Back to Search Start Over

Antiparasitic effects induced by polyclonal IgY antibodies anti-phospholipase A 2 from Bothrops pauloensis venom.

Authors :
Borges IP
Silva MF
Santiago FM
de Faria LS
Júnior ÁF
da Silva RJ
Costa MS
de Freitas V
Yoneyama KAG
Ferro EAV
Lopes DS
Rodrigues RS
de Melo Rodrigues V
Source :
International journal of biological macromolecules [Int J Biol Macromol] 2018 Jun; Vol. 112, pp. 333-342. Date of Electronic Publication: 2018 Jan 31.
Publication Year :
2018

Abstract

Activities of phospholipases (PLAs) have been linked to pathogenesis in various microorganisms, and implicated in cell invasion and so the interest in these enzymes as potential targets that could contribute to the control of parasite survival and proliferation. Chicken eggs immunized with BnSP-7, a Lys49 phospholipase A <subscript>2</subscript> (PLA <subscript>2</subscript> ) homologue from Bothrops pauloensis snake venom, represent an excellent source of polyclonal antibodies with potential inhibitory activity on parasite PLA <subscript>s.</subscript> Herein, we report the production, characterization and anti-parasitic effect of IgY antibodies from egg yolks of hens immunized with BnSP-7. Produced antibodies presented increasing avidity and affinity for antigenic toxin epitopes throughout immunization, attaining a plateau after 4weeks. Pooled egg yolks-purified anti-BnSP-7 IgY antibodies were able to specifically recognize different PLA <subscript>2</subscript> s from Bothrops pauloensis and Bothrops jararacussu venom. Antibodies also neutralized BnSP-7 cytotoxic activity in C2C12 cells. Also, the antibodies recognized targets in Leishmania (Leishmania) amazonensis and Toxoplasma gondii extracts by ELISA and immunofluorescence assays. Anti-BnSP-7 IgY antibodies were cytotoxic to T. gondii tachyzoite and L. (L.) amazonensis promastigotes, and were able to decrease proliferation of both parasites treated before infection. These data suggest that the anti-BnSP-7 IgY is an important tool for discovering new parasite targets and blocking parasitic effects.<br /> (Copyright © 2018 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1879-0003
Volume :
112
Database :
MEDLINE
Journal :
International journal of biological macromolecules
Publication Type :
Academic Journal
Accession number :
29391226
Full Text :
https://doi.org/10.1016/j.ijbiomac.2018.01.178