The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein - PubMed (original) (raw)
The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein
F Guirakhoo et al. Virology. 1992 Dec.
Abstract
To study the role of the precursor to the membrane protein (prM) in flavivirus maturation, we inhibited the proteolytic processing of the Murray Valley encephalitis (MVE) virus prM to membrane protein in infected cells by adding the acidotropic agent ammonium chloride late in the virus replication cycle. Viruses purified from supernatants of ammonium chloride-treated cells contained prM protein and were unable to fuse C6/36 mosquito cells from without. When ammonium chloride was removed from the cells, both the processing of prM and the fusion activity of the purified viruses were partially restored. By using monoclonal antibodies (MAbs) specific for the envelope (E) glycoprotein of MVE virus, we found that at least three epitopes were less accessible to their corresponding antibodies in the prM-containing MVE virus particles. Amino-terminal sequencing of proteolytic fragments of the E protein which were reactive with sequence-specific peptide antisera or MAb enabled us to estimate the site of the E protein interacting with the prM to be within amino acids 200 to 327. Since prM-containing viruses were up to 400-fold more resistant to a low pH environment, we conclude that the E-prM interaction might be necessary to protect the E protein from irreversible conformational changes caused by maturation into the acidic vesicles of the exocytic pathway.
Similar articles
- Acidotropic amines inhibit proteolytic processing of flavivirus prM protein.
Randolph VB, Winkler G, Stollar V. Randolph VB, et al. Virology. 1990 Feb;174(2):450-8. doi: 10.1016/0042-6822(90)90099-d. Virology. 1990. PMID: 2154882 - The interactions of the flavivirus envelope proteins: implications for virus entry and release.
Heinz FX, Auer G, Stiasny K, Holzmann H, Mandl C, Guirakhoo F, Kunz C. Heinz FX, et al. Arch Virol Suppl. 1994;9:339-48. doi: 10.1007/978-3-7091-9326-6_34. Arch Virol Suppl. 1994. PMID: 7913359 - Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM.
Heinz FX, Stiasny K, Püschner-Auer G, Holzmann H, Allison SL, Mandl CW, Kunz C. Heinz FX, et al. Virology. 1994 Jan;198(1):109-17. doi: 10.1006/viro.1994.1013. Virology. 1994. PMID: 8259646 - Post-translational regulation and modifications of flavivirus structural proteins.
Roby JA, Setoh YX, Hall RA, Khromykh AA. Roby JA, et al. J Gen Virol. 2015 Jul;96(Pt 7):1551-69. doi: 10.1099/vir.0.000097. Epub 2015 Feb 23. J Gen Virol. 2015. PMID: 25711963 Review. - Chaperone fusion proteins aid entropy-driven maturation of class II viral fusion proteins.
Ge P, Zhou ZH. Ge P, et al. Trends Microbiol. 2014 Feb;22(2):100-6. doi: 10.1016/j.tim.2013.11.006. Epub 2013 Dec 28. Trends Microbiol. 2014. PMID: 24380727 Free PMC article. Review.
Cited by
- Ins and Outs of Reovirus: Vesicular Trafficking in Viral Entry and Egress.
Roth AN, Aravamudhan P, Fernández de Castro I, Tenorio R, Risco C, Dermody TS. Roth AN, et al. Trends Microbiol. 2021 Apr;29(4):363-375. doi: 10.1016/j.tim.2020.09.004. Epub 2020 Sep 29. Trends Microbiol. 2021. PMID: 33008713 Free PMC article. Review. - Deconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and Immunity.
VanBlargan LA, Goo L, Pierson TC. VanBlargan LA, et al. Microbiol Mol Biol Rev. 2016 Oct 26;80(4):989-1010. doi: 10.1128/MMBR.00024-15. Print 2016 Dec. Microbiol Mol Biol Rev. 2016. PMID: 27784796 Free PMC article. Review. - A protective human monoclonal antibody targeting the West Nile virus E protein preferentially recognizes mature virions.
Goo L, Debbink K, Kose N, Sapparapu G, Doyle MP, Wessel AW, Richner JM, Burgomaster KE, Larman BC, Dowd KA, Diamond MS, Crowe JE Jr, Pierson TC. Goo L, et al. Nat Microbiol. 2019 Jan;4(1):71-77. doi: 10.1038/s41564-018-0283-7. Epub 2018 Nov 19. Nat Microbiol. 2019. PMID: 30455471 Free PMC article. - Isolation of capsid protein dimers from the tick-borne encephalitis flavivirus and in vitro assembly of capsid-like particles.
Kiermayr S, Kofler RM, Mandl CW, Messner P, Heinz FX. Kiermayr S, et al. J Virol. 2004 Aug;78(15):8078-84. doi: 10.1128/JVI.78.15.8078-8084.2004. J Virol. 2004. PMID: 15254179 Free PMC article. - C-terminal helical domains of dengue virus type 4 E protein affect the expression/stability of prM protein and conformation of prM and E proteins.
Tsai WY, Hsieh SC, Lai CY, Lin HE, Nerurkar VR, Wang WK. Tsai WY, et al. PLoS One. 2012;7(12):e52600. doi: 10.1371/journal.pone.0052600. Epub 2012 Dec 26. PLoS One. 2012. PMID: 23300717 Free PMC article.
References
- Bray M., Lai C.-J. Dengue virus premembrane and membrane proteins elicit a protective immune response. Virology. 1991;185:505–508. - PubMed
- Ciampor F., Thompson C.A., Grambas S., Hay A.J. Regulation of pH by the M2 protein of influenza A viruses. Virus Res. 1992;22:247–258. - PubMed
- Dalgarno L., Trent D.W., Strauss J.H., Rice C.M. Partial nucleotide sequence of the Murray Valley encephalitis virus genome: Comparison of the encoded polypeptides with Yellow Fever virus structural and non-structural proteins. J. Mol. Biol. 1986;187:309–323. - PubMed
- Doms R.W., Helenius A., White J. Membrane fusion activity of the influenza virus hemagglutinin: The low pH-induced conformational change. J. Biol. Chem. 1985;260:2973–2981. - PubMed
- Fischer J.M., Scheller R.H. Prohormone processing and the secretory pathway. J. Biol. Chem. 1988;32:16515–16518. - PubMed
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources