Zika Virus NS1 Protein (strain Zika SPH2015) (recombinant)

Zika virus (ZIKV) is a mosquito-borne, positive-stranded RNA virus and a member of the Flavivirus genus.^1,2 ZIKV infection is associated with fever, rashes, and conjunctivitis, as well as more severe symptoms, which include Guillain-Barré syndrome in adults and microcephaly or congenital malformations in fetuses and newborns.^1,3 The single-stranded RNA genome of ZIKV is translated as a polypeptide, which is cleaved by host and viral proteases into structural capsid (C), precursor membrane (prM), and envelope (E) proteins and seven non-structural proteins: NS1, NS2A, NS2B, NS3, NS4A, NS4B, and NS5.^1,4 ZIKV NS1 protein is composed of an N-terminal β-roll, a flexible wing domain, and a C-terminal β ladder and is present in the endoplasmic reticulum (ER) as a flat, cross-shaped homodimer with a glycosylated hydrophilic side and a hydrophobic side that forms contacts with lipids and lipid membranes.⁵ It is secreted from the Golgi body as a homohexamer where it can form lipoprotein complexes and interfere with host cell immune signaling.^5,6,7 ZIKV NS1 protein prevents retinoic acid-inducible gene I-induced phosphorylation of TANK-binding kinase 1 (TBK1) and IFN response factor 3 (IRF3), thus inhibiting IFN-β gene expression and secretion from infected host cells.⁶ It also promotes caspase 1-induced cyclic GMP-AMP synthase (cGAS) degradation, further reducing IFN-β signaling and allowing for continued replication of ZIKV in infected cells.⁷ Cayman's Zika Virus NS1 Protein (strain Zika SPH2015) (recombinant) protein consists of 361 amino acids, has a calculated molecular weight of 42.6 kDa, and a predicted N-terminus of Val296 after signal peptide cleavage.

WARNING This product is not for human or veterinary use.

1. Lei, J., Hansen, G., Nitsche, C., et al. Crystal structure of Zika virus NS2B-NS3 protease in complex with a boronate inhibitor. Science 353(6298), 503-505 (2016).

2. Hu, T., Wu, Z., Wu, S., et al. The key amino acids of E protein involved in early flavivirus infection: Viral entry. Virol. J. 18(1), 136 (2021).

3. Carbaugh, D.L., Baric, R.S., and Lazear, H.M. Envelope protein glycosylation mediates Zika virus pathogenesis. J. Virol. 93(12), e00113-e00119 (2019).

4. Dai, L., Song, J., Lu, X., et al. Structures of the Zika virus envelope protein and its complex with a flavivirus broadly protective antibody. Cell Host Microbe. 19(5), 696-704 (2016).

5. Brown, W.C., Akey, D.L., Konwerski, J.R., et al. Extended surface for membrane association in Zika virus NS1 structure. Nat. Struct. Mol. Biol. 23(9), 865-867 (2016).

6. Wu, Y., Liu, Q., Zhou, J., et al. Zika virus evades interferon-mediated antiviral response through the co-operation of multiple nonstructural proteins in vitro. Cell Discov. 3, 17006 (2017).

7. Zheng, Y., Liu, Q., Wu, Y., et al. Zika virus elicits inflammation to evade antiviral response by cleaving cGAS via NS1-caspase-1 axis. EMBO J. 37(18), e99347 (2018).