Bunyamwera orthobunyavirus glycoprotein precursor is processed by cellular signal peptidase and signal peptide peptidase
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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.
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 . DOI: 10.1073/pnas.1603364113
Proceedings of the National Academy of Sciences of the United States of America
© 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
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.
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