2_40_2 e_1_3_2_65_2 e_1_3_2_21_2 e_1_3_2_42_2 e_1_3_2_63_2 e_1_3_2_23_2 e_1_3_2_69_2 e_1_3_2_25_2 e_1_3_2_46_2 e_1_3_2_67_2 Whitley R. J. (e_1_3_2_66_2) 1982; 3 e_1_3_2_61_2 Chou P. Y. (e_1_3_2_7_2) 1978; 47 e_1_3_2_15_2 e_1_3_2_38_2 e_1_3_2_8_2 e_1_3_2_17_2 e_1_3_2_59_2 e_1_3_2_6_2 e_1_3_2_19_2 e_1_3_2_30_2 Oehlke J. (e_1_3_2_44_2) 1996; 3 e_1_3_2_53_2 e_1_3_2_32_2 e_1_3_2_51_2 e_1_3_2_11_2 e_1_3_2_34_2 e_1_3_2_57_2 e_1_3_2_4_2 e_1_3_2_36_2 e_1_3_2_55_2 e_1_3_2_2_2
References_xml	– ident: e_1_3_2_57_2 doi: 10.1016/S0021-9258(19)50546-4 – ident: e_1_3_2_34_2 doi: 10.1099/0022-1317-72-5-1131 – ident: e_1_3_2_50_2 doi: 10.1126/science.285.5433.1569 – ident: e_1_3_2_43_2 doi: 10.1074/jbc.274.39.27875 – ident: e_1_3_2_14_2 doi: 10.1073/pnas.84.15.5454 – ident: e_1_3_2_17_2 doi: 10.1073/pnas.82.23.7969 – ident: e_1_3_2_20_2 doi: 10.1128/jvi.63.6.2874-2876.1989 – ident: e_1_3_2_12_2 doi: 10.1073/pnas.91.2.664 – ident: e_1_3_2_22_2 doi: 10.1128/jvi.65.3.1090-1098.1991 – ident: e_1_3_2_28_2 doi: 10.1038/3293 – ident: e_1_3_2_9_2 doi: 10.1128/jvi.49.1.236-247.1984 – ident: e_1_3_2_55_2 doi: 10.1006/smvy.1993.1012 – ident: e_1_3_2_10_2 doi: 10.1016/S0021-9258(17)34080-2 – ident: e_1_3_2_54_2 doi: 10.1128/jvi.68.2.1224-1228.1994 – ident: e_1_3_2_3_2 doi: 10.1006/viro.1995.1184 – ident: e_1_3_2_19_2 doi: 10.1128/jvi.68.9.5825-5834.1994 – ident: e_1_3_2_39_2 doi: 10.1099/0022-1317-67-6-1001 – ident: e_1_3_2_16_2 doi: 10.1126/science.280.5369.1618 – ident: e_1_3_2_26_2 doi: 10.1128/jvi.66.4.2240-2250.1992 – ident: e_1_3_2_63_2 doi: 10.1128/jvi.71.3.2285-2291.1997 – ident: e_1_3_2_38_2 doi: 10.1021/ja00897a025 – volume: 3 start-page: 393 year: 1996 ident: e_1_3_2_44_2 article-title: Nonendocytic, amphipathicity dependent cellular uptake of helical model peptides publication-title: Protein Pept. Lett. doi: 10.2174/092986650306221101121141 contributor: fullname: Oehlke J. – ident: e_1_3_2_2_2 doi: 10.1093/nar/26.21.4910 – ident: e_1_3_2_21_2 doi: 10.1128/jvi.70.9.6076-6082.1996 – ident: e_1_3_2_52_2 – ident: e_1_3_2_8_2 doi: 10.1128/JVI.72.5.4430-4433.1998 – ident: e_1_3_2_62_2 doi: 10.1074/jbc.272.25.16010 – ident: e_1_3_2_65_2 doi: 10.1126/science.1439803 – ident: e_1_3_2_27_2 doi: 10.1128/jvi.63.2.819-827.1989 – ident: e_1_3_2_4_2 doi: 10.1016/0006-2952(90)90138-B – volume: 47 start-page: 45 year: 1978 ident: e_1_3_2_7_2 article-title: Prediction of the secondary structure of proteins from their amino acid sequence publication-title: Adv. Enzymol Relat. Areas Mol. Biol. contributor: fullname: Chou P. Y. – ident: e_1_3_2_6_2 doi: 10.1016/0042-6822(90)90396-9 – ident: e_1_3_2_11_2 doi: 10.1099/0022-1317-69-6-1147 – ident: e_1_3_2_49_2 doi: 10.1128/jvi.71.5.3872-3878.1997 – volume: 4 start-page: 95 year: 1991 ident: e_1_3_2_13_2 article-title: HBTU activation for automated Fmoc solid-phase peptide synthesis publication-title: Peptide Res. contributor: fullname: Fields C. G. – ident: e_1_3_2_59_2 doi: 10.1523/JNEUROSCI.15-11-07158.1995 – ident: e_1_3_2_60_2 doi: 10.1128/JVI.72.1.873-875.1998 – ident: e_1_3_2_40_2 doi: 10.1016/S0092-8674(00)81363-X – ident: e_1_3_2_33_2 doi: 10.1074/jbc.270.24.14255 – ident: e_1_3_2_53_2 doi: 10.1083/jcb.116.5.1273 – volume: 3 start-page: 1 year: 1982 ident: e_1_3_2_66_2 article-title: Epidemiology of herpes simplex viruses publication-title: The herpesviruses contributor: fullname: Whitley R. J. – ident: e_1_3_2_47_2 doi: 10.1128/JVI.72.2.986-993.1998 – ident: e_1_3_2_68_2 doi: 10.1128/jvi.63.1.52-58.1989 – ident: e_1_3_2_37_2 doi: 10.1111/j.1399-3011.1979.tb01847.x – ident: e_1_3_2_67_2 doi: 10.1073/pnas.89.21.10537 – ident: e_1_3_2_5_2 doi: 10.1128/jvi.62.8.2596-2604.1988 – ident: e_1_3_2_41_2 doi: 10.1128/jvi.70.6.3815-3822.1996 – ident: e_1_3_2_29_2 doi: 10.1099/0022-1317-68-5-1429 – ident: e_1_3_2_35_2 doi: 10.1073/pnas.74.9.3913 – volume: 30 start-page: 2474 year: 1989 ident: e_1_3_2_18_2 article-title: Herpes simplex virus stromal keratitis is not titer-dependent and does not correlate with neurovirulence publication-title: Investig. Ophthalmol. Visual Sci. contributor: fullname: Grau D. R. – ident: e_1_3_2_23_2 doi: 10.1099/0022-1317-75-6-1211 – ident: e_1_3_2_42_2 doi: 10.1128/JVI.72.5.3595-3601.1998 – ident: e_1_3_2_51_2 doi: 10.1073/pnas.88.12.5087 – ident: e_1_3_2_46_2 doi: 10.1096/fsb2fasebj.12.1.67 – ident: e_1_3_2_45_2 doi: 10.1016/S0014-5793(97)01123-X – ident: e_1_3_2_25_2 doi: 10.1128/jvi.61.11.3356-3364.1987 – ident: e_1_3_2_36_2 doi: 10.1016/0166-3542(93)90001-Y – ident: e_1_3_2_56_2 doi: 10.1016/0042-6822(90)90229-K – ident: e_1_3_2_48_2 doi: 10.1128/jvi.67.4.2285-2297.1993 – ident: e_1_3_2_61_2 doi: 10.1016/0168-1702(93)90057-T – ident: e_1_3_2_24_2 doi: 10.1128/jvi.70.6.3461-3469.1996 – ident: e_1_3_2_30_2 doi: 10.1128/JVI.72.9.7064-7074.1998 – ident: e_1_3_2_64_2 doi: 10.1128/jvi.71.8.6083-6093.1997 – ident: e_1_3_2_32_2 doi: 10.1128/jvi.62.5.1486-1494.1988 – ident: e_1_3_2_58_2 doi: 10.1128/jvi.69.7.4471-4483.1995 – ident: e_1_3_2_69_2 doi: 10.1006/viro.1996.0459 – ident: e_1_3_2_15_2 doi: 10.1128/jvi.66.8.5002-5012.1992 – ident: e_1_3_2_31_2 doi: 10.1128/JVI.72.7.6119-6130.1998
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Snippet	Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... Entry of herpes simplex virus type 1 (HSV-1) into host cells occurs through fusion of the viral envelope with the plasma membrane and involves complex and... ABSTRACT Entry of herpes simplex virus type 1 (HSV-1) into host cells occurs through fusion of the viral envelope with the plasma membrane and involves complex... Entry of herpes simplex virus type 1 (HSV-1) into host cells occurs through fusion of the viral envelope with the plasma membrane and involves complex and...
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StartPage	2634
SubjectTerms	Animals Chlorocebus aethiops Fibroblast Growth Factors Herpes Simplex - virology Herpes simplex virus 1 Herpesvirus 1, Human - drug effects Herpesvirus 1, Human - pathogenicity Herpesvirus 1, Human - physiology Peptides - chemical synthesis Peptides - chemistry Peptides - metabolism Peptides - pharmacology Protein Sorting Signals Vero Cells Viral Plaque Assay Virion - metabolism Virus-Cell Interactions
Title	Modified FGF4 Signal Peptide Inhibits Entry of Herpes Simplex Virus Type 1
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