Resumo

Antiviral proteins are proteins that are induced by human or animal cells to interfere with viral replication. These proteins are isolated to inhibit the virus from replicating in a host's cells and stop it from spreading to other cells. The control of viruses is of great interest to the public health area. Several studies have been conducted that show the presence of pharmacologically active substances in the hemolymph of insects. Recently we have demonstrated the existence of a potent antiviral in the hemolymph of Lonomia obliqua caterpillar. This protein was able to reduce at 106 times the replication of herpes virus and in 10,000 fold the rubella virus. Assays using RT-PCR to determine viral RNA present in no treated and rAVLO treated infected cells also showed a reduction in the same scale. The analysis of this protein by bioinformatics suggests that this protein is globular, secreted with a signal peptide which is cleaved between amino acids 16 and 17. The studies also allows us to infer that this antiviral protein has the ability to bind to MHC class I. It was found that there are several protein binding sites on the weak and strong bases with various HLA. The bioinformatic analysis also shows a strong presence of α-helices in the N-terminal region and allowed to classify the antiviral protein as α/β type of structure, as we detected the presence of more than 30% α-helix and 20 % of β-sheet found separately along the protein chain. In the BLAST sequence analysis of cDNA antiviral protein, no sequence similarity was found in Genbank, suggesting that it is from a novel protein family. It can be inferred by an analysis of this region that the possible antigenicity region would be between the 70-110 amino acids, showing high accessibility. This high antigenic region on the surface, can be a possible region to interaction with other proteins.