Background: At the present time, dengue is one of the most important arboviruses affecting
man, becoming a serious global public health problem, especially in subtropical and tropical
countries, where environmental conditions favor the development and proliferation of the mosquito
Aedes aegypti. Dengue is caused by a type of flavivírus, which is an enveloped virus of spherical
geometry. Nowadays, it is one of the diseases with the highest incidence in Brazil, reaching the
population of all states, regardless of social class. Several papers address the molecular aspects of
infection of human cell by the viruses, which are reviewed in this work.
Conclusion: Analyzing the three-dimensional structures of the fusion peptide of dengue virus protein
E, we observed that the fusion peptide presents a region rich in hydrophobic residues and a
“collar” of charged, polar residues. Probably, this hydrophilic collar plays an important role in the
fusion process between the dengue virus and the cell membrane. In order for this disease to cease
being a serious global public health problem, we must deepen our knowledge about the fusion
process between the dengue virus and the cell membrane through further experimental and, especially,
computational studies to find ways to inhibit the mechanism of virus infection.