» Articles » PMID: 17553172

Human Neuronal Cell Protein Responses to Nipah Virus Infection

Overview
Journal Virol J
Publisher Biomed Central
Specialty Microbiology
Date 2007 Jun 8
PMID 17553172
Citations 6
Authors
Affiliations
Soon will be listed here.
Abstract

Background: Nipah virus (NiV), a recently discovered zoonotic virus infects and replicates in several human cell types. Its replication in human neuronal cells, however, is less efficient in comparison to other fully susceptible cells. In the present study, the SK-N-MC human neuronal cell protein response to NiV infection is examined using proteomic approaches.

Results: Method for separation of the NiV-infected human neuronal cell proteins using two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) was established. At least 800 protein spots were resolved of which seven were unique, six were significantly up-regulated and eight were significantly down-regulated. Six of these altered proteins were identified using mass spectrometry (MS) and confirmed using MS/MS. The heterogenous nuclear ribonucleoprotein (hnRNP) F, guanine nucleotide binding protein (G protein), voltage-dependent anion channel 2 (VDAC2) and cytochrome bc1 were present in abundance in the NiV-infected SK-N-MC cells in contrast to hnRNPs H and H2 that were significantly down-regulated.

Conclusion: Several human neuronal cell proteins that are differentially expressed following NiV infection are identified. The proteins are associated with various cellular functions and their abundance reflects their significance in the cytopathologic responses to the infection and the regulation of NiV replication. The potential importance of the ratio of hnRNP F, and hnRNPs H and H2 in regulation of NiV replication, the association of the mitochondrial protein with the cytopathologic responses to the infection and induction of apoptosis are highlighted.

Citing Articles

Recent Advances in Immunological Landscape and Immunotherapeutic Agent of Nipah Virus Infection.

Chakraborty C, Saha S, Bhattacharya M Cell Biochem Biophys. 2024; 82(4):3053-3069.

PMID: 39052192 DOI: 10.1007/s12013-024-01424-4.


Multiple functions of heterogeneous nuclear ribonucleoproteins in the positive single-stranded RNA virus life cycle.

Wang J, Sun D, Wang M, Cheng A, Zhu Y, Mao S Front Immunol. 2022; 13:989298.

PMID: 36119073 PMC: 9478383. DOI: 10.3389/fimmu.2022.989298.


Henipavirus infection of the central nervous system.

Dawes B, Freiberg A Pathog Dis. 2019; 77(2).

PMID: 30985897 PMC: 6974701. DOI: 10.1093/femspd/ftz023.


hnRNP F directs formation of an exon 4 minus variant of tumor-associated NADH oxidase (ENOX2).

Tang X, Kane V, Morre D, Morre D Mol Cell Biochem. 2011; 357(1-2):55-63.

PMID: 21625959 DOI: 10.1007/s11010-011-0875-5.


Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs.

Dominguez C, Fisette J, Chabot B, Allain F Nat Struct Mol Biol. 2010; 17(7):853-61.

PMID: 20526337 DOI: 10.1038/nsmb.1814.


References
1.
Birney E, Kumar S, Krainer A . Analysis of the RNA-recognition motif and RS and RGG domains: conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res. 1993; 21(25):5803-16. PMC: 310458. DOI: 10.1093/nar/21.25.5803. View

2.
AbuBakar S, Chang L, Ali A, Sharifah S, Yusoff K, Zamrod Z . Isolation and molecular identification of Nipah virus from pigs. Emerg Infect Dis. 2005; 10(12):2228-30. PMC: 3323361. DOI: 10.3201/eid1012.040452. View

3.
Schreck R, Rieber P, Baeuerle P . Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-kappa B transcription factor and HIV-1. EMBO J. 1991; 10(8):2247-58. PMC: 452914. DOI: 10.1002/j.1460-2075.1991.tb07761.x. View

4.
Neuhoff V, Arold N, Taube D, Ehrhardt W . Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis. 1988; 9(6):255-62. DOI: 10.1002/elps.1150090603. View

5.
Roberts D, Waelbroeck M . G protein activation by G protein coupled receptors: ternary complex formation or catalyzed reaction?. Biochem Pharmacol. 2004; 68(5):799-806. DOI: 10.1016/j.bcp.2004.05.044. View