Viral inactivation based on inhibition of membrane fusion: understanding the role of histidine protonation to develop new viral vaccines
- PMID: 19601907
- DOI: 10.2174/092986609788681823
Viral inactivation based on inhibition of membrane fusion: understanding the role of histidine protonation to develop new viral vaccines
Abstract
Membrane fusion is an essential step in the entry of enveloped viruses into their host cells, what makes it a potentially attractive target for viral inactivation approaches. Fusion is mediated by viral surface glycoproteins that undergo conformational changes triggered by interaction with specific cellular receptors or by the exposition to low pH of endossomal medium. Here we review how several studies on the structural rearrangements of vesicular stomatitis virus (VSV) glycoprotein G during cellular recognition and fusion led us to propose a crucial role of the protonation of His residues for G protein activity. Moreover, we demonstrated that using diethylpyrocarbonate (DEPC), a histidine-modifying compound, it was possible to abolish viral infectivity and pathogenicity in mice, and to elicit neutralizing antibodies that confer protection in these animals against challenge using lethal doses of the virus. The presence of conserved His residues in a wide range of viral fusion proteins and the use of DEPC as a more general means for vaccine development will be also discussed.
Similar articles
-
Structures of vesicular stomatitis virus glycoprotein: membrane fusion revisited.Cell Mol Life Sci. 2008 Jun;65(11):1716-28. doi: 10.1007/s00018-008-7534-3. Cell Mol Life Sci. 2008. PMID: 18345480 Free PMC article. Review.
-
New chemical method of viral inactivation for vaccine development based on membrane fusion inhibition.Vaccine. 2007 Nov 14;25(46):7885-92. doi: 10.1016/j.vaccine.2007.09.025. Epub 2007 Sep 29. Vaccine. 2007. PMID: 17949864
-
The Role of histidine residues in low-pH-mediated viral membrane fusion.Structure. 2006 Oct;14(10):1481-7. doi: 10.1016/j.str.2006.07.011. Structure. 2006. PMID: 17027497 Review.
-
Inactivation of vesicular stomatitis virus through inhibition of membrane fusion by chemical modification of the viral glycoprotein.Antiviral Res. 2007 Jan;73(1):31-9. doi: 10.1016/j.antiviral.2006.07.007. Epub 2006 Aug 2. Antiviral Res. 2007. PMID: 16934341
-
Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation.J Biol Chem. 2003 Apr 18;278(16):13789-94. doi: 10.1074/jbc.M210615200. Epub 2003 Feb 4. J Biol Chem. 2003. PMID: 12571240
Cited by
-
Recent Development of Ruminant Vaccine Against Viral Diseases.Front Vet Sci. 2021 Nov 3;8:697194. doi: 10.3389/fvets.2021.697194. eCollection 2021. Front Vet Sci. 2021. PMID: 34805327 Free PMC article. Review.
-
A histidine-rich linker region in peptidylglycine α-amidating monooxygenase has the properties of a pH sensor.J Biol Chem. 2014 May 2;289(18):12404-20. doi: 10.1074/jbc.M113.545947. Epub 2014 Mar 13. J Biol Chem. 2014. PMID: 24627494 Free PMC article.
-
Autographa californica multiple nucleopolyhedrovirus GP64 protein: roles of histidine residues in triggering membrane fusion and fusion pore expansion.J Virol. 2011 Dec;85(23):12492-504. doi: 10.1128/JVI.05153-11. Epub 2011 Sep 21. J Virol. 2011. PMID: 21937651 Free PMC article.
-
Dengue virus ensures its fusion in late endosomes using compartment-specific lipids.PLoS Pathog. 2010 Oct 7;6(10):e1001131. doi: 10.1371/journal.ppat.1001131. PLoS Pathog. 2010. PMID: 20949067 Free PMC article.
-
Adaptive evolution and inherent tolerance to extreme thermal environments.BMC Evol Biol. 2010 Mar 12;10:75. doi: 10.1186/1471-2148-10-75. BMC Evol Biol. 2010. PMID: 20226044 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
