Isolation, identification and functional profile of excretory-secretory peptides from Onchocerca ochengi
Standard
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, Jahrgang 142, 01.02.2015, S. 156-66.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
Harvard
APA
Vancouver
Bibtex
}
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 -