Imperial College London
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Dr Poh-Choo Pang

Faculty of Natural Sciences, Department of Life Sciences

Visiting Researcher
 
 
 
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Contact

 

p.pang05 Website

 
 
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Location

 

Room 3158 Prince's GateSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Lété:2016:10.1128/JVI.01722-15,
author = {Lété, C and Markine-Goriaynoff, N and Machiels, B and Pang, P and Xiao, X and Canis, K and Suzuki, M and Fukuda, M and Dell, A and Haslam, SM and Vanderplasschen, A and Gillet, L},
doi = {10.1128/JVI.01722-15},
journal = {Journal of Virology},
pages = {2039--2051},
title = {Bovine Herpesvirus 4 Modulates Its β-1,6-N-Acetylglucosaminyltransferase Activity through Alternative Splicing},
url = {http://dx.doi.org/10.1128/JVI.01722-15},
volume = {90},
year = {2016}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - Carbohydrates play major roles in host-virus interactions. It is therefore not surprising that, during coevolution with their hosts, viruses have developed sophisticated mechanisms to hijack for their profit different pathways of glycan synthesis. Thus, the Bo17 gene of Bovine herpesvirus 4 (BoHV-4) encodes a homologue of the cellular core 2 protein β-1,6-N-acetylglucosaminyltransferase-mucin type (C2GnT-M), which is a key player for the synthesis of complex O-glycans. Surprisingly, we show in this study that, as opposed to what is observed for the cellular enzyme, two different mRNAs are encoded by the Bo17 gene of all available BoHV-4 strains. While the first one corresponds to the entire coding sequence of the Bo17 gene, the second results from the splicing of a 138-bp intron encoding critical residues of the enzyme. Antibodies generated against the Bo17 C terminus showed that the two forms of Bo17 are expressed in BoHV-4 infected cells, but enzymatic assays revealed that the spliced form is not active. In order to reveal the function of these two forms, we then generated recombinant strains expressing only the long or the short form of Bo17. Although we did not highlight replication differences between these strains, glycomic analyses and lectin neutralization assays confirmed that the splicing of the Bo17 gene gives the potential to BoHV-4 to fine-tune the global level of core 2 branching activity in the infected cell. Altogether, these results suggest the existence of new mechanisms to regulate the activity of glycosyltransferases from the Golgi apparatus.IMPORTANCE Viruses are masters of adaptation that hijack cellular pathways to allow their growth. Glycans play a central role in many biological processes, and several studies have highlighted mechanisms by which viruses can affect glycosylation. Glycan synthesis is a nontemplate process regulated by the availability of key glycosyltransferases. Interestingly, bovine herpesvirus 4 encodes one such enzyme
AU  - Lété,C
AU  - Markine-Goriaynoff,N
AU  - Machiels,B
AU  - Pang,P
AU  - Xiao,X
AU  - Canis,K
AU  - Suzuki,M
AU  - Fukuda,M
AU  - Dell,A
AU  - Haslam,SM
AU  - Vanderplasschen,A
AU  - Gillet,L
DO  - 10.1128/JVI.01722-15
EP  - 2051
PY  - 2016///
SP  - 2039
TI  - Bovine Herpesvirus 4 Modulates Its β-1,6-N-Acetylglucosaminyltransferase Activity through Alternative Splicing
T2  - Journal of Virology
UR  - http://dx.doi.org/10.1128/JVI.01722-15
UR  - http://jvi.asm.org/content/90/4/2039.abstract
UR  - http://hdl.handle.net/10044/1/28671
VL  - 90
ER  -
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