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https://hdl.handle.net/2440/23886
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Type: | Journal article |
Title: | Recognition and inactivation of LPS by lipophorin particles |
Author: | Ma, G. Hay, D. Li, D. Asgari, S. Schmidt, O. |
Citation: | Developmental and Comparative Immunology, 2006; 30(7):619-626 |
Publisher: | Pergamon-Elsevier Science Ltd |
Issue Date: | 2006 |
ISSN: | 0145-305X 1879-0089 |
Statement of Responsibility: | Gang Ma, Douglas Hay, Dongmei Li, Sassan Asgari and Otto Schmidt |
Abstract: | Lipophorin is the major lipid carrier in insects, but various observations indicate that lipophorin is also involved in immune reactions. To examine a possible role of lipophorin in defence reactions, we mixed hemolymph plasma from Galleria mellonella with LPS and noticed that lipophorin forms detergent-insoluble aggregates, while most other plasma proteins are not affected. Lipophorin particles isolated by low-density gradient centrifugation retained LPS-induced aggregation properties, which suggested to us that these immune-reactive particles are able to recognise LPS and respond by forming insoluble aggregates. Antibodies against LPS-binding proteins, such as immulectin-2 and β-1,3-glucan binding protein, cross-reacted with proteins associated with purified lipophorin particles. To examine whether LPS-mediated aggregates inactivate LPS, we added LPS–lipophorin mixtures to purified lipophorin particles and monitored aggregate formation. Under these conditions lipophorin did not form insoluble aggregates, which indicates that lipophorin particles sequester LPS into non-toxic aggregates. |
Keywords: | lipopolysaccharide lipophorin coagulation LPS binding protein Galleria mellonella |
DOI: | 10.1016/j.dci.2005.09.003 |
Description (link): | http://www.elsevier.com/wps/find/journaldescription.cws_home/275/description#description |
Published version: | http://dx.doi.org/10.1016/j.dci.2005.09.003 |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest 2 |
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