EurekaMag.com logo
+ Site Statistics
References:
52,725,316
Abstracts:
28,411,598
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Regulation of herpesvirus macro molecular synthesis part 5 properties of alpha poly peptides made in herpes simplex virus type 1 and herpes simplex virus type 2 infected cells


Virology 77(2): 733-749
Regulation of herpesvirus macro molecular synthesis part 5 properties of alpha poly peptides made in herpes simplex virus type 1 and herpes simplex virus type 2 infected cells
Previous reports defined as .alpha. those viral polypeptides whose production in infected [human laryngeal carcinoma HEp-2] cells does not require prior protein synthesis. Two subsequent groups, .beta. and .gamma., depend on prior .alpha. and .beta. polypeptide synthesis, respectively. Comparison of the synthesis and properties of .alpha. polypeptides specified by herpes simplex viruses (HSV) 1 and 2 showed that the 3 earliest virus-specific infected cell polypeptides (ICP) made in HSV-2 infected cells migrated slightly more slowly in polyacrylamide gels than the HSV-1 .alpha. polypeptides, ICP 4.0 and 27. Cells treated with canavanine from the time of infection with HSV-2 produced all .alpha., a subset of .beta. and a small amount of 1 .gamma. polypeptide; the synthesis of these polypeptides continued for many hours, at rates related to the multiplicity of infection. The transition from .alpha. to this subset of .beta. polypeptide synthesis did not appear to be affected by the arginine analog, but transition to the other sets of .beta. and to .gamma. polypeptide synthesis was blocked. A similar discrimination between different subsets of .beta. proteins was seen in treated HSV-1 infected cells. All .alpha. and a number of .beta. polypeptides observed underwent translocation into the nucleus, post translational modification resulting in a reduced electrophoretic mobility and phosphorylation. The modification of HSV-1 and HSV-2 ICP 4 was in at least 2 steps from the translational product ICP 4a, labeled during a pulse, to slower-migrating forms ICP 4b and 4c. All 3 forms were phosphorylated, but only 4b and 4c were found in the nucleus. In untreated infected cells ICP 4 ultimately accumulated in form ICP 4c. ICP 4a made in the presence of canavanine was not processed efficiently into ICP 4c. In another instance the polypeptide made in the presence of canavanine was not translocated into nuclei.


Accession: 006288444



Related references

Anatomy of herpes simplex virus dna part 10 mapping of viral genes by analysis of poly peptides and functions specified by herpes simplex virus type 1 x herpes simplex virus type 2 recombinants. Journal of Virology 26(2): 389-410, 1978

Physical mapping of herpes simplex virus coded functions and poly peptides by marker rescue and analysis of herpes simplex virus type 1 herpes simplex virus type 2 inter typic recombinants. De-The, G , W Henle And F Rapp (Ed ) Iarc (International Agency For Research on Cancer) Science Publications, No 24 Oncogenesis And Herpesviruses, Iii Part 1: Dna Of Herpesviruses, Viral Antigens, Cell-Virus Interaction; Proceedings Of The 3rd International Symposium, Cambridge, Mass , Usa, July 25-29, 1977 Lv+580p International Agency For Research on Cancer: Lyon, France Illus P11-32, 1978, 1979

Vaccinia virus recombinant that expresses the herpes simplex virus type 1 glycoprotein d gene protects mice against lethal challenge by herpes simplex virus type 1 or herpes simplex type 2 and the establishment of a latent ganglionic infection by herpes simplex virus type 1. Lerner, R A , R M Chanock And F Brown (Ed ) Vaccines 85: Molecular And Chemical Basis Of Resistance to Parasitic, Bacterial, And Viral Diseases; Meeting, 1983 Xxi+407p Cold Spring Harbor Laboratory: Cold Spring Harbor, N Y , Usa Illus Paper 169-174, 1985

Rna synthesis in cells infected with herpes simplex virus part 7 control of transcription and of transcript abundancies of unique and common sequences of herpes simplex virus 1 and herpes simplex virus 2. Journal of Virology 11(6): 886-892, 1973

Mapping of a herpes simplex virus type 2 encoded function that affects the susceptibility of herpes simplex virus infected target cells to lysis by herpes simplex virus specific cyto toxic t lymphocytes. Journal of Virology 49(3): 766-771, 1984

Mapping of a herpes simplex virus type 2-encoded function that affects the susceptibility of herpes simplex virus-infected target cells to lysis by herpes simplex virus-specific cytotoxic T lymphocytes. Journal of Virology 49(3): 766-771, 1984

Regulation of tmp and other nucleotides of thymidine kinase ec 27175 activity in extracts from primary rabbit kidney cells infected by herpes simplex virus type 1 and herpes simplex virus type 2. 1975

Control of protein synthesis in herpesvirus infected cells analysis of the poly peptides induced by wild type and 16 temperature sensitive mutants of herpes simplex virus strain 17. Journal of General Virology 31(3): 347-372, 1976

Anatomy of herpes simplex virus dna part 9 apparent exclusion of some parental dna arrangements in the generation of inter typic herpes simplex virus type 1 x herpes simplex virus type 2 recombinants. Journal of Virology 24(1): 231-248, 1977

Proteins specified by herpes simplex virus part 11 identification and relative molar rates of synthesis of structural and nonstructural herpes virus poly peptides in the infected cells. Journal of Virology 12(6): 1347-1365, 1973