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Bunyamwera orthobunyavirus glycoprotein precursor is processed by cellular signal peptidase and signal peptide peptidase

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Shi_2016_PNAS_Cleavage_AAM.pdf (845.0Kb)
Date
02/08/2016
Author
Shi, Xiaohong
Botting, Catherine Helen
Li, Ping
Niglas, Mark
Brennan, Benjamin
Shirran, Sally Lorna
Szemiel, Agnieszka Marta
Elliott, Richard Michael
Keywords
Bunyavirua
Bunyamwera virus
Glycoprotein precursor processing
Signal peptidase
Signal peptide peptidase
QD Chemistry
QH301 Biology
BDC
R2C
Metadata
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Abstract
Bunyamwera virus (BUNV) is the prototype of the Orthobunyavirus genus and Bunyaviridae family that contains important human and animal pathogens. The cleavage mechanism of orthobunyavirus glycoprotein precursor (GPC) and the host proteases involved have not been clarified. Here we found that NSm and Gc contain their own internal signal peptides, which mediate the GPC cleavage by host signal peptidase and signal peptide peptidase (SPP). Furthermore, the NSm domain-I plays an important postcleavage role in cell fusion. Our data clarified the implication of host proteases in the processing of the orthobunyavirus GPC. This work identifies SPP as a potential intervention target, and the knowledge we gained will benefit preventive strategies against other orthobunyavirus infections.
Citation
Shi , X , Botting , C H , Li , P , Niglas , M , Brennan , B , Shirran , S L , Szemiel , A M & Elliott , R M 2016 , ' Bunyamwera orthobunyavirus glycoprotein precursor is processed by cellular signal peptidase and signal peptide peptidase ' , Proceedings of the National Academy of Sciences of the United States of America , vol. 113 , no. 31 , pp. 8825-8830 . https://doi.org/10.1073/pnas.1603364113
Publication
Proceedings of the National Academy of Sciences of the United States of America
Status
Peer reviewed
DOI
https://doi.org/10.1073/pnas.1603364113
ISSN
1091-6490
Type
Journal article
Rights
© 2016, the Author(s). This work is made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at www.pnas.org / https://dx.doi.org/10.1073/pnas.1603364113
Description
This study was supported by Wellcome Trust Grant 099220/B/12/Z (to R.M.E.) and Grant 094476/Z/10/Z that funded the purchase of the TripleTOF 5600 mass spectrometer at the Biomedical Sciences Research Complex (BSRC) of University of St. Andrews.
Collections
  • University of St Andrews Research
URI
http://hdl.handle.net/10023/10142

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