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The Dengue virus serotype 3 pre-membrane protein (prM) is a structural protein essential for the assembly and maturation of infectious virions (Source: UniProt P27915). It functions primarily as a molecular chaperone for the envelope (E) protein, preventing it from undergoing premature conformational changes in the acidic environment of the trans-Golgi network (Source: PubMed 11831707). During the maturation process, prM is cleaved by the host cell protease furin into the "pr" peptide and the mature "M" protein, which triggers a reorganization of the viral surface (Source: PubMed 12191392). In clinical medicine, prM is a key antigenic component of chimeric vaccines like Dengvaxia and Qdenga, designed to elicit protective immunity against all four dengue serotypes (Source: WHO). However, prM is also a major target for non-neutralizing, cross-reactive antibodies that can facilitate antibody-dependent enhancement (ADE), a phenomenon where viral entry into host cells is increased, potentially leading to severe dengue hemorrhagic fever (Source: PubMed 20413591). Consequently, the prM protein is a focal point for both vaccine development and the study of dengue immunopathology.
Induction of neutralizing antibodies and cellular immune responses against the prM and E proteins to prevent viral infection and replication (Source: PubMed 28407470).
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