#PAGE_PARAMS# #ADS_HEAD_SCRIPTS# #MICRODATA#

Analysis of the Initiating Events in HIV-1 Particle Assembly and Genome Packaging


HIV-1 Gag drives a number of events during the genesis of virions and is the only viral protein required for the assembly of virus-like particles in vitro and in cells. Although a reasonable understanding of the processes that accompany the later stages of HIV-1 assembly has accrued, events that occur at the initiation of assembly are less well defined. In this regard, important uncertainties include where in the cell Gag first multimerizes and interacts with the viral RNA, and whether Gag-RNA interaction requires or induces Gag multimerization in a living cell. To address these questions, we developed assays in which protein crosslinking and RNA/protein co-immunoprecipitation were coupled with membrane flotation analyses in transfected or infected cells. We found that interaction between Gag and viral RNA occurred in the cytoplasm and was independent of the ability of Gag to localize to the plasma membrane. However, Gag:RNA binding was stabilized by the C-terminal domain (CTD) of capsid (CA), which participates in Gag-Gag interactions. We also found that Gag was present as monomers and low-order multimers (e.g. dimers) but did not form higher-order multimers in the cytoplasm. Rather, high-order multimers formed only at the plasma membrane and required the presence of a membrane-binding signal, but not a Gag domain (the CA-CTD) that is essential for complete particle assembly. Finally, sequential RNA-immunoprecipitation assays indicated that at least a fraction of Gag molecules can form multimers on viral genomes in the cytoplasm. Taken together, our results suggest that HIV-1 particle assembly is initiated by the interaction between Gag and viral RNA in the cytoplasm and that this initial Gag-RNA encounter involves Gag monomers or low order multimers. These interactions per se do not induce or require high-order Gag multimerization in the cytoplasm. Instead, membrane interactions are necessary for higher order Gag multimerization and subsequent particle assembly in cells.


Vyšlo v časopise: Analysis of the Initiating Events in HIV-1 Particle Assembly and Genome Packaging. PLoS Pathog 6(11): e32767. doi:10.1371/journal.ppat.1001200
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1001200

Souhrn

HIV-1 Gag drives a number of events during the genesis of virions and is the only viral protein required for the assembly of virus-like particles in vitro and in cells. Although a reasonable understanding of the processes that accompany the later stages of HIV-1 assembly has accrued, events that occur at the initiation of assembly are less well defined. In this regard, important uncertainties include where in the cell Gag first multimerizes and interacts with the viral RNA, and whether Gag-RNA interaction requires or induces Gag multimerization in a living cell. To address these questions, we developed assays in which protein crosslinking and RNA/protein co-immunoprecipitation were coupled with membrane flotation analyses in transfected or infected cells. We found that interaction between Gag and viral RNA occurred in the cytoplasm and was independent of the ability of Gag to localize to the plasma membrane. However, Gag:RNA binding was stabilized by the C-terminal domain (CTD) of capsid (CA), which participates in Gag-Gag interactions. We also found that Gag was present as monomers and low-order multimers (e.g. dimers) but did not form higher-order multimers in the cytoplasm. Rather, high-order multimers formed only at the plasma membrane and required the presence of a membrane-binding signal, but not a Gag domain (the CA-CTD) that is essential for complete particle assembly. Finally, sequential RNA-immunoprecipitation assays indicated that at least a fraction of Gag molecules can form multimers on viral genomes in the cytoplasm. Taken together, our results suggest that HIV-1 particle assembly is initiated by the interaction between Gag and viral RNA in the cytoplasm and that this initial Gag-RNA encounter involves Gag monomers or low order multimers. These interactions per se do not induce or require high-order Gag multimerization in the cytoplasm. Instead, membrane interactions are necessary for higher order Gag multimerization and subsequent particle assembly in cells.


Zdroje

1. HarrisonGP

LeverAM

1992

The human immunodeficiency virus type 1 packaging signal and major splice donor region have a conserved stable secondary structure.

J Virol

66

4144

4153

2. LeverA

GottlingerH

HaseltineW

SodroskiJ

1989

Identification of a sequence required for efficient packaging of human immunodeficiency virus type 1 RNA into virions.

J Virol

63

4085

4087

3. LubanJ

GoffSP

1994

Mutational analysis of cis-acting packaging signals in human immunodeficiency virus type 1 RNA.

J Virol

68

3784

3793

4. CleverJ

SassettiC

ParslowTG

1995

RNA secondary structure and binding sites for gag gene products in the 5′ packaging signal of human immunodeficiency virus type 1.

J Virol

69

2101

2109

5. FinziA

OrthweinA

MercierJ

CohenEA

2007

Productive human immunodeficiency virus type 1 assembly takes place at the plasma membrane.

J Virol

81

7476

7490

6. JouvenetN

NeilSJ

BessC

JohnsonMC

VirgenCA

2006

Plasma membrane is the site of productive HIV-1 particle assembly.

PLoS Biol

4

e435

7. WelschS

KepplerOT

HabermannA

AllespachI

Krijnse-LockerJ

2007

HIV-1 buds predominantly at the plasma membrane of primary human macrophages.

PLoS Pathog

3

e36

8. BryantM

RatnerL

1990

Myristoylation-dependent replication and assembly of human immunodeficiency virus 1.

Proc Natl Acad Sci U S A

87

523

527

9. GottlingerHG

SodroskiJG

HaseltineWA

1989

Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1.

Proc Natl Acad Sci U S A

86

5781

5785

10. ZhouW

ParentLJ

WillsJW

ReshMD

1994

Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids.

J Virol

68

2556

2569

11. SaadJS

MillerJ

TaiJ

KimA

GhanamRH

2006

Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly.

Proc Natl Acad Sci U S A

103

11364

11369

12. SaadJS

LoeligerE

LuncsfordP

LirianoM

TaiJ

2007

Point mutations in the HIV-1 matrix protein turn off the myristyl switch.

J Mol Biol

366

574

585

13. OnoA

AblanSD

LockettSJ

NagashimaK

FreedEO

2004

Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane.

Proc Natl Acad Sci U S A

101

14889

14894

14. D'SouzaV

SummersMF

2005

How retroviruses select their genomes.

Nat Rev Microbiol

3

643

655

15. Ganser-PornillosBK

YeagerM

SundquistWI

2008

The structural biology of HIV assembly.

Curr Opin Struct Biol

18

203

217

16. MateuMG

2009

The capsid protein of human immunodeficiency virus: intersubunit interactions during virus assembly.

FEBS J

276

6098

6109

17. BriggsJA

SimonMN

GrossI

KrausslichHG

FullerSD

2004

The stoichiometry of Gag protein in HIV-1.

Nat Struct Mol Biol

11

672

675

18. MoritaE

SundquistWI

2004

Retrovirus budding.

Annu Rev Cell Dev Biol

20

395

425

19. BieniaszPD

2006

Late budding domains and host proteins in enveloped virus release.

Virology

344

55

63

20. CarltonJG

Martin-SerranoJ

2009

The ESCRT machinery: new functions in viral and cellular biology.

Biochem Soc Trans

37

195

199

21. HillCP

WorthylakeD

BancroftDP

ChristensenAM

SundquistWI

1996

Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly.

Proc Natl Acad Sci U S A

93

3099

3104

22. LeePP

LinialML

1994

Efficient particle formation can occur if the matrix domain of human immunodeficiency virus type 1 Gag is substituted by a myristylation signal.

J Virol

68

6644

6654

23. ReilH

BukovskyAA

GelderblomHR

GottlingerHG

1998

Efficient HIV-1 replication can occur in the absence of the viral matrix protein.

EMBO J

17

2699

2708

24. WangCT

LaiHY

LiJJ

1998

Analysis of minimal human immunodeficiency virus type 1 gag coding sequences capable of virus-like particle assembly and release.

J Virol

72

7950

7959

25. WangCT

ZhangY

McDermottJ

BarklisE

1993

Conditional infectivity of a human immunodeficiency virus matrix domain deletion mutant.

J Virol

67

7067

7076

26. DorfmanT

BukovskyA

OhagenA

HoglundS

GottlingerHG

1994

Functional domains of the capsid protein of human immunodeficiency virus type 1.

J Virol

68

8180

8187

27. LiangC

HuJ

RussellRS

RoldanA

KleimanL

2002

Characterization of a putative alpha-helix across the capsid-SP1 boundary that is critical for the multimerization of human immunodeficiency virus type 1 gag.

J Virol

76

11729

11737

28. ReicinAS

PaikS

BerkowitzRD

LubanJ

LowyI

1995

Linker insertion mutations in the human immunodeficiency virus type 1 gag gene: effects on virion particle assembly, release, and infectivity.

J Virol

69

642

650

29. von SchwedlerUK

StrayKM

GarrusJE

SundquistWI

2003

Functional surfaces of the human immunodeficiency virus type 1 capsid protein.

J Virol

77

5439

5450

30. GambleTR

YooS

VajdosFF

von SchwedlerUK

WorthylakeDK

1997

Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein.

Science

278

849

853

31. AccolaMA

StrackB

GottlingerHG

2000

Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain.

J Virol

74

5395

5402

32. GanserBK

LiS

KlishkoVY

FinchJT

SundquistWI

1999

Assembly and analysis of conical models for the HIV-1 core.

Science

283

80

83

33. LiS

HillCP

SundquistWI

FinchJT

2000

Image reconstructions of helical assemblies of the HIV-1 CA protein.

Nature

407

409

413

34. BowzardJB

BennettRP

KrishnaNK

ErnstSM

ReinA

1998

Importance of basic residues in the nucleocapsid sequence for retrovirus Gag assembly and complementation rescue.

J Virol

72

9034

9044

35. BurnistonMT

CimarelliA

ColganJ

CurtisSP

LubanJ

1999

Human immunodeficiency virus type 1 Gag polyprotein multimerization requires the nucleocapsid domain and RNA and is promoted by the capsid-dimer interface and the basic region of matrix protein.

J Virol

73

8527

8540

36. OnoA

WaheedAA

JoshiA

FreedEO

2005

Association of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assay.

J Virol

79

14131

14140

37. CimarelliA

SandinS

HoglundS

LubanJ

2000

Basic residues in human immunodeficiency virus type 1 nucleocapsid promote virion assembly via interaction with RNA.

J Virol

74

3046

3057

38. MuriauxD

MirroJ

HarvinD

ReinA

2001

RNA is a structural element in retrovirus particles.

Proc Natl Acad Sci U S A

98

5246

5251

39. CampbellS

ReinA

1999

In vitro assembly properties of human immunodeficiency virus type 1 Gag protein lacking the p6 domain.

J Virol

73

2270

2279

40. CampbellS

VogtVM

1995

Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1.

J Virol

69

6487

6497

41. GrossI

HohenbergH

KrausslichHG

1997

In vitro assembly properties of purified bacterially expressed capsid proteins of human immunodeficiency virus.

Eur J Biochem

249

592

600

42. KhorchidA

HalwaniR

WainbergMA

KleimanL

2002

Role of RNA in facilitating Gag/Gag-Pol interaction.

J Virol

76

4131

4137

43. JouvenetN

SimonSM

BieniaszPD

2009

Imaging the interaction of HIV-1 genomes and Gag during assembly of individual viral particles.

Proc Natl Acad Sci U S A

106

19114

19119

44. MorikawaY

HockleyDJ

NermutMV

JonesIM

2000

Roles of matrix, p2, and N-terminal myristoylation in human immunodeficiency virus type 1 Gag assembly.

J Virol

74

16

23

45. OnoA

DemirovD

FreedEO

2000

Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding.

J Virol

74

5142

5150

46. GuoX

RoldanA

HuJ

WainbergMA

LiangC

2005

Mutation of the SP1 sequence impairs both multimerization and membrane-binding activities of human immunodeficiency virus type 1 Gag.

J Virol

79

1803

1812

47. LiangC

HuJ

WhitneyJB

KleimanL

WainbergMA

2003

A structurally disordered region at the C terminus of capsid plays essential roles in multimerization and membrane binding of the gag protein of human immunodeficiency virus type 1.

J Virol

77

1772

1783

48. DerdowskiA

DingL

SpearmanP

2004

A novel fluorescence resonance energy transfer assay demonstrates that the human immunodeficiency virus type 1 Pr55Gag I domain mediates Gag-Gag interactions.

J Virol

78

1230

1242

49. LarsonDR

MaYM

VogtVM

WebbWW

2003

Direct measurement of Gag-Gag interaction during retrovirus assembly with FRET and fluorescence correlation spectroscopy.

J Cell Biol

162

1233

1244

50. LiH

DouJ

DingL

SpearmanP

2007

Myristoylation is required for human immunodeficiency virus type 1 Gag-Gag multimerization in mammalian cells.

J Virol

81

12899

12910

51. HogueIB

HoppeA

OnoA

2009

Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding.

J Virol

83

7322

7336

52. HubnerW

ChenP

Del PortilloA

LiuY

GordonRE

2007

Sequence of human immunodeficiency virus type 1 (HIV-1) Gag localization and oligomerization monitored with live confocal imaging of a replication-competent, fluorescently tagged HIV-1.

J Virol

81

12596

12607

53. JinJ

SturgeonT

ChenC

WatkinsSC

WeiszOA

2007

Distinct intracellular trafficking of equine infectious anemia virus and human immunodeficiency virus type 1 Gag during viral assembly and budding revealed by bimolecular fluorescence complementation assays.

J Virol

81

11226

11235

54. MilevMP

BrownCM

MoulandAJ

2010

Live cell visualization of the interactions between HIV-1 Gag and the cellular RNA-binding protein Staufen1.

Retrovirology

7

41

55. DattaSA

ZhaoZ

ClarkPK

TarasovS

AlexandratosJN

2007

Interactions between HIV-1 Gag molecules in solution: an inositol phosphate-mediated switch.

J Mol Biol

365

799

811

56. RoldanA

RussellRS

MarchandB

GotteM

LiangC

2004

In vitro identification and characterization of an early complex linking HIV-1 genomic RNA recognition and Pr55Gag multimerization.

J Biol Chem

279

39886

39894

57. JouvenetN

BieniaszPD

SimonSM

2008

Imaging the biogenesis of individual HIV-1 virions in live cells.

Nature

454

236

240

58. RulliSJJr

HibbertCS

MirroJ

PedersonT

BiswalS

2007

Selective and nonselective packaging of cellular RNAs in retrovirus particles.

J Virol

81

6623

6631

59. GeisbergJV

StruhlK

2004

Quantitative sequential chromatin immunoprecipitation, a method for analyzing co-occupancy of proteins at genomic regions in vivo.

Nucleic Acids Res

32

e151

60. Garbitt-HirstR

KenneySP

ParentLJ

2009

Genetic evidence for a connection between Rous sarcoma virus gag nuclear trafficking and genomic RNA packaging.

J Virol

83

6790

6797

61. GudleskiN

FlanaganJM

RyanEP

BewleyMC

ParentLJ

2010

Directionality of nucleocytoplasmic transport of the retroviral gag protein depends on sequential binding of karyopherins and viral RNA.

Proc Natl Acad Sci U S A

107

9358

9363

62. KemlerI

MeehanA

2010

Poeschla EM Live cell co-imaging of the genomic RNAs and Gag proteins of two lentiviruses. (2010)

J Virol

84

6352

6366

63. MooreMD

NikolaitchikOA

ChenJ

HammarskjoldML

RekoshD

2009

Probing the HIV-1 genomic RNA trafficking pathway and dimerization by genetic recombination and single virion analyses.

PLoS Pathog

5

e1000627

64. GomezCY

HopeTJ

2006

Mobility of human immunodeficiency virus type 1 Pr55Gag in living cells.

J Virol

80

8796

8806

65. PaillartJC

Shehu-XhilagaM

MarquetR

MakJ

2004

Dimerization of retroviral RNA genomes: an inseparable pair.

Nat Rev Microbiol

2

461

472

66. DurocherY

PerretS

KamenA

2002

High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells.

Nucleic Acids Res

30

E9

67. Perez-CaballeroD

HatziioannouT

Martin-SerranoJ

BieniaszPD

2004

Human immunodeficiency virus type 1 matrix inhibits and confers cooperativity on gag precursor-membrane interactions.

J Virol

78

9560

9563

68. ZennouV

Perez-CaballeroD

GottlingerH

BieniaszPD

2004

APOBEC3G incorporation into human immunodeficiency virus type 1 particles.

J Virol

78

12058

12061

69. BaroniTE

ChitturSV

GeorgeAD

TenenbaumSA

2008

Advances in RIP-chip analysis : RNA-binding protein immunoprecipitation-microarray profiling.

Methods Mol Biol

419

93

108

70. PalmerS

WiegandAP

MaldarelliF

BazmiH

MicanJM

2003

New real-time reverse transcriptase-initiated PCR assay with single-copy sensitivity for human immunodeficiency virus type 1 RNA in plasma.

J Clin Microbiol

41

4531

4536

71. SpearmanP

HortonR

RatnerL

Kuli-ZadeI

1997

Membrane binding of human immunodeficiency virus type 1 matrix protein in vivo supports a conformational myristyl switch mechanism.

J Virol

71

6582

6592

72. Simoes-BarbosaA

SantanaJM

TeixeiraAR

2000

Solubilization of delipidated macrophage membrane proteins for analysis by two-dimensional electrophoresis.

Electrophoresis

21

641

644

Štítky
Hygiena a epidemiológia Infekčné lekárstvo Laboratórium

Článok vyšiel v časopise

PLOS Pathogens


2010 Číslo 11
Najčítanejšie tento týždeň
Najčítanejšie v tomto čísle
Kurzy

Zvýšte si kvalifikáciu online z pohodlia domova

Získaná hemofilie - Povědomí o nemoci a její diagnostika
nový kurz

Eozinofilní granulomatóza s polyangiitidou
Autori: doc. MUDr. Martina Doubková, Ph.D.

Všetky kurzy
Prihlásenie
Zabudnuté heslo

Zadajte e-mailovú adresu, s ktorou ste vytvárali účet. Budú Vám na ňu zasielané informácie k nastaveniu nového hesla.

Prihlásenie

Nemáte účet?  Registrujte sa

#ADS_BOTTOM_SCRIPTS#