The Genome of Cowpox Virus Contains a Gene Related to Those Encoding the Epidermal Growth Factor, Transforming Growth Factor Alpha and Vaccinia Growth Factor

Overview

Journal Virus Genes

Specialties Microbiology
Molecular Biology

Date 1999 Jul 14

PMID 10403701

Citations 8

Authors

F G Da Fonseca

R L Silva

J T Marques

P C Ferreira

E G Kroon

Affiliations

Soon will be listed here.

Abstract

Cowpox virus (CPV) is a member of the Orthopoxvirus genus and has the genetic capacity to encode a multitude of genes that interfere with the host inflammatory and immune response or modulate the physiological state of infected and non-infected cells. Among these CPV factors are receptors homologous to interferon and tumor necrosis factor receptors and also a viral cellular serine-proteinase analog. Here we describe the detection of a CPV gene that encodes a protein homologous to epidermal growth factor, transforming growth factor alpha and poxvirus growth factors, such as the vaccinia growth factor (VGF). The VGF and other poxvirus growth factors are produced early in the infection and are secreted into the medium where they bind to the EGF receptors, generating mytotic responses. The cowpox growth factor (CGF) gene was detected in three copies on the virus genome by PCR, and by northern and southern blot hybridization using VGF nucleotide sequences as primers and probes. The CPV gene has a strong nucleotide and predicted amino acid similarity with VGF, and is also produced early in the infection.

Citing Articles

Role of EGF Receptor Regulatory Networks in the Host Response to Viral Infections.

Carlin C Front Cell Infect Microbiol. 2022; 11:820355.

PMID: 35083168 PMC: 8785968. DOI: 10.3389/fcimb.2021.820355.

ErbB1-4-dependent EGF/neuregulin signals and their cross talk in the central nervous system: pathological implications in schizophrenia and Parkinson's disease.

Iwakura Y, Nawa H Front Cell Neurosci. 2013; 7:4.

PMID: 23408472 PMC: 3570895. DOI: 10.3389/fncel.2013.00004.

The tanapoxvirus 15L protein is a virus-encoded neuregulin that promotes viral replication in human endothelial cells.

Jeng D, Ma Z, Barrett J, McFadden G, Loeb J, Essani K J Virol. 2012; 87(6):3018-26.

PMID: 23269801 PMC: 3592142. DOI: 10.1128/JVI.02112-12.

Chasing Jenner's vaccine: revisiting cowpox virus classification.

Carroll D, Emerson G, Li Y, Sammons S, Olson V, Frace M PLoS One. 2011; 6(8):e23086.

PMID: 21858000 PMC: 3152555. DOI: 10.1371/journal.pone.0023086.

Modulation of the host immune response by cowpox virus.

Alzhanova D, Fruh K Microbes Infect. 2010; 12(12-13):900-9.

PMID: 20673807 PMC: 3500136. DOI: 10.1016/j.micinf.2010.07.007.

References

Rajcani J, Vojvodova A . The role of herpes simplex virus glycoproteins in the virus replication cycle. Acta Virol. 1998; 42(2):103-18. View

Dick J, Rosenthal K . A block in glycoprotein processing correlates with small plaque morphology and virion targetting to cell-cell junctions for an oral and an anal strain of herpes simplex virus type-1. Arch Virol. 1995; 140(12):2163-81. DOI: 10.1007/BF01323238. View

Baines J, Ward P, Roizman B . The UL20 gene of herpes simplex virus 1 encodes a function necessary for viral egress. J Virol. 1991; 65(12):6414-24. PMC: 250678. DOI: 10.1128/JVI.65.12.6414-6424.1991. View

Ligas M, Johnson D . A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells. J Virol. 1988; 62(5):1486-94. PMC: 253172. DOI: 10.1128/JVI.62.5.1486-1494.1988. View

Johnson D, Spear P . Monensin inhibits the processing of herpes simplex virus glycoproteins, their transport to the cell surface, and the egress of virions from infected cells. J Virol. 1982; 43(3):1102-12. PMC: 256222. DOI: 10.1128/JVI.43.3.1102-1112.1982. View

Spear P . The single base pair substitution responsible for the Syn phenotype of herpes simplex virus type 1, strain MP. Virology. 1987; 157(1):67-74. DOI: 10.1016/0042-6822(87)90314-x. View

Hutchinson L, Johnson D . Herpes simplex virus glycoprotein K is known to influence fusion of infected cells, yet is not on the cell surface. J Virol. 1995; 69(7):4556-63. PMC: 189205. DOI: 10.1128/JVI.69.7.4556-4563.1995. View

Tognon M, Guandalini R, Romanelli M, Manservigi R, Trevisani B . Phenotypic and genotypic characterization of locus Syn 5 in herpes simplex virus 1. Virus Res. 1991; 18(2-3):135-50. DOI: 10.1016/0168-1702(91)90014-m. View

Rajcani J, Sabo A, Mucha V, Kostal M, Compel P . Herpes simplex virus type 1 envelope subunit vaccine not only protects against lethal virus challenge, but also may restrict latency and virus reactivation. Acta Virol. 1995; 39(1):37-49. View

10.

Randazzo B, Kucharczuk J, Litzky L, Kaiser L, Brown S, MacLean A . Herpes simplex 1716--an ICP 34.5 mutant--is severely replication restricted in human skin xenografts in vivo. Virology. 1996; 223(2):392-5. DOI: 10.1006/viro.1996.0493. View

11.

Ruyechan W, Morse L, Knipe D, Roizman B . Molecular genetics of herpes simplex virus. II. Mapping of the major viral glycoproteins and of the genetic loci specifying the social behavior of infected cells. J Virol. 1979; 29(2):677-97. PMC: 353200. DOI: 10.1128/JVI.29.2.677-697.1979. View

12.

Baghian A, Kousoulas K . Role of the Na+,K+ pump in herpes simplex type 1-induced cell fusion: melittin causes specific reversion of syncytial mutants with the syn1 mutation to Syn+ (wild-type) phenotype. Virology. 1993; 196(2):548-56. DOI: 10.1006/viro.1993.1510. View

13.

Deluca N, Bzik D, Bond V, Person S, SNIPES W . Nucleotide sequences of herpes simplex virus type 1 (HSV-1) affecting virus entry, cell fusion, and production of glycoprotein gb (VP7). Virology. 1982; 122(2):411-23. DOI: 10.1016/0042-6822(82)90240-9. View

14.

Lingen M, Seck T, Weise K, Falke D . Single amino acid substitutions in the glycoprotein B carboxy terminus influence the fusion from without property of herpes simplex virus type 1. J Gen Virol. 1995; 76 ( Pt 7):1843-9. DOI: 10.1099/0022-1317-76-7-1843. View

15.

Ghiasi H, Cai S, Slanina S, Nesburn A, Wechsler S . Nonneutralizing antibody against the glycoprotein K of herpes simplex virus type-1 exacerbates herpes simplex virus type-1-induced corneal scarring in various virus-mouse strain combinations. Invest Ophthalmol Vis Sci. 1997; 38(6):1213-21. View

16.

Stannard L, Himmelhoch S, Wynchank S . Intra-nuclear localization of two envelope proteins, gB and gD, of herpes simplex virus. Arch Virol. 1996; 141(3-4):505-24. DOI: 10.1007/BF01718314. View

17.

Walev I, Weise K, Falke D . Differentiation of herpes simplex virus-induced fusion from without and fusion from within by cyclosporin A and compound 48/80. J Gen Virol. 1991; 72 ( Pt 6):1377-82. DOI: 10.1099/0022-1317-72-6-1377. View

18.

McGeoch D, Dalrymple M, Davison A, Dolan A, Frame M, McNab D . The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1. J Gen Virol. 1988; 69 ( Pt 7):1531-74. DOI: 10.1099/0022-1317-69-7-1531. View

19.

Ramaswamy R, Holland T . In vitro characterization of the HSV-1 UL53 gene product. Virology. 1992; 186(2):579-87. DOI: 10.1016/0042-6822(92)90024-j. View

20.

Klupp B, Baumeister J, Dietz P, Granzow H, Mettenleiter T . Pseudorabies virus glycoprotein gK is a virion structural component involved in virus release but is not required for entry. J Virol. 1998; 72(3):1949-58. PMC: 109487. DOI: 10.1128/JVI.72.3.1949-1958.1998. View