+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Identification and characterization of a Golgi retention signal in feline coronavirus accessory protein 7b

Identification and characterization of a Golgi retention signal in feline coronavirus accessory protein 7b

Journal of General Virology 98(8): 2017-2029

Feline coronaviruses encode five accessory proteins with largely elusive functions. Here, one of these proteins, called 7b (206 residues), was investigated using a reverse genetic approach established for feline infectious peritonitis virus (FIPV) strain 79-1146. Recombinant FIPVs (rFPIVs) expressing mutant and/or FLAG-tagged forms of 7b were generated and used to investigate the expression, processing, glycosylation, localization and trafficking of the 7b protein in rFIPV-infected cells, focusing on a previously predicted ER retention signal, KTEL, at the C-terminus of 7b. The study revealed that 7b is N-terminally processed by a cellular signalase. The cleavage site, 17-Ala|Thr-18, was unambiguously identified by N-terminal sequence analysis of a 7b processing product purified from rFIPV-infected cells. Based on this information, rFIPVs expressing FLAG-tagged 7b proteins were generated and the effects of substitutions in the C-terminal 202KTEL206 sequence were investigated. The data show that (i) 7b localizes to and is retained in the medial- and/or trans-Golgi compartment, (ii) the C-terminal KTEL sequence acts as a Golgi [rather than an endoplasmic reticulum (ER)] retention signal, (iii) minor changes in the KTEL motif (such as KTE, KTEV, or the addition of a C-terminal tag) abolish Golgi retention, resulting in relocalization and secretion of 7b, and (iv) a KTEL-to-KDEL replacement causes retention of 7b in the ER of rFIPV-infected feline cells. Taken together, this study provides interesting new insights into an efficient Golgi retention signal that controls the cellular localization and trafficking of the FIPV 7b protein in virus-infected feline cells.

Please choose payment method:

(PDF emailed within 1 workday: $29.90)

Accession: 059822089

Download citation: RISBibTeXText

PMID: 28758629

Related references

A Golgi retention signal in a membrane-spanning domain of coronavirus E1 protein. Journal of Cell Biology 115(1): 19-30, 1991

Characterization of monoclonal antibodies against feline coronavirus accessory protein 7b. Veterinary Microbiology 184: 11-19, 2016

Identification of a Golgi complex-targeting signal in the cytoplasmic tail of the severe acute respiratory syndrome coronavirus envelope protein. Journal of Virology 85(12): 5794-5803, 2011

A novel glycoprotein of feline infectious peritonitis coronavirus contains a KDEL-like endoplasmic reticulum retention signal. Advances in experimental medicine and biology42(342): 209-214, 1993

The missing link in coronavirus assembly. Retention of the avian coronavirus infectious bronchitis virus envelope protein in the pre-Golgi compartments and physical interaction between the envelope and membrane proteins. Journal of Biological Chemistry 276(20): 17515-17523, 2001

Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal. Molecular Biology of the Cell 6(1): 7-20, 1995

The transmembrane domain of the severe acute respiratory syndrome coronavirus ORF7b protein is necessary and sufficient for its retention in the Golgi complex. Journal of Virology 82(19): 9477-9491, 2008

Delineation and modelling of a nucleolar retention signal in the coronavirus nucleocapsid protein. Traffic 7(7): 833-848, 2006

Characterization of a Golgi retention signal within a heterodimeric viral glycoprotein complex. Molecular Biology of the Cell 4(Suppl. ): 314A, 1993

Identification and characterization of a coronavirus packaging signal. Journal of Virology 66(6): 3522-3530, 1992

The rat testicular protein Crisp-2 contains a carboxyl-terminus Golgi retention signal. Molecular Biology of the Cell 12(Suppl.): 379a, 2001

A lysine-methionine exchange in a coronavirus surface protein transforms a retention motif into an endocytosis signal. Biological Chemistry 395(6): 657-665, 2014

Feline coronavirus type II strains 79-1683 and 79-1146 originate from a double recombination between feline coronavirus type I and canine coronavirus. Journal of Virology 72(5): 4508-4514, 1998

The retention signal for a model golgi protein is contained in a membrane spanning domain. Journal of Cell Biology 111(5 Part 2): 202A, 1990

Mapping a retention signal for Golgi localization of a viral spike protein complex. Cold Spring Harbor Symposia on Quantitative Biology 60: 147-155, 1995