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

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Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi. / Eberle, Raphael; Brattig, Norbert W; Trusch, Maria; Schlüter, Hartmut; Achukwi, Mbunkah Daniel; Eisenbarth, Albert; Renz, Alfons; Liebau, Eva; Perbandt, Markus; Betzel, Christian.

In: ACTA TROP, Vol. 142, 01.02.2015, p. 156-66.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Eberle, R, Brattig, NW, Trusch, M, Schlüter, H, Achukwi, MD, Eisenbarth, A, Renz, A, Liebau, E, Perbandt, M & Betzel, C 2015, 'Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi', ACTA TROP, vol. 142, pp. 156-66. https://doi.org/10.1016/j.actatropica.2014.11.015

APA

Eberle, R., Brattig, N. W., Trusch, M., Schlüter, H., Achukwi, M. D., Eisenbarth, A., Renz, A., Liebau, E., Perbandt, M., & Betzel, C. (2015). Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi. ACTA TROP, 142, 156-66. https://doi.org/10.1016/j.actatropica.2014.11.015

Vancouver

Eberle R, Brattig NW, Trusch M, Schlüter H, Achukwi MD, Eisenbarth A et al. Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi. ACTA TROP. 2015 Feb 1;142:156-66. https://doi.org/10.1016/j.actatropica.2014.11.015

Bibtex

@article{e959d5c7c1244184b8ebdf30b8082d0e,
title = "Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi",
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.",
author = "Raphael Eberle and Brattig, {Norbert W} and Maria Trusch and Hartmut Schl{\"u}ter and Achukwi, {Mbunkah Daniel} and Albert Eisenbarth and Alfons Renz and Eva Liebau and Markus Perbandt and Christian Betzel",
note = "Copyright {\textcopyright} 2014 Elsevier B.V. All rights reserved.",
year = "2015",
month = feb,
day = "1",
doi = "10.1016/j.actatropica.2014.11.015",
language = "English",
volume = "142",
pages = "156--66",
journal = "ACTA TROP",
issn = "0001-706X",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi

AU - Eberle, Raphael

AU - Brattig, Norbert W

AU - Trusch, Maria

AU - Schlüter, Hartmut

AU - Achukwi, Mbunkah Daniel

AU - Eisenbarth, Albert

AU - Renz, Alfons

AU - Liebau, Eva

AU - Perbandt, Markus

AU - Betzel, Christian

N1 - Copyright © 2014 Elsevier B.V. All rights reserved.

PY - 2015/2/1

Y1 - 2015/2/1

N2 - 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.

AB - 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.

U2 - 10.1016/j.actatropica.2014.11.015

DO - 10.1016/j.actatropica.2014.11.015

M3 - SCORING: Journal article

C2 - 25479441

VL - 142

SP - 156

EP - 166

JO - ACTA TROP

JF - ACTA TROP

SN - 0001-706X

ER -