Using structural analysis to generate parasite-selective monoclonal antibodies.

Protein Science : a Publication of the Protein Society
Michael KronLeslie A Kuhn

Abstract

Diagnosis of eukaryotic parasitic infection using antibody-based tests such as ELISAs (enzyme-linked immunosorbent assays) is often problematic because of the need to differentiate between homologous host and pathogen proteins and to ensure that antibodies raised against a peptide will also bind to the peptide in the context of its three-dimensional protein structure. Filariasis caused by the nematode, Brugia malayi, is an important worldwide tropical disease in which parasites disappear from the bloodstream during daylight hours, thus hampering standard microscopic diagnostic methods. To address this problem, a structural approach was used to develop monoclonal antibodies (mAbs) that detect asparaginyl-tRNA synthetase (AsnRS) secreted from B. malayi. B. malayi and human AsnRS amino acid sequences were aligned to identify regions that are relatively unconserved, and a 1.9 A crystallographic structure of B. malayi AsnRS was used to identify peptidyl regions that are surface accessible and available for antibody binding. Sequery and SSA (Superpositional Structural Analysis) software was used to analyze which of these peptides was most likely to maintain its native conformation as a synthetic peptide, and its predicted helical str...Continue Reading

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Citations

Nov 6, 2010·Hybridoma·ShiTing LiJinShan Zhang
May 12, 2009·Molekuliarnaia biologiia·M G Safro, N A Moor
Dec 18, 2009·Journal of Molecular Recognition : JMR·Rebecca L Rich, David G Myszka

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