The E5 proteins

被引:198
作者
DiMaio, Daniel [1 ,2 ,3 ]
Petti, Lisa M. [1 ]
机构
[1] Yale Univ, Sch Med, Dept Genet, POB 208005, New Haven, CT 06520 USA
[2] Yale Univ, Sch Med, Dept Therapeut Radiol, New Haven, CT 06520 USA
[3] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
关键词
Papillomaviruses; Cervical cancer; Transmembrane proteins; PDGF receptor; Vacuolar ATPase; EGF receptor; HPV; HUMAN-PAPILLOMAVIRUS TYPE-16; GROWTH-FACTOR RECEPTOR; FACTOR-BETA RECEPTOR; MHC CLASS-I; VACUOLAR H+-ATPASE; OPEN READING FRAME; HUMAN FORESKIN KERATINOCYTES; MORTAL HUMAN FIBROBLASTS; FASL-MEDIATED APOPTOSIS; CELL-CYCLE PROGRESSION;
D O I
10.1016/j.virol.2013.05.006
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The E5 proteins are short transmembrane proteins encoded by many animal and human papillomaviruses. These proteins display transforming activity in cultured cells and animals, and they presumably also play a role in the productive virus life cycle. The E5 proteins are thought to act by modulating the activity of cellular proteins. Here, we describe the biological activities of the best-studied E5 proteins and discuss the evidence implicating specific protein targets and pathways in mediating these activities. The primary target of the 44-amino acid BPV1 E5 protein is the PDGF beta receptor, whereas the EGF receptor appears to be an important target of the 83-amino acid HPV16 E5 protein. Both E5 proteins also bind to the vacuolar ATPase and affect MHC class I expression and cell-cell communication. Continued studies of the E5 proteins will elucidate important aspects of transmembrane protein- protein interactions, cellular signal transduction, cell biology, virus replication, and tumorigenesis. (C) 2013 Elsevier Inc. All rights reserved.
引用
收藏
页码:99 / 114
页数:16
相关论文
共 180 条
[1]   A mutagenic analysis of the E5 protein of human papillomavirus type 16 reveals that E5 binding to the vacuolar H+-ATPase is not sufficient for biological activity, using mammalian and yeast expression systems [J].
Adam, JL ;
Briggs, MW ;
McCance, DJ .
VIROLOGY, 2000, 272 (02) :315-325
[2]   The transmembrane domain of the E5 oncoprotein contains functionally discrete helical faces [J].
Adduci, AJ ;
Schlegel, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (15) :10249-10258
[3]   Viral proteins of bovine papillomavirus type 4 during the development of alimentary canal tumours [J].
Anderson, RA ;
Scobie, L ;
ONeil, BW ;
Grindlay, GJ ;
Campo, MS .
VETERINARY JOURNAL, 1997, 154 (01) :69-78
[4]   VACUOLAR H+-ATPASE MUTANTS TRANSFORM CELLS AND DEFINE A BINDING-SITE FOR THE PAPILLOMAVIRUS E5 ONCOPROTEIN [J].
ANDRESSON, T ;
SPARKOWSKI, J ;
GOLDSTEIN, DJ ;
SCHLEGEL, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (12) :6830-6837
[5]   E5 transforming proteins of papillomaviruses do not disturb the activity of the vacuolar H+-ATPase [J].
Ashby, ADM ;
Meagher, L ;
Campo, MS ;
Finbow, ME .
JOURNAL OF GENERAL VIROLOGY, 2001, 82 :2353-2362
[6]   Down-regulation of MHC class I is a property common to papillomavirus E5 proteins [J].
Ashrafi, G. H. ;
Brown, D. R. ;
Fife, K. H. ;
Campo, M. S. .
VIRUS RESEARCH, 2006, 120 (1-2) :208-211
[7]   E5 protein of human papillomavirus 16 downregulates HLA class I and interacts with the heavy chain via its first hydrophobic domain [J].
Ashrafi, G. Hossein ;
Haghshenas, Mohammad ;
Marchetti, Barbara ;
Campo, M. Saveria .
INTERNATIONAL JOURNAL OF CANCER, 2006, 119 (09) :2105-2112
[8]   E5 protein of human papillomavirus type 16 selectively downregulates surface HLA class I [J].
Ashrafi, GH ;
Haghshenas, MR ;
Marchetti, B ;
O'Brien, PM ;
Campo, MS .
INTERNATIONAL JOURNAL OF CANCER, 2005, 113 (02) :276-283
[9]   Binding of bovine papillomavirus type 4 E8 to ductin (16K proteolipid), down-regulation of gap junction intercellular communication and full cell transformation are independent events [J].
Ashrafi, GH ;
Pitts, JD ;
Faccini, A ;
McLean, P ;
O'Brien, V ;
Finbow, ME ;
Campo, MS .
JOURNAL OF GENERAL VIROLOGY, 2000, 81 :689-694
[10]  
Ashrafi GH, 2002, ONCOGENE, V21, P248