| Literature DB >> 19818803 |
C Dias-Lopes1, G Guimarães, L Felicori, P Fernandes, L Emery, E Kalapothakis, C Nguyen, F Molina, C Granier, C Chávez-Olórtegui.
Abstract
Antibodies raised against recombinant Loxosceles intermedia dermonecrotic protein isoform 1 (rLiD1) display neutralizing capacity for the L. intermedia whole venom. We previously found that an immunodominant continuous B-cell epitope, recognized by these antibodies corresponds to a region of the protein known to be involved in the active site. In this study, we extend previous work by preparing a 27-residue synthetic replica of this epitope ((25)NLGANSIETDVSFDDNANPEYTYHGIP(51)) and using it as an immunogen in mice and rabbits. The immunization process induced antibodies that protected mice from a lethal dose of L. intermedia crude venom and rabbits against the dermonecrotic effects of rLiD1. An Ala scan of the epitope indicated that 4 residues, E44, Y45, T46 and Y47, are essential (over 70% decrease in binding upon replacement with alanine) for antibody recognition. The possible mechanisms of neutralization are discussed in light of these findings. Copyright 2009 Elsevier Ltd. All rights reserved.Entities:
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Year: 2009 PMID： 19818803 DOI： 10.1016/j.toxicon.2009.09.019
Source DB: PubMed Journal: Toxicon ISSN： 0041-0101 Impact factor: 3.033