Literature DB >> 2837011

Individual herpes simplex virus 1 glycoproteins display characteristic rates of maturation from precursor to mature form both in infected cells and in cells that constitutively express the glycoproteins.

G Campadelli-Fiume1, M T Lombardo, L Foà-Tomasi, E Avitabile, F Serafini-Cessi.   

Abstract

Pulse-chase experiments in conjunction with quantitative immunoprecipitation have been used to study the time-course of conversion from precursor to mature form of herpes simplex virus 1 glycoproteins C, D and B (gC, gD, and gB). The experimental systems employed were two infected cell lines and cells that constitutively express gD or gB. The relative rates of conversion among the glycoproteins did not vary in the systems used; the rate of maturation of gC was about two-fold higher than that of gD which, in turn, was about one and a half-fold higher than that of gB. Treatment with phosphonoacetate which inhibits viral DNA synthesis and hence virion morphogenesis induced a striking increase in the time course of conversion of immature gC, gD, and gB to fully glycosylated forms when measured late in the infection. The model of HSV glycoproteins maturation as integral components of the virion envelope is discussed.

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Year:  1988        PMID: 2837011     DOI: 10.1016/0168-1702(88)90055-x

Source DB:  PubMed          Journal:  Virus Res        ISSN: 0168-1702            Impact factor:   3.303


  8 in total

1.  Herpes simplex virus envelopment and maturation studied by fracture label.

Authors:  M R Torrisi; C Di Lazzaro; A Pavan; L Pereira; G Campadelli-Fiume
Journal:  J Virol       Date:  1992-01       Impact factor: 5.103

2.  Herpes simplex virus type 1 glycoprotein K is not essential for infectious virus production in actively replicating cells but is required for efficient envelopment and translocation of infectious virions from the cytoplasm to the extracellular space.

Authors:  S Jayachandra; A Baghian; K G Kousoulas
Journal:  J Virol       Date:  1997-07       Impact factor: 5.103

3.  Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1.

Authors:  G Campadelli; R Brandimarti; C Di Lazzaro; P L Ward; B Roizman; M R Torrisi
Journal:  Proc Natl Acad Sci U S A       Date:  1993-04-01       Impact factor: 11.205

4.  The herpes simplex virus UL20 protein compensates for the differential disruption of exocytosis of virions and viral membrane glycoproteins associated with fragmentation of the Golgi apparatus.

Authors:  E Avitabile; P L Ward; C Di Lazzaro; M R Torrisi; B Roizman; G Campadelli-Fiume
Journal:  J Virol       Date:  1994-11       Impact factor: 5.103

5.  Herpes simplex virus particles are unable to traverse the secretory pathway in the mouse L-cell mutant gro29.

Authors:  B W Banfield; F Tufaro
Journal:  J Virol       Date:  1990-12       Impact factor: 5.103

6.  Protection from herpes simplex virus type 1 lethal and latent infections by secreted recombinant glycoprotein B constitutively expressed in human cells with a BK virus episomal vector.

Authors:  R Manservigi; M P Grossi; R Gualandri; P G Balboni; A Marchini; A Rotola; P Rimessi; D Di Luca; E Cassai; G Barbanti-Brodano
Journal:  J Virol       Date:  1990-01       Impact factor: 5.103

7.  Differential rates of processing and transport of herpes simplex virus type 1 glycoproteins gB and gC.

Authors:  M Sommer; R J Courtney
Journal:  J Virol       Date:  1991-01       Impact factor: 5.103

8.  A block in glycoprotein processing correlates with small plaque morphology and virion targetting to cell-cell junctions for an oral and an anal strain of herpes simplex virus type-1.

Authors:  J W Dick; K S Rosenthal
Journal:  Arch Virol       Date:  1995       Impact factor: 2.574

  8 in total

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