Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharide
There are several human serum proteins for which no clear role is yet known. Among these is the abundant serum protein beta2-glycoprotein-I (β2GPI), which is known to bind to negatively charged phospholipids as well as to bacterial lipopolysaccharides (LPS), and was therefore proposed to play a role...
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| Format: | Article |
| Language: | English |
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Wiley
2014-01-01
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| Series: | FEBS Open Bio |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211546314000448 |
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| author | Anna Gries Ruth Prassl Satoshi Fukuoka Manfred Rössle Yani Kaconis Lena Heinbockel Thomas Gutsmann Klaus Brandenburg |
| author_facet | Anna Gries Ruth Prassl Satoshi Fukuoka Manfred Rössle Yani Kaconis Lena Heinbockel Thomas Gutsmann Klaus Brandenburg |
| author_sort | Anna Gries |
| collection | DOAJ |
| description | There are several human serum proteins for which no clear role is yet known. Among these is the abundant serum protein beta2-glycoprotein-I (β2GPI), which is known to bind to negatively charged phospholipids as well as to bacterial lipopolysaccharides (LPS), and was therefore proposed to play a role in the immune response. To understand the details of these interactions, a biophysical analysis of the binding of β2GPI to LPS and phosphatidylserine (PS) was performed. The data indicate only a moderate tendency of the protein (1) to influence the LPS-induced cytokine production in vitro, (2) to react exothermally with LPS in a non-saturable way, and (3) to change its local microenvironment upon LPS association. Additionally, we found that the protein binds more strongly to phosphatidylserine (PS) than to LPS. Furthermore, β2GPI converts the LPS bilayer aggregates into a stronger multilamellar form, and reduces the fluidity of the hydrocarbon moiety of LPS due to a rigidification of the acyl chains. From these data it can be concluded that β2GPI plays a role as an immune-modulating agent, but there is much less evidence for a role in immune defense against bacterial toxins such as LPS. |
| first_indexed | 2024-12-10T23:36:16Z |
| format | Article |
| id | doaj.art-4c98b3d9ad404a9dbb8e35e297c66aa6 |
| institution | Directory Open Access Journal |
| issn | 2211-5463 |
| language | English |
| last_indexed | 2024-12-10T23:36:16Z |
| publishDate | 2014-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | FEBS Open Bio |
| spelling | doaj.art-4c98b3d9ad404a9dbb8e35e297c66aa62022-12-22T01:29:10ZengWileyFEBS Open Bio2211-54632014-01-014C43244010.1016/j.fob.2014.04.008Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharideAnna Gries0Ruth Prassl1Satoshi Fukuoka2Manfred Rössle3Yani Kaconis4Lena Heinbockel5Thomas Gutsmann6Klaus Brandenburg7Institute of Physiology, Medical University of Graz, Harrachgasse 21/V, 8010 Graz, AustriaInstitute of Biophysics, Medical University of Graz, Schmiedlstr. 6, 8042 Graz, AustriaNational Institute of Advanced Industrial Science and Technology AIST, Takamatsu, JapanEuropean Molecular Biology Laboratory, c/o DESY, D-22603 Hamburg, GermanyForschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Parkallee 10, D-23845 Borstel, GermanyForschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Parkallee 10, D-23845 Borstel, GermanyForschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Parkallee 10, D-23845 Borstel, GermanyForschungszentrum Borstel, Leibniz-Zentrum für Medizin und Biowissenschaften, Parkallee 10, D-23845 Borstel, GermanyThere are several human serum proteins for which no clear role is yet known. Among these is the abundant serum protein beta2-glycoprotein-I (β2GPI), which is known to bind to negatively charged phospholipids as well as to bacterial lipopolysaccharides (LPS), and was therefore proposed to play a role in the immune response. To understand the details of these interactions, a biophysical analysis of the binding of β2GPI to LPS and phosphatidylserine (PS) was performed. The data indicate only a moderate tendency of the protein (1) to influence the LPS-induced cytokine production in vitro, (2) to react exothermally with LPS in a non-saturable way, and (3) to change its local microenvironment upon LPS association. Additionally, we found that the protein binds more strongly to phosphatidylserine (PS) than to LPS. Furthermore, β2GPI converts the LPS bilayer aggregates into a stronger multilamellar form, and reduces the fluidity of the hydrocarbon moiety of LPS due to a rigidification of the acyl chains. From these data it can be concluded that β2GPI plays a role as an immune-modulating agent, but there is much less evidence for a role in immune defense against bacterial toxins such as LPS.http://www.sciencedirect.com/science/article/pii/S2211546314000448Human glycoprotein β2GPILipopolysaccharideCytokine productionImmune modulationLAL test |
| spellingShingle | Anna Gries Ruth Prassl Satoshi Fukuoka Manfred Rössle Yani Kaconis Lena Heinbockel Thomas Gutsmann Klaus Brandenburg Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharide FEBS Open Bio Human glycoprotein β2GPI Lipopolysaccharide Cytokine production Immune modulation LAL test |
| title | Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharide |
| title_full | Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharide |
| title_fullStr | Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharide |
| title_full_unstemmed | Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharide |
| title_short | Biophysical analysis of the interaction of the serum protein human β2GPI with bacterial lipopolysaccharide |
| title_sort | biophysical analysis of the interaction of the serum protein human β2gpi with bacterial lipopolysaccharide |
| topic | Human glycoprotein β2GPI Lipopolysaccharide Cytokine production Immune modulation LAL test |
| url | http://www.sciencedirect.com/science/article/pii/S2211546314000448 |
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