TY - JOUR
T1 - Binding of Salmonella typhimurium lipopolysaccharides to rat high-density lipoproteins
AU - Munford, R. S.
AU - Hall, C. L.
AU - Dietschy, J. M.
PY - 1981
Y1 - 1981
N2 - These studies were undertaken to investigate the binding of gram-negative bacterial lipopolysaccharides (LPS) to high-density lipoproteins (HDL) of rat plasma. Purified Salmonella typhimurium LPS, intrinsically labeled with [3H]-galactose, bound rapidly in vitro to isolated rat HDL. Maximal binding of LPS to HDL occurred when LPS and HDL were incubated with lipoprotein-free plasma (p < 1.21 g/ml). Since LPS, when purified, from large aggregates, we tested the hypothesis that disaggregation of LPS enhances LPS-HDL binding. We found that calcium chloride (1 mM), an agent which prevents LPS disaggregation, inhibited binding of LPS to HDL by interfering with the modification of LPS by lipoprotein-free plasma. Conversely, sodium deoxycholate (0.15 g/dl), which disaggregates LPS, greatly increased binding of LPS to HDL in the absence of lipoprotein-free plasma. Analysis of labeled LPS by sodium deodecyl sulfate-polyacrylamide gel electrophoresis showed only minor differences in the sizes of LPS molecules before and after binding to HDL, suggesting that chemical modification of LPS is not required for binding. The results provide evidence that disaggregation increases the binding of LPS to HDL.
AB - These studies were undertaken to investigate the binding of gram-negative bacterial lipopolysaccharides (LPS) to high-density lipoproteins (HDL) of rat plasma. Purified Salmonella typhimurium LPS, intrinsically labeled with [3H]-galactose, bound rapidly in vitro to isolated rat HDL. Maximal binding of LPS to HDL occurred when LPS and HDL were incubated with lipoprotein-free plasma (p < 1.21 g/ml). Since LPS, when purified, from large aggregates, we tested the hypothesis that disaggregation of LPS enhances LPS-HDL binding. We found that calcium chloride (1 mM), an agent which prevents LPS disaggregation, inhibited binding of LPS to HDL by interfering with the modification of LPS by lipoprotein-free plasma. Conversely, sodium deoxycholate (0.15 g/dl), which disaggregates LPS, greatly increased binding of LPS to HDL in the absence of lipoprotein-free plasma. Analysis of labeled LPS by sodium deodecyl sulfate-polyacrylamide gel electrophoresis showed only minor differences in the sizes of LPS molecules before and after binding to HDL, suggesting that chemical modification of LPS is not required for binding. The results provide evidence that disaggregation increases the binding of LPS to HDL.
UR - http://www.scopus.com/inward/record.url?scp=0019844358&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0019844358&partnerID=8YFLogxK
U2 - 10.1128/iai.34.3.835-843.1981
DO - 10.1128/iai.34.3.835-843.1981
M3 - Article
C2 - 7037642
AN - SCOPUS:0019844358
SN - 0019-9567
VL - 34
SP - 835
EP - 843
JO - Infection and immunity
JF - Infection and immunity
IS - 3
ER -