Zika Virus Membrane 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 Flavivirus membrane proteins, such as ZIKV membrane protein, are translated as a precursor protein, prM, which is translocated to the endoplasmic reticulum (ER).^5,6 In the ER, prM forms heterodimers with the envelope protein that combine into trimeric projections on the surface of the immature virion.⁶ The prM is translocated to the Golgi apparatus for maturation, where the low pH environment induces reorganization of the projections from trimeric to heterodimeric, allowing the precursor portion to be proteolytically cleaved by furin but to stay associated with the envelope protein and shield its fusion loop to prevent premature membrane fusion.^6,7 The mature virus particles are composed of envelope and membrane homodimers, with the membrane proteins irreversibly locking the envelope proteins into the mature structure.⁷ In this way, the membrane protein is involved in viral assembly, maturation, and secretion.^5,6,7 ZIKV membrane protein contains cholesterol-binding motifs that, when mutated, reduce infectivity and viral assembly in vitro.⁸ Cayman’s Zika virus Membrane Protein (strain Zika SPH2015) (recombinant) protein is a disulfide-linked homodimer. The reduced monomer, composed of ZIKV membrane protein (amino acids 216-290) fused to human IgG1 Fc at its C-terminus, consists of 313 amino acids and has a calculated molecular weight of 35.2 kDa.

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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. Pierson, T.C., and Diamond, M.S. Degrees of maturity: The complex structure and biology of flaviviruses. Curr. Opin. Virol. 2(2), 168-175 (2012).

6. Agrelli, A., de Moura, R.R., Crovella, S., et al. ZIKA virus entry mechanisms in human cells. Infect. Genet. Evol. 69, 22-29 (2019).

7. Majowicz, S.A., Narayanan, A., Moustafa, I.M., et al. Zika virus M protein latches and locks the E protein from transitioning to an immature state after prM cleavage. npj Viruses 1(4), (2023).

8. Goellner, S., Enkavi, G., Prasad, V., et al. Zika virus prM protein contains cholesterol binding motifs required for virus entry and assembly. Nat. Commun. 14(1), 7344 (2023).