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Table of Contents   
LETTER TO THE EDITOR  
Year : 2017  |  Volume : 10  |  Issue : 6  |  Page : 1844-1845
Structural and functional analysis of Zika virus nonstructural protein 1 by structural genomics approach


1 RVT Medical Center, Bangkok, Thailand
2 Hainan Medical University, Hainan, China

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Date of Web Publication11-Jan-2018
 

How to cite this article:
Sriwijitalai W, Wiwanitkit V. Structural and functional analysis of Zika virus nonstructural protein 1 by structural genomics approach. Ann Trop Med Public Health 2017;10:1844-5

How to cite this URL:
Sriwijitalai W, Wiwanitkit V. Structural and functional analysis of Zika virus nonstructural protein 1 by structural genomics approach. Ann Trop Med Public Health [serial online] 2017 [cited 2018 Aug 15];10:1844-5. Available from: http://www.atmph.org/text.asp?2017/10/6/1844/222650


Dear Sir,

Zika virus is a new emerging pathogen to be focused in the present day. As a new problematic virus, there are only a few reports on its structure and function. Of several parts of the virus, nonstructural protein 1 is widely mentioned for its clinical correlation to pathogenesis.[1] Here, the authors use structural genomics approach for predicting and assessing the structure and function of Zika virus nonstructural protein 1 (5IY3). The tool namely ProFunc [2] was used. According to the study, the functional prediction by gene ontology approach shows no function and biological process of nonstructural protein 1, but the protein is confirmed to be within the group of “Flavivirus non-structural Protein NS1.” There is no identified enzyme active site and ligand binding site within the molecule. For the similarity, the Zika virus nonstructural protein 1 is high similarly to dengue virus nonstructural protein ns1 and West Nile virus nonstructural protein ns1. Focusing on sequences, the similarity to West Nile virus nonstructural protein ns1 is less than that to dengue virus nonstructural protein ns1. But focusing on matching folds, the similarity to West Nile virus nonstructural protein ns1 is more than that to dengue virus nonstructural protein ns1. Based on this finding, there might be no actual function of Zika virus nonstructural protein 1, but it might play roles in complex formation with host protein during infection. In addition, the similarity to West Nile virus protein brings our attention to further study the common problem between Zika virus and West Nile virus infections. Also, it might be the way to find new drug against Zika virus infection.[3]

Financial support and sponsorship

Nil.

Conflicts of interest

There are no conflicts of interest.



 
   References Top

1.
Song H, Qi J, Haywood J, Shi Y, Gao GF. Zika virus NS1 structure reveals diversity of electrostatic surfaces among flaviviruses. Nat Struct Mol Biol 2016;23:456-8.  Back to cited text no. 1
    
2.
Laskowski RA, Watson JD, Thornton JM. ProFunc: a server for predicting protein function from 3D structure. Nucleic Acids Res 2005;33:W89-93.  Back to cited text no. 2
[PUBMED]    
3.
Savidis G, Perreira JM, Portmann JM, Meraner P, Guo Z, Green S. The IFITMs inhibit zika virus replication. Cell Rep 2016;15:2323-30.  Back to cited text no. 3
    

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Correspondence Address:
Won Sriwijitalai
RVT Medical Center, Bangkok
Thailand
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/1755-6783.222650

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