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Discovery of a new antiviral protein isolated Lonomia obliqua analysed by bioinformatics and real-time approaches.

Carmo, Ana Carolina Viegas; Yamasaki, Lilian Hiromi Tomanari; Figueiredo, Cristina Adelaide; da Silva Giovanni, Dalton Nogueira; de Oliveira, Maria Isabel; Dos Santos, Fabiana Cristina Pereira; Curti, Suely Pires; Rahal, Paula; Mendonça, Ronaldo Zucatelli.
Cytotechnology; 67(6): 1011-22, 2015 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-24908059
This study presents a new recombinant protein that acts as a powerful antiviral (rAVLO-recombinant Antiviral protein of Lonomia obliqua). It was able to reduce the replication by 10(6) fold for herpes virus and by 10(4) fold for rubella virus. RT-PCR of viral RNA rAVLO treated infected cells also showed similar rate of inhibition in replication. The analysis of this protein by bioinformatics suggests that this protein is globular, secreted with a signal peptide and has the ability to bind to MHC class I. It was found that there are several protein binding sites with various HLA and a prevalence of α-helices in the N-terminal region (overall classified as a α/ß protein type). BLAST similarity sequence search for corresponding cDNA did not reveal a similar sequence in Genbank, suggesting that it is from a novel protein family. In this study we have observed that this recombinant protein and hemolymph has a potent antiviral action. This protein was produced in a baculovirus/Sf-9 system. Therefore, these analyses suggest that this novel polypeptide is a candidate as a broad spectrum antiviral.