Literature DB >> 3871510

Vaccinia virus encodes a polypeptide homologous to epidermal growth factor and transforming growth factor.

J P Brown, D R Twardzik, H Marquardt, G J Todaro.   

Abstract

Epidermal growth factor (EGF) and transforming growth factor type I (TGF) are polypeptides of 53 and 50 amino acid residues, respectively. Both bind to EGF receptor, a 1,200-residue transmembranous glycoprotein, leading to phosphorylation of the receptor, enhancement of its tyrosine-specific kinase activity and ultimately to stimulation of cell growth. We report here that a 140-residue polypeptide encoded by one of the early genes of vaccinia virus (VV) is related closely to EGF and TGF. The presence of putative signal and transmembranous sequences further suggests that the viral protein might be an integral membrane protein, but that, as in the case of EGF itself, the membrane-associated form may be the precursor of a soluble growth factor. Production of EGF-like growth factors by virally infected cells could account for the proliferative diseases associated with members of the poxvirus family such as Shope fibroma virus, Yaba tumour virus, and molluscum contagiosum virus (MCV).

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Year:  1985        PMID: 3871510     DOI: 10.1038/313491a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  58 in total

1.  The vaccinia virus-stimulated mitogen-activated protein kinase (MAPK) pathway is required for virus multiplication.

Authors:  Anderson A Andrade; Patrícia N G Silva; Anna C T C Pereira; Lirlândia P De Sousa; Paulo C P Ferreira; Ricardo T Gazzinelli; Erna G Kroon; Catherine Ropert; Cláudio A Bonjardim
Journal:  Biochem J       Date:  2004-07-15       Impact factor: 3.857

Review 2.  Polypeptide growth factors and the kidney: a developmental perspective.

Authors:  E D Avner
Journal:  Pediatr Nephrol       Date:  1990-07       Impact factor: 3.714

3.  Immunological and structural homology between human T-cell leukemia virus type I envelope glycoprotein and a region of human interleukin-2 implicated in binding the beta receptor.

Authors:  D S Kohtz; A Altman; J D Kohtz; S Puszkin
Journal:  J Virol       Date:  1988-02       Impact factor: 5.103

4.  Amino acids bracketing the predicted transmembrane domains of membrane proteins.

Authors:  C Pidgeon; R L Williard; S C Schroeder
Journal:  Pharm Res       Date:  1989-09       Impact factor: 4.200

5.  Structure-function analysis of human transforming growth factor-alpha by site-directed mutagenesis.

Authors:  J A Feild; R H Reid; D J Rieman; T P Kline; G Sathe; R G Greig; M A Anzano
Journal:  Biochem J       Date:  1992-04-01       Impact factor: 3.857

6.  Pathogenic poxviruses reveal viral strategies to exploit the ErbB signaling network.

Authors:  E Tzahar; J D Moyer; H Waterman; E G Barbacci; J Bao; G Levkowitz; M Shelly; S Strano; R Pinkas-Kramarski; J H Pierce; G C Andrews; Y Yarden
Journal:  EMBO J       Date:  1998-10-15       Impact factor: 11.598

7.  The genome of Shope fibroma virus, a tumorigenic poxvirus, contains a growth factor gene with sequence similarity to those encoding epidermal growth factor and transforming growth factor alpha.

Authors:  W Chang; C Upton; S L Hu; A F Purchio; G McFadden
Journal:  Mol Cell Biol       Date:  1987-01       Impact factor: 4.272

8.  Deletion of the vaccinia virus growth factor gene reduces virus virulence.

Authors:  R M Buller; S Chakrabarti; J A Cooper; D R Twardzik; B Moss
Journal:  J Virol       Date:  1988-03       Impact factor: 5.103

9.  Characterization of vaccinia virus growth factor biosynthetic pathway with an antipeptide antiserum.

Authors:  W Chang; J G Lim; I Hellström; L E Gentry
Journal:  J Virol       Date:  1988-03       Impact factor: 5.103

10.  Chicken epidermal growth factor (EGF) receptor: cDNA cloning, expression in mouse cells, and differential binding of EGF and transforming growth factor alpha.

Authors:  I Lax; A Johnson; R Howk; J Sap; F Bellot; M Winkler; A Ullrich; B Vennstrom; J Schlessinger; D Givol
Journal:  Mol Cell Biol       Date:  1988-05       Impact factor: 4.272

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