Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi

Raphael Eberle; Norbert W Brattig; Maria Trusch; Hartmut Schlüter; Mbunkah Daniel Achukwi; Albert Eisenbarth; Alfons Renz; Eva Liebau; Markus Perbandt; Christian Betzel

doi:10.1016/j.actatropica.2014.11.015

Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi

Acta Trop. 2015 Feb:142:156-66. doi: 10.1016/j.actatropica.2014.11.015. Epub 2014 Dec 3.

Authors

Affiliations

¹ Institute of Biochemistry and Molecular Biology, University of Hamburg, Laboratory of Structural Biology of Infection and Inflammation, c/o DESY, Notkestr. 85, Build. 22a, 22603 Hamburg, Germany.
² Bernhard Nocht Institute for Tropical Medicine, 20359 Hamburg, Germany.
³ Institute of Organic Chemistry, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.
⁴ Institute of Clinical Chemistry, University Medical Center Hamburg-Eppendorf (UKE), 20246 Hamburg, Germany.
⁵ Institute of Agricultural Research for Development, Veterinary Research Laboratory, Wakwa Centre, PO Box 65, Ngaoundéré, Cameroon.
⁶ Institute of Evolution and Ecology, University of Tübingen, Auf der Morgenstelle 28, 72076 Tübingen, Germany.
⁷ Institute of Animal Physiology, University of Münster, Schlossplatz 8, 48143 Münster, Germany.
⁸ Institute of Biochemistry and Molecular Biology, University of Hamburg, Laboratory of Structural Biology of Infection and Inflammation, c/o DESY, Notkestr. 85, Build. 22a, 22603 Hamburg, Germany; Institute of Medical Microbiology, Virology and Hygiene, University Medical Center Hamburg-Eppendorf (UKE), 20246 Hamburg, Germany.
⁹ Institute of Biochemistry and Molecular Biology, University of Hamburg, Laboratory of Structural Biology of Infection and Inflammation, c/o DESY, Notkestr. 85, Build. 22a, 22603 Hamburg, Germany. Electronic address: Christian.Betzel@uni-hamburg.de.

PMID: 25479441
DOI: 10.1016/j.actatropica.2014.11.015

Abstract

Parasitic helminths excrete or secrete a variety of functional molecules into the internal milieu of their mammalian hosts and arthropod vectors which reveal distinct immunomodulatory and other biological activities. We identified and initially characterized the low molecular weight peptide composition of the secretome from the filarial parasite Onchocerca ochengi. A total of 85 peptides were purified by liquid chromatography and further characterized by mass spectrometry. 72 of these peptides were derived from already described Onchocerca proteins and 13 peptide sequences are included in the sequence of uncharacterized proteins. Three peptides, similar to host defense peptides, revealed antibacterial activity. The present analysis confirms the putative involvement of low molecular weight compounds in the parasite-host cross-talk.

Keywords: Antibacterial activity; Excretory–secretory products; Filaria; Functional peptides; Onchocerca.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Cross Reactions
Female
Helminth Proteins / metabolism*
Onchocerca / physiology*
Onchocerciasis / prevention & control
Onchocerciasis / transmission*
Simuliidae / parasitology

Substances

Helminth Proteins