Vol. 11, Issue 2, Part A (2024)

Author(s): Darren Nichole Ocampo, Hans Ezekiel Olorosisimo, Erica Julienne Palting, Lyka Angel Pascual, Edrole Siegfred Ramos, Julienne Aubrey Ruela, Sebastiane Salonga, Andrea Bianca Francesca Sanchez and Mary Rose Lirio

Abstract: AeD7L1 and AeD7L2 are components of the salivary proteins of Aedes aegypti, contributing to the successful blood-feeding of the arthropod. This event is caused by inhibiting the hemostatic response of the host by acting as scavengers for biogenic amines such as serotonin, inducing vasodilation and increased vascular permeability that leads to excessive bleeding. In silico methods have been utilized to establish the similarities and distinct differences of these proteins, as well as the determination of their structures in correlation with their binding mechanisms through the use of homology modeling. AeD7L1 has a higher antigenicity score, but AeD7L2 gained the ability to bind to a thromboxane analog due to a difference in the amino acid composition. Their structures also showed areas responsible for their binding mechanisms and protein interactions. Recognizing these functional properties may aid in drug developments, protein modifications, and others that may alleviate the burden of arthropod-borne viruses.

DOI: 10.22271/23487941.2024.v11.i2a.766