Clinical-grade DCs were prepared as described elsewhere [21],[22]. presence of ectoM was crucial to the immunogenicity of IV-23 inserted EDIII. The adjuvant capacity of ectoM correlated with its ability to promote the maturation of dendritic cells and the secretion of proinflammatory and antiviral cytokines and chemokines involved in adaptive immunity. The protective efficacy of this vaccine should be analyzed in non-human primates. A combined measlesCdengue vaccine might provide a one-shot approach to immunize children against Prkwnk1 both diseases where they co-exist. Author Summary Dengue is usually a tropical emerging disease that threatens one-third of the world’s populace, mainly children under the age of 15. The development of an affordable pediatric vaccine that could provide long-term protection against all four dengue serotypes remains a global public health priority. To address this challenge, we evaluated a strategy based on the expression of a minimal dengue antigen by live attenuated measles vaccine (MV), one of the most safe, stable, and effective human vaccines. As a proof-of-concept, we constructed a MV vector expressing a secreted dengue antigen composed of the domain name III of the envelope glycoprotein (EDIII), which contains major serotype-specific neutralizing epitopes, fused to the ectodomain of the membrane protein (ectoM) from DV-1, as an adjuvant. This vector induced in mice durable serotype-specific virus-neutralizing antibodies against DV1. The amazing adjuvant capacity of ectoM to EDIII immunogenicity was correlated to its capacity to mature dendritic cells, known to initiate immune response, and to activate the secretion of a panel of cytokines and chemokines determinant for the establishment of specific adaptive immunity. Such strategy might offer pediatric vaccines to immunize children simultaneously against measles and dengue in areas of the world where the diseases co-exist. Introduction Dengue fever is usually a mosquito-borne viral disease that threatens the health of a third of the world’s populace. During the last twenty years, the four serotypes of dengue computer virus spread throughout the tropics due to the presence of the mosquito vector in all urban sites and to the major demographic changes that occurred in these regions. This global re-emergence shows larger epidemics associated with more severe disease [1]. Dengue is usually a major worldwide public health problem with an estimated 100 million annual cases of dengue fever (DF) and 500,000 annual cases of dengue hemorrhagic fever (DHF), the severe form of the disease, resulting in about 25,000 fatal cases, mainly in children under the age of 15. Although global prevention appears the best strategy to control dengue growth, there is still no licensed vaccine available. Dengue viruses (DV) are enveloped, positive-stranded RNA viruses (family). Four antigenically unique viral serotypes exist (DV1-4). The surface of virions is composed of the major envelope glycoprotein (E) and a small membrane protein (M). Very little information is available concerning the IV-23 role of the 75-amino acid long M protein. We previously reported that ectopic expression of the 40-residue intraluminal ectodomain of M (referred hereafter as ectoM) is able to induce apoptosis in mammalian cells, suggesting that M might play an important role in the pathogenicity of flaviviruses [2]. The envelope E protein, which is uncovered on the surface of viral particles, is responsible for virus attachment and virus-specific membrane fusion. Anti-E antibodies inhibit viral binding to cells and neutralize infectivity. A primary DV infection is usually believed to induce life-long immunity to the infecting serotype, while heterologous cross-protection against other serotypes lasts only a few weeks, allowing re-infection by another serotype. A number of clinical IV-23 and experimental data exhibited the implication of the immune response in the pathogenesis of severe forms of dengue, possibly through an antibody-dependant enhancement (ADE) phenomenon based on the cross-reactivity of DV antibodies [3],[4]. The molecular structure of the ectodomain of E glycoprotein has been determined [5]. It is folded in three unique domains I, II and III. The C-terminal immunoglobulin-like domain name III (EDIII) can be independently folded as a core protein through IV-23 a single disulfide bond and contains major serotype-specific neutralizing epitopes [6]. On the opposite, epitopes inducing antibodies that cross-react between.