Dengue virus precursor membrane protein (prM) (prM)

The Dengue virus precursor membrane protein (prM) is a vital structural protein of the Dengue virus (DENV) that facilitates the assembly and maturation of infectious virions [1]. During the viral replication cycle, prM serves as a molecular chaperone for the Envelope (E) protein, preventing it from undergoing premature, acid-induced conformational changes as the virus moves through the host cell's acidic secretory pathway [2][3]. In the trans-Golgi network, the host cell protease furin cleaves the prM protein into a 'pr' peptide and the mature 'M' protein, a process that triggers a dramatic reorganization of the viral surface and renders the particle infectious [4]. Incomplete cleavage often occurs, leading to the secretion of immature or partially mature particles that contain varying amounts of prM [5]. While prM is a target for the host's humoral immune response, antibodies generated against it are frequently cross-reactive across different DENV serotypes but possess poor neutralizing capacity [6]. These anti-prM antibodies are a primary driver of antibody-dependent enhancement (ADE), where they facilitate the entry of the virus into Fc-receptor-bearing cells, significantly increasing the risk of severe disease such as Dengue Hemorrhagic Fever [7]. Consequently, prM is a critical consideration in the development of vaccines and therapeutic antibodies, which must balance the induction of protective immunity against the risk of enhancing infection [8]. Citations: [1] UniProt (P14337); [2] Yu, I. M., et al. (2008) Science; [3] Pierson, T. C., & Diamond, M. S. (2012) Cell Host & Microbe; [4] Stadler, K., et al. (1997) J. Virol.; [5] Rodenhuis-Zybert, I. A., et al. (2010) Nat. Rev. Microbiol.; [6] Dejnirattisai, W., et al. (2010) Science; [7] Beltramello, M., et al. (2010) Cell Host & Microbe; [8] White, L. J., et al. (2023) Vaccines.

Other names

Pre-membrane proteinprM proteinMembrane glycoprotein precursorpMDengue virus prM protein

Induction of neutralizing antibodies, inhibition of viral maturation by blocking furin cleavage, and prevention of viral entry.