Salt Enhances the Thermostability of Enteroviruses by Stabilizing Capsid Protein Interfaces.
coxsackievirus B1
coxsackievirus B5
echovirus 11
pentamer interface
protomer interface
thermostability
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
18 05 2020
18 05 2020
Historique:
received:
26
12
2019
accepted:
11
03
2020
pubmed:
28
3
2020
medline:
21
10
2020
entrez:
28
3
2020
Statut:
epublish
Résumé
Enteroviruses are common agents of infectious disease that are spread by the fecal-oral route. They are readily inactivated by mild heat, which causes the viral capsid to disintegrate or undergo conformational change. While beneficial for the thermal treatment of food or water, this heat sensitivity poses challenges for the stability of enterovirus vaccines. The thermostability of an enterovirus can be modulated by the composition of the suspending matrix, though the effects of the matrix on virus stability are not understood. Here, we determined the thermostability of four enterovirus strains in solutions with various concentrations of NaCl and different pH values. The experimental findings were combined with molecular modeling of the protein interaction forces at the pentamer and the protomer interfaces of the viral capsids. While pH only had a modest effect on thermostability, increasing NaCl concentrations raised the breakpoint temperatures of all viruses tested by up to 20°C. This breakpoint shift could be explained by an enhancement of the van der Waals attraction forces at the two protein interfaces. In comparison, the (net repulsive) electrostatic interactions were less affected by NaCl. Depending on the interface considered, the breakpoint temperature shifted by 7.5 or 5.6°C per 100-kcal/(mol·Å) increase in protein interaction force.
Identifiants
pubmed: 32213614
pii: JVI.02176-19
doi: 10.1128/JVI.02176-19
pmc: PMC7269450
pii:
doi:
Substances chimiques
Capsid Proteins
0
Sodium Chloride
451W47IQ8X
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2020 American Society for Microbiology.
Références
Arch Gesamte Virusforsch. 1965;17(5):585-93
pubmed: 4286860
Nat Struct Mol Biol. 2015 Oct;22(10):788-94
pubmed: 26389739
Appl Environ Microbiol. 1985 Apr;49(4):981-3
pubmed: 2988441
J Mol Graph. 1996 Feb;14(1):33-8, 27-8
pubmed: 8744570
BMC Struct Biol. 2011 Jan 26;11:6
pubmed: 21269479
Curr Opin Infect Dis. 2015 Oct;28(5):479-87
pubmed: 26203854
J Comput Chem. 2005 Dec;26(16):1781-802
pubmed: 16222654
J Virol. 2017 Apr 28;91(10):
pubmed: 28298597
Appl Microbiol. 1966 Mar;14(2):141-4
pubmed: 5335380
J Virol. 2019 Mar 5;93(6):
pubmed: 30567995
J Med Virol. 2004 Nov;74(3):484-91
pubmed: 15368512
Hum Vaccin Immunother. 2014;10(2):360-7
pubmed: 24231751
Lancet Child Adolesc Health. 2019 Oct;3(10):697-704
pubmed: 31375313
J Virol. 2011 Jan;85(2):776-83
pubmed: 20980499
J Appl Microbiol. 2012 Jun;112(6):1059-74
pubmed: 22380614
J Virol. 2017 Jan 31;91(4):
pubmed: 27928008
J Food Prot. 1981 Apr;44(4):320-325
pubmed: 30836585
Expert Rev Vaccines. 2014 Jul;13(7):843-54
pubmed: 24865112
PLoS Pathog. 2013 Mar;9(3):e1003255
pubmed: 23544011
Virology. 1965 Aug;26(4):694-9
pubmed: 4284207
Nat Struct Mol Biol. 2012 Mar 04;19(4):424-9
pubmed: 22388738
Structure. 2014 Nov 4;22(11):1560-70
pubmed: 25308865
Structure. 1995 Jul 15;3(7):653-67
pubmed: 8591043
J Virol. 2012 Jul;86(13):7207-15
pubmed: 22514349
J Virol. 2000 Feb;74(3):1342-54
pubmed: 10627545
Environ Sci Technol. 2018 Mar 20;52(6):3696-3705
pubmed: 29466658
Tex Rep Biol Med. 1961;19:683-700
pubmed: 14004708
Curr Protoc Bioinformatics. 2014 Sep 08;47:5.6.1-32
pubmed: 25199792
Vaccine. 2018 Jan 29;36(5):653-659
pubmed: 29295756
J Virol. 2010 May;84(9):4426-41
pubmed: 20181687
Appl Environ Microbiol. 1985 Feb;49(2):359-64
pubmed: 2984991
PLoS Pathog. 2013 Mar;9(3):e1003240
pubmed: 23555253