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Recognition and inactivation of LPS by lipophorin particles.

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 beta-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.

journal_name

Dev Comp Immunol

journal_title

Developmental and comparative immunology

authors

Ma G,Hay D,Li D,Asgari S,Schmidt O

doi

10.1016/j.dci.2005.09.003

keywords:

subject

Has Abstract

pub_date

2006-01-01 00:00:00

pages

619-26

issue

7

eissn

0145-305X

issn

1879-0089

pii

S0145-305X(05)00187-4

journal_volume

30

pub_type

杂志文章

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