Mathematical determination of the HIV-1 matrix shell structure and its impact on the biology of HIV-1.
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2019
2019
Historique:
received:
10
07
2019
accepted:
26
10
2019
entrez:
13
11
2019
pubmed:
13
11
2019
medline:
21
3
2020
Statut:
epublish
Résumé
Since its discovery in the early 1980s, there has been significant progress in understanding the biology of type 1 human immunodeficiency virus (HIV-1). Structural biologists have made tremendous contributions to this challenge, guiding the development of current therapeutic strategies. Despite our efforts, there are unresolved structural features of the virus and consequently, significant knowledge gaps in our understanding. The superstructure of the HIV-1 matrix (MA) shell has not been elucidated. Evidence by various high-resolution microscopy techniques support a model composed of MA trimers arranged in a hexameric configuration consisting of 6 MA trimers forming a hexagon. In this manuscript we review the mathematical limitations of this model and propose a new model consisting of a 6-lune hosohedra structure, which aligns with available structural evidence. We used geometric and rotational matrix computation methods to construct our model and predict a new mechanism for viral entry that explains the increase in particle size observed during CD4 receptor engagement and the most common HIV-1 ellipsoidal shapes observed in cryo-EM tomograms. A better understanding of the HIV-1 MA shell structure is a key step towards better models for viral assembly, maturation and entry. Our new model will facilitate efforts to improve understanding of the biology of HIV-1.
Identifiants
pubmed: 31714942
doi: 10.1371/journal.pone.0224965
pii: PONE-D-19-19426
pmc: PMC6850549
doi:
Substances chimiques
Peptides
0
Viral Matrix Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0224965Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
Références
Adv Chem Phys. 2014;155:1-68
pubmed: 25663722
PLoS One. 2018 Apr 20;13(4):e0196133
pubmed: 29677208
EMBO J. 2003 Apr 1;22(7):1707-15
pubmed: 12660176
J Mol Biol. 2011 Jul 22;410(4):582-608
pubmed: 21762802
Proc Natl Acad Sci U S A. 2014 Jun 3;111(22):8233-8
pubmed: 24843179
Proc Natl Acad Sci U S A. 2009 Jul 7;106(27):11090-5
pubmed: 19549863
J Virol. 1996 Jan;70(1):341-51
pubmed: 8523546
Structure. 2006 Jan;14(1):15-20
pubmed: 16407061
Bull Math Biol. 2019 May;81(5):1506-1526
pubmed: 30706326
J Mol Biol. 2005 Feb 18;346(2):577-88
pubmed: 15670606
J Virol. 2013 Jul;87(13):7516-25
pubmed: 23637402
PLoS Pathog. 2013;9(11):e1003739
pubmed: 24244165
Annu Rev Phys Chem. 2015 Apr;66:217-39
pubmed: 25532951
Biochemistry. 1999 Nov 2;38(44):14644-52
pubmed: 10545189
Faraday Discuss. 2014;169:23-44
pubmed: 25253262
Proc Natl Acad Sci U S A. 2003 Dec 23;100(26):15812-7
pubmed: 14668432
PLoS Comput Biol. 2014 Jul 17;10(7):e1003720
pubmed: 25032790
Virology. 2009 May 10;387(2):466-72
pubmed: 19327811
Curr Opin Virol. 2016 Jun;18:36-43
pubmed: 27016708
J Mol Biol. 2007 Feb 16;366(2):574-85
pubmed: 17188710
PLoS Pathog. 2013 Feb;9(2):e1003198
pubmed: 23468635
Proc Natl Acad Sci U S A. 2018 Nov 6;115(45):11519-11524
pubmed: 30333189
Nature. 2013 May 30;497(7451):643-6
pubmed: 23719463
Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):3099-104
pubmed: 8610175
J Mol Biol. 1994 Aug 5;241(1):59-67
pubmed: 8051707
Nat Rev Microbiol. 2015 Aug;13(8):484-96
pubmed: 26119571
EMBO J. 1996 Nov 1;15(21):5783-8
pubmed: 8918455
Virology. 2015 Dec;486:121-33
pubmed: 26432024