Immunocytochemical study of the partition and distribution of Sindbis virus glycoproteins in freeze-fractured membranes of infected baby hamster kidney cells - PubMed (original) (raw)
Immunocytochemical study of the partition and distribution of Sindbis virus glycoproteins in freeze-fractured membranes of infected baby hamster kidney cells
M R Torrisi et al. J Cell Biol. 1985 Oct.
Abstract
Sindbis virus-infected baby hamster kidney cells were analyzed by thin section fracture-label. Specific immunolabel with antiviral glycoprotein antibodies or with conventional lectin label (wheat germ agglutinin) were used in conjunction with colloidal gold-conjugated protein A or ovomucoid, respectively. In addition, intact infected cells were analyzed with both labeling procedures. Experiments with Sindbis infected-chick embryo fibroblast cells were carried out as controls. Viral transmembrane glycoproteins appeared present in freeze-fractured inner and outer nuclear membrane, endoplasmic reticulum, Golgi stacks and vesicles, and plasma membranes; a clear preferential partition with the exoplasmic faces of all intracellular membranes was observed. By contrast, at the plasma membrane level, Sindbis glycoproteins were found to partition preferentially with the protoplasmic face. It seems likely that this protoplasmic partition is related to the binding with the nucleocapsid that takes place during the budding of the virus. At the cell surface, viral glycoproteins always appeared clustered and were predominantly associated with budding figures: moreover, large portions of the plasma membrane were devoid of both glycoproteins and budding viruses.
Similar articles
- Free diffusion to and from the inner nuclear membrane of newly synthesized plasma membrane glycoproteins.
Torrisi MR, Lotti LV, Pavan A, Migliaccio G, Bonatti S. Torrisi MR, et al. J Cell Biol. 1987 Mar;104(3):733-7. doi: 10.1083/jcb.104.3.733. J Cell Biol. 1987. PMID: 3818797 Free PMC article. - Anchorage-dependent surface distribution and partition during freeze-fracture of viral transmembrane glycoproteins.
Torrisi MR, Pavan A, Lotti LV, Migliaccio G, Pascale MC, Covelli E, Leone A, Bonatti S. Torrisi MR, et al. J Histochem Cytochem. 1990 Oct;38(10):1421-6. doi: 10.1177/38.10.2401782. J Histochem Cytochem. 1990. PMID: 2401782 - Regional distribution of Sindbis virus glycoproteins on the plasma membrane of infected baby hamster kidney cells.
Pavan A, Lotti LV, Torrisi MR, Migliaccio G, Bonatti S. Pavan A, et al. Exp Cell Res. 1987 Jan;168(1):53-62. doi: 10.1016/0014-4827(87)90415-0. Exp Cell Res. 1987. PMID: 3780874 - Synthesis and assembly of transmembrane viral and cellular glycoproteins.
Lodish HF, Zilberstein A, Porter M. Lodish HF, et al. Methods Cell Biol. 1981;23:5-25. doi: 10.1016/s0091-679x(08)61488-0. Methods Cell Biol. 1981. PMID: 6276668 Review. No abstract available. - Glycoproteins as components of cellular membranes.
Hughes RC. Hughes RC. Prog Biophys Mol Biol. 1973;26:189-268. doi: 10.1016/0079-6107(73)90020-5. Prog Biophys Mol Biol. 1973. PMID: 4122628 Review. No abstract available.
Cited by
- A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells.
Roux KJ, Kim DI, Raida M, Burke B. Roux KJ, et al. J Cell Biol. 2012 Mar 19;196(6):801-10. doi: 10.1083/jcb.201112098. Epub 2012 Mar 12. J Cell Biol. 2012. PMID: 22412018 Free PMC article. - A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein.
Rolls MM, Stein PA, Taylor SS, Ha E, McKeon F, Rapoport TA. Rolls MM, et al. J Cell Biol. 1999 Jul 12;146(1):29-44. doi: 10.1083/jcb.146.1.29. J Cell Biol. 1999. PMID: 10402458 Free PMC article. - Viral glycoproteins accumulate in newly formed annulate lamellae following infection of lymphoid cells by human herpesvirus 6.
Cardinali G, Gentile M, Cirone M, Zompetta C, Frati L, Faggioni A, Torrisi MR. Cardinali G, et al. J Virol. 1998 Dec;72(12):9738-46. doi: 10.1128/JVI.72.12.9738-9746.1998. J Virol. 1998. PMID: 9811708 Free PMC article. - Freeze-fracture immunogold labeling.
Torrisi MR, Mancini P. Torrisi MR, et al. Histochem Cell Biol. 1996 Jul;106(1):19-30. doi: 10.1007/BF02473199. Histochem Cell Biol. 1996. PMID: 8858364 Review. - The first membrane spanning region of the lamin B receptor is sufficient for sorting to the inner nuclear membrane.
Smith S, Blobel G. Smith S, et al. J Cell Biol. 1993 Feb;120(3):631-7. doi: 10.1083/jcb.120.3.631. J Cell Biol. 1993. PMID: 8381121 Free PMC article.
References
- J Virol. 1972 Nov;10(5):925-32 - PubMed
- Virology. 1963 Jul;20:433-45 - PubMed
- J Histochem Cytochem. 1977 Nov;25(11):1187-200 - PubMed
- J Mol Biol. 1978 Oct 5;124(4):587-600 - PubMed
- J Cell Biol. 1979 Jan;80(1):219-24 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources