Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1995 Jul;69(7):4292–4298. doi: 10.1128/jvi.69.7.4292-4298.1995

Region E3 of subgroup B human adenoviruses encodes a 16-kilodalton membrane protein that may be a distant analog of the E3-6.7K protein of subgroup C adenoviruses.

L K Hawkins 1, J Wilson-Rawls 1, W S Wold 1
PMCID: PMC189168  PMID: 7769690

Abstract

There is an open reading frame in the E3 transcription unit of adenovirus type 3 (Ad3) and Ad7 that could encode a protein of 16 kDa (16K protein). Ad3 and Ad7 are members of subgroup B of human adenoviruses. Using a rabbit antipeptide antiserum, we show that the 16K protein is expressed in Ad3- and Ad7-infected cells at early and late stages of infection; it is not expressed in cells infected with an Ad7 mutant that deletes the 16K gene. The 16K protein was also transcribed and translated in vitro from DNA containing the open reading frame for the 16K protein. The 16K protein has two hydrophobic domains typical of integral membrane proteins; consistent with this, we detected 16K in the crude membrane but not the cytosol cellular fractions. Although 16K has two potential sites for Asn-linked glycosylation, the protein is not glycosylated. The 16K gene is located in the same position in region E3 as the gene for the 6.7K protein of subgroup C adenoviruses (Ad2 and Ad5). E3-6.7K is an Asn-linked integral membrane glycoprotein, localized in the endoplasmic reticulum, whose function is unknown. The 16K protein has a putative transmembrane domain located in the same place in 16K as is the transmembrane domain in 6.7K, and the C-terminal portion of 16K is partially homologous to the C-terminal cytoplasmic domain of 6.7K; we suggest that these domains in 16K and 6.7K may have a similar function. The N-terminal 102 residues in 16K are not found in 6.7K; these residues may have a function that is unique to the 16K protein. In common with all known E3 proteins, the 16K protein is dispensable for virus replication in cultured cells; this suggests that the 16K protein may function in virus-host interactions.

Full Text

The Full Text of this article is available as a PDF (353.8 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andersson M., McMichael A., Peterson P. A. Reduced allorecognition of adenovirus-2 infected cells. J Immunol. 1987 Jun 1;138(11):3960–3966. [PubMed] [Google Scholar]
  2. Andersson M., Päbo S., Nilsson T., Peterson P. A. Impaired intracellular transport of class I MHC antigens as a possible means for adenoviruses to evade immune surveillance. Cell. 1985 Nov;43(1):215–222. doi: 10.1016/0092-8674(85)90026-1. [DOI] [PubMed] [Google Scholar]
  3. Bailey A., Mautner V. Phylogenetic relationships among adenovirus serotypes. Virology. 1994 Dec;205(2):438–452. doi: 10.1006/viro.1994.1664. [DOI] [PubMed] [Google Scholar]
  4. Bause E. Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem J. 1983 Feb 1;209(2):331–336. doi: 10.1042/bj2090331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Beier D. C., Cox J. H., Vining D. R., Cresswell P., Engelhard V. H. Association of human class I MHC alleles with the adenovirus E3/19K protein. J Immunol. 1994 Apr 15;152(8):3862–3872. [PubMed] [Google Scholar]
  6. Burgert H. G., Kvist S. An adenovirus type 2 glycoprotein blocks cell surface expression of human histocompatibility class I antigens. Cell. 1985 Jul;41(3):987–997. doi: 10.1016/s0092-8674(85)80079-9. [DOI] [PubMed] [Google Scholar]
  7. Burgert H. G., Maryanski J. L., Kvist S. "E3/19K" protein of adenovirus type 2 inhibits lysis of cytolytic T lymphocytes by blocking cell-surface expression of histocompatibility class I antigens. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1356–1360. doi: 10.1073/pnas.84.5.1356. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Carlin C. R., Tollefson A. E., Brady H. A., Hoffman B. L., Wold W. S. Epidermal growth factor receptor is down-regulated by a 10,400 MW protein encoded by the E3 region of adenovirus. Cell. 1989 Apr 7;57(1):135–144. doi: 10.1016/0092-8674(89)90179-7. [DOI] [PubMed] [Google Scholar]
  9. Chow L. T., Lewis J. B., Broker T. R. RNA transcription and splicing at early and intermediate times after adenovirus-2 infection. Cold Spring Harb Symp Quant Biol. 1980;44(Pt 1):401–414. doi: 10.1101/sqb.1980.044.01.044. [DOI] [PubMed] [Google Scholar]
  10. Chroboczek J., Bieber F., Jacrot B. The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2. Virology. 1992 Jan;186(1):280–285. doi: 10.1016/0042-6822(92)90082-z. [DOI] [PubMed] [Google Scholar]
  11. Cladaras C., Bhat B., Wold W. S. Mapping the 5' ends, 3' ends, and splice sites of mRNAs from the early E3 transcription unit of adenovirus 5. Virology. 1985 Jan 15;140(1):44–54. doi: 10.1016/0042-6822(85)90444-1. [DOI] [PubMed] [Google Scholar]
  12. Cladaras C., Wold W. S. DNA sequence of the early E3 transcription unit of adenovirus 5. Virology. 1985 Jan 15;140(1):28–43. doi: 10.1016/0042-6822(85)90443-x. [DOI] [PubMed] [Google Scholar]
  13. Cousin C., Winter N., Gomes S. A., D'Halluin J. C. Cellular transformation by E1 genes of enteric adenoviruses. Virology. 1991 Mar;181(1):277–287. doi: 10.1016/0042-6822(91)90493-u. [DOI] [PubMed] [Google Scholar]
  14. Cox J. H., Buller R. M., Bennink J. R., Yewdell J. W., Karupiah G. Expression of adenovirus E3/19K protein does not alter mouse MHC class I-restricted responses to vaccinia virus. Virology. 1994 Nov 1;204(2):558–562. doi: 10.1006/viro.1994.1569. [DOI] [PubMed] [Google Scholar]
  15. Cox J. H., Yewdell J. W., Eisenlohr L. C., Johnson P. R., Bennink J. R. Antigen presentation requires transport of MHC class I molecules from the endoplasmic reticulum. Science. 1990 Feb 9;247(4943):715–718. doi: 10.1126/science.2137259. [DOI] [PubMed] [Google Scholar]
  16. Davison A. J., Telford E. A., Watson M. S., McBride K., Mautner V. The DNA sequence of adenovirus type 40. J Mol Biol. 1993 Dec 20;234(4):1308–1316. doi: 10.1006/jmbi.1993.1687. [DOI] [PubMed] [Google Scholar]
  17. Engelman D. M., Steitz T. A. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell. 1981 Feb;23(2):411–422. doi: 10.1016/0092-8674(81)90136-7. [DOI] [PubMed] [Google Scholar]
  18. Flomenberg P. R., Chen M., Horwitz M. S. Sequence and genetic organization of adenovirus type 35 early region 3. J Virol. 1988 Nov;62(11):4431–4437. doi: 10.1128/jvi.62.11.4431-4437.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Gavel Y., von Heijne G. Sequence differences between glycosylated and non-glycosylated Asn-X-Thr/Ser acceptor sites: implications for protein engineering. Protein Eng. 1990 Apr;3(5):433–442. doi: 10.1093/protein/3.5.433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Ginsberg H. S., Lundholm-Beauchamp U., Horswood R. L., Pernis B., Wold W. S., Chanock R. M., Prince G. A. Role of early region 3 (E3) in pathogenesis of adenovirus disease. Proc Natl Acad Sci U S A. 1989 May;86(10):3823–3827. doi: 10.1073/pnas.86.10.3823. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Ginsberg H. S., Prince G. A. The molecular basis of adenovirus pathogenesis. Infect Agents Dis. 1994 Feb;3(1):1–8. [PubMed] [Google Scholar]
  22. Gooding L. R., Elmore L. W., Tollefson A. E., Brady H. A., Wold W. S. A 14,700 MW protein from the E3 region of adenovirus inhibits cytolysis by tumor necrosis factor. Cell. 1988 May 6;53(3):341–346. doi: 10.1016/0092-8674(88)90154-7. [DOI] [PubMed] [Google Scholar]
  23. Gooding L. R., Ranheim T. S., Tollefson A. E., Aquino L., Duerksen-Hughes P., Horton T. M., Wold W. S. The 10,400- and 14,500-dalton proteins encoded by region E3 of adenovirus function together to protect many but not all mouse cell lines against lysis by tumor necrosis factor. J Virol. 1991 Aug;65(8):4114–4123. doi: 10.1128/jvi.65.8.4114-4123.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Gooding L. R., Sofola I. O., Tollefson A. E., Duerksen-Hughes P., Wold W. S. The adenovirus E3-14.7K protein is a general inhibitor of tumor necrosis factor-mediated cytolysis. J Immunol. 1990 Nov 1;145(9):3080–3086. [PubMed] [Google Scholar]
  25. Green M., Wold W. S. Human adenoviruses: growth, purification, and transfection assay. Methods Enzymol. 1979;58:425–435. doi: 10.1016/s0076-6879(79)58157-9. [DOI] [PubMed] [Google Scholar]
  26. Grunhaus A., Cho S., Horwitz M. S. Association of vaccinia virus-expressed adenovirus E3-19K glycoprotein with class I MHC and its effects on virulence in a murine pneumonia model. Virology. 1994 May 1;200(2):535–546. doi: 10.1006/viro.1994.1216. [DOI] [PubMed] [Google Scholar]
  27. Hartmann E., Rapoport T. A., Lodish H. F. Predicting the orientation of eukaryotic membrane-spanning proteins. Proc Natl Acad Sci U S A. 1989 Aug;86(15):5786–5790. doi: 10.1073/pnas.86.15.5786. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Hawkins L. K., Wold W. S. A 12,500 MW protein is coded by region E3 of adenovirus. Virology. 1992 Jun;188(2):486–494. doi: 10.1016/0042-6822(92)90502-g. [DOI] [PubMed] [Google Scholar]
  29. Hawkins L. K., Wold W. S. A 20,500-Dalton protein is coded by region E3 of subgroup B but not subgroup C human adenoviruses. Virology. 1995 Apr 1;208(1):226–233. doi: 10.1006/viro.1995.1146. [DOI] [PubMed] [Google Scholar]
  30. Hermiston T. W., Hellwig R., Hierholzer J. C., Wold W. S. Sequence and functional analysis of the human adenovirus type 7 E3-gp19K protein from 17 clinical isolates. Virology. 1993 Dec;197(2):593–600. doi: 10.1006/viro.1993.1633. [DOI] [PubMed] [Google Scholar]
  31. Hermiston T. W., Tripp R. A., Sparer T., Gooding L. R., Wold W. S. Deletion mutation analysis of the adenovirus type 2 E3-gp19K protein: identification of sequences within the endoplasmic reticulum lumenal domain that are required for class I antigen binding and protection from adenovirus-specific cytotoxic T lymphocytes. J Virol. 1993 Sep;67(9):5289–5298. doi: 10.1128/jvi.67.9.5289-5298.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Hoffman P., Carlin C. Adenovirus E3 protein causes constitutively internalized epidermal growth factor receptors to accumulate in a prelysosomal compartment, resulting in enhanced degradation. Mol Cell Biol. 1994 Jun;14(6):3695–3706. doi: 10.1128/mcb.14.6.3695. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Hoffman P., Rajakumar P., Hoffman B., Heuertz R., Wold W. S., Carlin C. R. Evidence for intracellular down-regulation of the epidermal growth factor (EGF) receptor during adenovirus infection by an EGF-independent mechanism. J Virol. 1992 Jan;66(1):197–203. doi: 10.1128/jvi.66.1.197-203.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Hoffman P., Yaffe M. B., Hoffman B. L., Yei S., Wold W. S., Carlin C. Characterization of the adenovirus E3 protein that down-regulates the epidermal growth factor receptor. Evidence for intermolecular disulfide bonding and plasma membrane localization. J Biol Chem. 1992 Jul 5;267(19):13480–13487. [PubMed] [Google Scholar]
  35. Hong J. S., Mullis K. G., Engler J. A. Characterization of the early region 3 and fiber genes of Ad7. Virology. 1988 Dec;167(2):545–553. [PubMed] [Google Scholar]
  36. Horton T. M., Ranheim T. S., Aquino L., Kusher D. I., Saha S. K., Ware C. F., Wold W. S., Gooding L. R. Adenovirus E3 14.7K protein functions in the absence of other adenovirus proteins to protect transfected cells from tumor necrosis factor cytolysis. J Virol. 1991 May;65(5):2629–2639. doi: 10.1128/jvi.65.5.2629-2639.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Horton T. M., Tollefson A. E., Wold W. S., Gooding L. R. A protein serologically and functionally related to the group C E3 14,700-kilodalton protein is found in multiple adenovirus serotypes. J Virol. 1990 Mar;64(3):1250–1255. doi: 10.1128/jvi.64.3.1250-1255.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Hérissé J., Courtois G., Galibert F. Nucleotide sequence of the EcoRI D fragment of adenovirus 2 genome. Nucleic Acids Res. 1980 May 24;8(10):2173–2192. doi: 10.1093/nar/8.10.2173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Inouye M., Halegoua S. Secretion and membrane localization of proteins in Escherichia coli. CRC Crit Rev Biochem. 1980;7(4):339–371. doi: 10.3109/10409238009105465. [DOI] [PubMed] [Google Scholar]
  40. Kozak M. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J Biol Chem. 1991 Oct 25;266(30):19867–19870. [PubMed] [Google Scholar]
  41. Krajcsi P., Tollefson A. E., Anderson C. W., Stewart A. R., Carlin C. R., Wold W. S. The E3-10.4K protein of adenovirus is an integral membrane protein that is partially cleaved between Ala22 and Ala23 and has a Ccyt orientation. Virology. 1992 Mar;187(1):131–144. doi: 10.1016/0042-6822(92)90302-6. [DOI] [PubMed] [Google Scholar]
  42. Krajcsi P., Tollefson A. E., Anderson C. W., Wold W. S. The adenovirus E3 14.5-kilodalton protein, which is required for down-regulation of the epidermal growth factor receptor and prevention of tumor necrosis factor cytolysis, is an integral membrane protein oriented with its C terminus in the cytoplasm. J Virol. 1992 Mar;66(3):1665–1673. doi: 10.1128/jvi.66.3.1665-1673.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Kuivinen E., Hoffman B. L., Hoffman P. A., Carlin C. R. Structurally related class I and class II receptor protein tyrosine kinases are down-regulated by the same E3 protein coded for by human group C adenoviruses. J Cell Biol. 1993 Mar;120(5):1271–1279. doi: 10.1083/jcb.120.5.1271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  45. Marchuk D., Drumm M., Saulino A., Collins F. S. Construction of T-vectors, a rapid and general system for direct cloning of unmodified PCR products. Nucleic Acids Res. 1991 Mar 11;19(5):1154–1154. doi: 10.1093/nar/19.5.1154. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. McDougall I., Mautner V. An adenovirus type 3 host range variant with mutations in the E1a and E3 early gene regions. J Gen Virol. 1987 May;68(Pt 5):1361–1371. doi: 10.1099/0022-1317-68-5-1361. [DOI] [PubMed] [Google Scholar]
  47. Mei Y. F., Wadell G. The nucleotide sequence of adenovirus type 11 early 3 region: comparison of genome type Ad11p and Ad11a. Virology. 1992 Nov;191(1):125–133. doi: 10.1016/0042-6822(92)90173-m. [DOI] [PubMed] [Google Scholar]
  48. Nilsson I. M., von Heijne G. Determination of the distance between the oligosaccharyltransferase active site and the endoplasmic reticulum membrane. J Biol Chem. 1993 Mar 15;268(8):5798–5801. [PubMed] [Google Scholar]
  49. Nilsson I., Whitley P., von Heijne G. The COOH-terminal ends of internal signal and signal-anchor sequences are positioned differently in the ER translocase. J Cell Biol. 1994 Sep;126(5):1127–1132. doi: 10.1083/jcb.126.5.1127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Perlman D., Halvorson H. O. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J Mol Biol. 1983 Jun 25;167(2):391–409. doi: 10.1016/s0022-2836(83)80341-6. [DOI] [PubMed] [Google Scholar]
  51. Päbo S., Nilsson T., Peterson P. A. Adenoviruses of subgenera B, C, D, and E modulate cell-surface expression of major histocompatibility complex class I antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(24):9665–9669. doi: 10.1073/pnas.83.24.9665. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Ranheim T. S., Shisler J., Horton T. M., Wold L. J., Gooding L. R., Wold W. S. Characterization of mutants within the gene for the adenovirus E3 14.7-kilodalton protein which prevents cytolysis by tumor necrosis factor. J Virol. 1993 Apr;67(4):2159–2167. doi: 10.1128/jvi.67.4.2159-2167.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Rawle F. C., Tollefson A. E., Wold W. S., Gooding L. R. Mouse anti-adenovirus cytotoxic T lymphocytes. Inhibition of lysis by E3 gp19K but not E3 14.7K. J Immunol. 1989 Sep 15;143(6):2031–2037. [PubMed] [Google Scholar]
  54. Roitsch T., Lehle L. Structural requirements for protein N-glycosylation. Influence of acceptor peptides on cotranslational glycosylation of yeast invertase and site-directed mutagenesis around a sequon sequence. Eur J Biochem. 1989 May 1;181(2):525–529. doi: 10.1111/j.1432-1033.1989.tb14755.x. [DOI] [PubMed] [Google Scholar]
  55. Scaria A., Tollefson A. E., Saha S. K., Wold W. S. The E3-11.6K protein of adenovirus is an Asn-glycosylated integral membrane protein that localizes to the nuclear membrane. Virology. 1992 Dec;191(2):743–753. doi: 10.1016/0042-6822(92)90250-s. [DOI] [PubMed] [Google Scholar]
  56. Schrier P. I., Bernards R., Vaessen R. T., Houweling A., van der Eb A. J. Expression of class I major histocompatibility antigens switched off by highly oncogenic adenovirus 12 in transformed rat cells. 1983 Oct 27-Nov 2Nature. 305(5937):771–775. doi: 10.1038/305771a0. [DOI] [PubMed] [Google Scholar]
  57. Shaw A. S., Rottier P. J., Rose J. K. Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7592–7596. doi: 10.1073/pnas.85.20.7592. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Signäs C., Akusjärvi G., Pettersson U. Region E3 of human adenoviruses; differences between the oncogenic adenovirus-3 and the non-oncogenic adenovirus-2. Gene. 1986;50(1-3):173–184. doi: 10.1016/0378-1119(86)90322-7. [DOI] [PubMed] [Google Scholar]
  59. Singer S. J. The structure and insertion of integral proteins in membranes. Annu Rev Cell Biol. 1990;6:247–296. doi: 10.1146/annurev.cb.06.110190.001335. [DOI] [PubMed] [Google Scholar]
  60. Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W. Nucleotide sequence of human adenovirus type 12 DNA: comparative functional analysis. J Virol. 1994 Jan;68(1):379–389. doi: 10.1128/jvi.68.1.379-389.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Stewart A. R., Tollefson A. E., Krajcsi P., Yei S. P., Wold W. S. The adenovirus E3 10.4K and 14.5K proteins, which function to prevent cytolysis by tumor necrosis factor and to down-regulate the epidermal growth factor receptor, are localized in the plasma membrane. J Virol. 1995 Jan;69(1):172–181. doi: 10.1128/jvi.69.1.172-181.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Struck D. K., Lennarz W. J. Evidence for the participation of saccharide-lipids in the synthesis of the oligosaccharide chain of ovalbumin. J Biol Chem. 1977 Feb 10;252(3):1007–1013. [PubMed] [Google Scholar]
  63. Tollefson A. E., Krajcsi P., Yei S. P., Carlin C. R., Wold W. S. A 10,400-molecular-weight membrane protein is coded by region E3 of adenovirus. J Virol. 1990 Feb;64(2):794–801. doi: 10.1128/jvi.64.2.794-801.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Tollefson A. E., Scaria A., Saha S. K., Wold W. S. The 11,600-MW protein encoded by region E3 of adenovirus is expressed early but is greatly amplified at late stages of infection. J Virol. 1992 Jun;66(6):3633–3642. doi: 10.1128/jvi.66.6.3633-3642.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Tollefson A. E., Stewart A. R., Yei S. P., Saha S. K., Wold W. S. The 10,400- and 14,500-dalton proteins encoded by region E3 of adenovirus form a complex and function together to down-regulate the epidermal growth factor receptor. J Virol. 1991 Jun;65(6):3095–3105. doi: 10.1128/jvi.65.6.3095-3105.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Tollefson A. E., Wold W. S. Identification and gene mapping of a 14,700-molecular-weight protein encoded by region E3 of group C adenoviruses. J Virol. 1988 Jan;62(1):33–39. doi: 10.1128/jvi.62.1.33-39.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Tufariello J. M., Cho S., Horwitz M. S. Adenovirus E3 14.7-kilodalton protein, an antagonist of tumor necrosis factor cytolysis, increases the virulence of vaccinia virus in severe combined immunodeficient mice. Proc Natl Acad Sci U S A. 1994 Nov 8;91(23):10987–10991. doi: 10.1073/pnas.91.23.10987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  68. Tufariello J., Cho S., Horwitz M. S. The adenovirus E3 14.7-kilodalton protein which inhibits cytolysis by tumor necrosis factor increases the virulence of vaccinia virus in a murine pneumonia model. J Virol. 1994 Jan;68(1):453–462. doi: 10.1128/jvi.68.1.453-462.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Wilson-Rawls J., Deutscher S. L., Wold W. S. The signal-anchor domain of adenovirus E3-6.7K, a type III integral membrane protein, can direct adenovirus E3-gp19K, a type I integral membrane protein, into the membrane of the endoplasmic reticulum. Virology. 1994 May 15;201(1):66–76. doi: 10.1006/viro.1994.1266. [DOI] [PubMed] [Google Scholar]
  70. Wilson-Rawls J., Saha S. K., Krajcsi P., Tollefson A. E., Gooding L. R., Wold W. S. A 6700 MW membrane protein is encoded by region E3 of adenovirus type 2. Virology. 1990 Sep;178(1):204–212. doi: 10.1016/0042-6822(90)90395-8. [DOI] [PubMed] [Google Scholar]
  71. Wilson-Rawls J., Wold W. S. The E3-6.7K protein of adenovirus is an Asn-linked integral membrane glycoprotein localized in the endoplasmic reticulum. Virology. 1993 Jul;195(1):6–15. doi: 10.1006/viro.1993.1341. [DOI] [PubMed] [Google Scholar]
  72. Wold W. S. Adenovirus genes that modulate the sensitivity of virus-infected cells to lysis by TNF. J Cell Biochem. 1993 Dec;53(4):329–335. doi: 10.1002/jcb.240530410. [DOI] [PubMed] [Google Scholar]
  73. Wold W. S., Cladaras C., Magie S. C., Yacoub N. Mapping a new gene that encodes an 11,600-molecular-weight protein in the E3 transcription unit of adenovirus 2. J Virol. 1984 Nov;52(2):307–313. doi: 10.1128/jvi.52.2.307-313.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Wold W. S., Gooding L. R. Region E3 of adenovirus: a cassette of genes involved in host immunosurveillance and virus-cell interactions. Virology. 1991 Sep;184(1):1–8. doi: 10.1016/0042-6822(91)90815-s. [DOI] [PubMed] [Google Scholar]
  75. Wold W. S., Hermiston T. W., Tollefson A. E. Adenovirus proteins that subvert host defenses. Trends Microbiol. 1994 Nov;2(11):437–443. doi: 10.1016/0966-842x(94)90801-x. [DOI] [PubMed] [Google Scholar]
  76. Wold W. S., Tollefson A. E., Hermiston T. W. E3 transcription unit of adenovirus. Curr Top Microbiol Immunol. 1995;199(Pt 1):237–274. doi: 10.1007/978-3-642-79496-4_13. [DOI] [PubMed] [Google Scholar]
  77. Zhang X., Bellett A. J., Hla R. T., Voss T., Müllbacher A., Braithwaite A. W. Down-regulation of human adenovirus E1a by E3 gene products: evidence for translational control of E1a by E3 14.5K and/or E3 10.4K products. J Gen Virol. 1994 Aug;75(Pt 8):1943–1951. doi: 10.1099/0022-1317-75-8-1943. [DOI] [PubMed] [Google Scholar]
  78. Zilli D., Voelkel-Johnson C., Skinner T., Laster S. M. The adenovirus E3 region 14.7 kDa protein, heat and sodium arsenite inhibit the TNF-induced release of arachidonic acid. Biochem Biophys Res Commun. 1992 Oct 15;188(1):177–183. doi: 10.1016/0006-291x(92)92366-6. [DOI] [PubMed] [Google Scholar]
  79. von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986 Jun 11;14(11):4683–4690. doi: 10.1093/nar/14.11.4683. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES