Literature DB >> 9852965

Intracellular transport of varicella-zoster glycoproteins.

Z Wang1, M D Gershon, O Lungu, C A Panagiotidis, Z Zhu, Y Hao, A A Gershon.   

Abstract

Previous observations have established that varicella-zoster virus (VZV) is enveloped in the trans-Golgi network (TGN) in cultures infected with VZV and that the glycoprotein gE is targeted to the TGN by a signal sequence (AYRV) and an acidic TGN signal patch in its cytosolic domain. Neither sequence is present in other VZV glycoproteins. Like gE, gI was targeted to the TGN when it was expressed in transfected cells, suggesting that gI also contains TGN targeting information (colocalized with gE and the AP-1 adaptin complex). In contrast, gB, gC, gH, and gL immunoreactivities were not detected in the TGN when they were expressed individually in transfected cells. In VZV-infected cells, gE, gI, gH, and gL were all concentrated in the TGN. Since VZV glycoproteins that lack targeting sequences (gB, gC, gH, and gL) concentrated in the TGN of infected cells, it is proposed that gE and gI, which have such sequences, serve as navigator glycoproteins, forming complexes that direct the signal-deficient glycoproteins to the TGN.

Entities:  

Mesh:

Substances:

Year:  1998        PMID: 9852965     DOI: 10.1086/514268

Source DB:  PubMed          Journal:  J Infect Dis        ISSN: 0022-1899            Impact factor:   5.226


  11 in total

1.  Trafficking of varicella-zoster virus glycoprotein gI: T(338)-dependent retention in the trans-Golgi network, secretion, and mannose 6-phosphate-inhibitable uptake of the ectodomain.

Authors:  Z H Wang; M D Gershon; O Lungu; Z Zhu; A A Gershon
Journal:  J Virol       Date:  2000-07       Impact factor: 5.103

Review 2.  Directed egress of animal viruses promotes cell-to-cell spread.

Authors:  David C Johnson; Mary T Huber
Journal:  J Virol       Date:  2002-01       Impact factor: 5.103

3.  Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope.

Authors:  Lucie Maresova; Tracy Jo Pasieka; Elizabeth Homan; Erick Gerday; Charles Grose
Journal:  J Virol       Date:  2005-01       Impact factor: 5.103

4.  Role of the varicella-zoster virus gB cytoplasmic domain in gB transport and viral egress.

Authors:  Thomas C Heineman; Susan L Hall
Journal:  J Virol       Date:  2002-01       Impact factor: 5.103

5.  The Glycoprotein B Cytoplasmic Domain Lysine Cluster Is Critical for Varicella-Zoster Virus Cell-Cell Fusion Regulation and Infection.

Authors:  Edward Yang; Ann M Arvin; Stefan L Oliver
Journal:  J Virol       Date:  2016-12-16       Impact factor: 5.103

6.  Essential role played by the C-terminal domain of glycoprotein I in envelopment of varicella-zoster virus in the trans-Golgi network: interactions of glycoproteins with tegument.

Authors:  Z H Wang; M D Gershon; O Lungu; Z Zhu; S Mallory; A M Arvin; A A Gershon
Journal:  J Virol       Date:  2001-01       Impact factor: 5.103

7.  Cytoplasmic domain signal sequences that mediate transport of varicella-zoster virus gB from the endoplasmic reticulum to the Golgi.

Authors:  T C Heineman; N Krudwig; S L Hall
Journal:  J Virol       Date:  2000-10       Impact factor: 5.103

8.  Virion association of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, requires expression of the VZV open reading frame 66 protein kinase.

Authors:  P R Kinchington; K Fite; A Seman; S E Turse
Journal:  J Virol       Date:  2001-10       Impact factor: 5.103

9.  Glycoprotein E of varicella-zoster virus enhances cell-cell contact in polarized epithelial cells.

Authors:  C Mo; E E Schneeberger; A M Arvin
Journal:  J Virol       Date:  2000-12       Impact factor: 5.103

10.  A functional YNKI motif in the short cytoplasmic tail of varicella-zoster virus glycoprotein gH mediates clathrin-dependent and antibody-independent endocytosis.

Authors:  Tracy Jo Pasieka; Lucie Maresova; Charles Grose
Journal:  J Virol       Date:  2003-04       Impact factor: 5.103

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.