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PMID: 15241548,4378413 The observation that the lipid A region of LPS interacts directly with plasma factor XII (Hageman factor) suggests that this factor contains an LPS binding site. PMID: 15241548 This interaction with LPS activates factor XII, and triggers the intrinsic coagulation pathway.

PMID: 15241548 Another plasma protein in association with apo A1 is lipopolysaccharide-binding protein (LBP)

PMID: 15241548,12417309 A second function of LBP is to increase the interaction of LPS with soluble CD14 (sCD14) by forming a stable trimolecular complex PMID: 15241548,7510680 This requires an interaction between LBP and CD14 which is mediated by the C-terminal half of LBP PMID: 15241548,11500507 Unlike the membrane form, which requires LBP, sCD14 can directly bind LPS with a dissociation constant of 74 nM

PMID: 15241548,11500507 Unlike the membrane form, which requires LBP, sCD14 can directly bind LPS with a dissociation constant of 74 nM PMID: 15241548,12417309 A second function of LBP is to increase the interaction of LPS with soluble CD14 (sCD14) by forming a stable trimolecular complex

PMID: 15241548,11500507 Unlike the membrane form, which requires LBP, sCD14 can directly bind LPS with a dissociation constant of 74 nM

PMID: 15241548,7534294 Lipoteichoic acid and phosphatidyl inositol also bind to sCD14

PMID: 15241548,7534294 Lipoteichoic acid and phosphatidyl inositol also bind to sCD14

PMID: 15241548 In contrast, cysteine residues such as Cys37, Cys95, Cys105 and Cys148 are important for forming a cell surface TLR4- MD-2 complex, in which MD-2 is docked to the extracellular leucine-rich repeats of TLR4.

PMID: 15241548,11500507 It has been shown that MD-2 can directly bind LPS (Kd = 65 nM)

PMID: 15241548,11521060 Concerning B lymphocytes, in addition to TLR4-MD-2, another cell surface complex, RP105-MD-1, is also involved in the recognition of LPS

PMID: 15241548,11521060 Concerning B lymphocytes, in addition to TLR4-MD-2, another cell surface complex, RP105-MD-1, is also involved in the recognition of LPS

PMID: 15241548 This LPS-binding capacity could be due to PGRP-LCa, because PGRP-LCx is required for activation by both peptidoglycan and LPS, whereas PGRP-LCa is required only for activation by LPS.

PMID: 15241548 This LPS-binding capacity could be due to PGRP-LCa, because PGRP-LCx is required for activation by both peptidoglycan and LPS, whereas PGRP-LCa is required only for activation by LPS.

PMID: 15241548 This LPS-binding capacity could be due to PGRP-LCa, because PGRP-LCx is required for activation by both peptidoglycan and LPS, whereas PGRP-LCa is required only for activation by LPS.

PMID: 15241548,11276205 Triantafilou et al. identified heat shock proteins 70 and 90 (HSP70 and HSP90), chemokine receptor 4 (CXCR4) and growth differentiation factor 5 (GDF-5) as four new molecules on the cell surface that bind LPS and are involved in LPS-induced signaling

PMID: 15241548,11276205 Triantafilou et al. identified heat shock proteins 70 and 90 (HSP70 and HSP90), chemokine receptor 4 (CXCR4) and growth differentiation factor 5 (GDF-5) as four new molecules on the cell surface that bind LPS and are involved in LPS-induced signaling

PMID: 15241548,11276205 Triantafilou et al. identified heat shock proteins 70 and 90 (HSP70 and HSP90), chemokine receptor 4 (CXCR4) and growth differentiation factor 5 (GDF-5) as four new molecules on the cell surface that bind LPS and are involved in LPS-induced signaling

PMID: 15241548,11276205 Triantafilou et al. identified heat shock proteins 70 and 90 (HSP70 and HSP90), chemokine receptor 4 (CXCR4) and growth differentiation factor 5 (GDF-5) as four new molecules on the cell surface that bind LPS and are involved in LPS-induced signaling

PMID: 15241548,2462607 A specific LPS binding motif was also shown in the CD11b chain of one of the three adhesion molecules (CR3) belonging to the b-integrin family

indirect

PMID: 15241548,9200483 CR3 can mediate LPS-induced activation of NF-kB in transfected CHO cells, although its cytosolic domain is not required for signaling

PMID: 15241548 Another membrane molecule involved in LPS recognition and signaling is the decay accelerating factor (DAF, CD55).

PMID: 15241548,8660298 For example, it has been reported that in human neutrophils, L-selectin (CD62L) can bind LPS

PMID;15241548 It has been established that the two hydrophilic surfactant proteins, SP-A and SP-D, bind phospholipids and LPS.

PMID: 15241548,9541593 In human platelets, LPS ligation occurs via another selectin, P-selectin

PMID;15241548 It has been established that the two hydrophilic surfactant proteins, SP-A and SP-D, bind phospholipids and LPS.

PMID: 15241548,11557581 In contrast, the authors reported that SP-C binds efficiently to LPS

PMID: 15241548,12496149 We also demonstrated that CD14 shares with LPS the same binding region on SP-C, and that the interaction with SPC modifies the conformation of CD14, allowing it to bind LPS more efficiently

PMID: 15241548,12496149 We also demonstrated that CD14 shares with LPS the same binding region on SP-C, and that the interaction with SPC modifies the conformation of CD14, allowing it to bind LPS more efficiently

PMID;15241548 It has been established that the two hydrophilic surfactant proteins, SP-A and SP-D, bind phospholipids and LPS.

PMID;15241548 It has been established that the two hydrophilic surfactant proteins, SP-A and SP-D, bind phospholipids and LPS.

PMID: 15241548,8569759,11330824,11820943,1536865,9720039 In insects, we can mention cecropin in Drosophila hemolymph, sarcotoxin IA from flesh fly, melittin in bee venom and attacin in silkmoth, which all bind LPS.

PMID: 15241548,8569759,11330824,11820943,1536865,9720039 In insects, we can mention cecropin in Drosophila hemolymph, sarcotoxin IA from flesh fly, melittin in bee venom and attacin in silkmoth, which all bind LPS.

PMID: 15241548,8569759,11330824,11820943,1536865,9720039 In insects, we can mention cecropin in Drosophila hemolymph, sarcotoxin IA from flesh fly, melittin in bee venom and attacin in silkmoth, which all bind LPS.

PMID: 15241548,8569759,11330824,11820943,1536865,9720039 In insects, we can mention cecropin in Drosophila hemolymph, sarcotoxin IA from flesh fly, melittin in bee venom and attacin in silkmoth, which all bind LPS.

PMID:15241548,7540596 The polysaccharide portion of LPSs is recognized by components of the alternative pathway and, for some mannose-containing O-chains, by the mannan-binding protein of the lectin pathway

PMID: 15241548,351060,2649081,7372350,12390351 In addition, the lipid A portion of LPSs activates the classical pathway [66] via interaction with C1q and C3.

PMID: 15241548,351060,2649081,7372350,12390351 In addition, the lipid A portion of LPSs activates the classical pathway [66] via interaction with C1q and C3.

PMID: 15241548,7528733 LPS also binds to all of the major plasma lipoproteins: HDLs, low-density lipoproteins (LDLs), very low density lipoproteins (VLDLs) and chylomicrons

PMID: 15241548,7528733 LPS also binds to all of the major plasma lipoproteins: HDLs, low-density lipoproteins (LDLs), very low density lipoproteins (VLDLs) and chylomicrons

PMID: 15241548,7528733 LPS also binds to all of the major plasma lipoproteins: HDLs, low-density lipoproteins (LDLs), very low density lipoproteins (VLDLs) and chylomicrons

PMID: 15241548,7528733 LPS also binds to all of the major plasma lipoproteins: HDLs, low-density lipoproteins (LDLs), very low density lipoproteins (VLDLs) and chylomicrons

PMID: 15241548,2463827,9153287 At least one type of protein constituent of lipoproteins, the apolipoprotein apoE, contains a heparin-binding sequence [and can directly bind LPS, possibly by its exposed hydrophilic domain involving arginine residues

PMID: 15241548,1547784 It (SAP) is a multispecific protein which binds heparin, various 3-sulfated carbohydrates, mannose- 6-phosphate and LPS

PMID: 15241548,1547784 It (SAP) is a multispecific protein which binds heparin, various 3-sulfated carbohydrates, mannose- 6-phosphate and LPS

PMID: 15241548,1547784 It (SAP) is a multispecific protein which binds heparin, various 3-sulfated carbohydrates, mannose- 6-phosphate and LPS

PMID: 15241548,1547784 It (SAP) is a multispecific protein which binds heparin, various 3-sulfated carbohydrates, mannose- 6-phosphate and LPS

PMID: 15241548,7831356 Hb is an LPS binding protein

PMID: 15241548 It (BPI) has both heparin- and LPS-binding capacity, and shares ~44% sequence homology with LBP

PMID: 15241548 It (BPI) has both heparin- and LPS-binding capacity, and shares ~44% sequence homology with LBP

PMID: 15241548,9359845,11509640 Lactoferrin (Lf) is a multispecific protein which binds iron, heparin, proteoglycan, DNA, oligodeoxyncleotides and LPS

PMID: 15241548,9359845,11509640 Lactoferrin (Lf) is a multispecific protein which binds iron, heparin, proteoglycan, DNA, oligodeoxyncleotides and LPS

PMID: 15241548,9359845,11509640 Lactoferrin (Lf) is a multispecific protein which binds iron, heparin, proteoglycan, DNA, oligodeoxyncleotides and LPS

PMID: 15241548,9359845,11509640 Lactoferrin (Lf) is a multispecific protein which binds iron, heparin, proteoglycan, DNA, oligodeoxyncleotides and LPS

PMID: 15241548,9359845,11509640 Lactoferrin (Lf) is a multispecific protein which binds iron, heparin, proteoglycan, DNA, oligodeoxyncleotides and LPS

PMID: 15241548,9359845,11509640 Lactoferrin (Lf) is a multispecific protein which binds iron, heparin, proteoglycan, DNA, oligodeoxyncleotides and LPS

PMID: 15241548 Once released from neutrophils, HBP binds to endothelial cell surface proteoglycans, such as syndecans and glypican, and contributes to the progression of inflammation

PMID: 15241548 Once released from neutrophils, HBP binds to endothelial cell surface proteoglycans, such as syndecans and glypican, and contributes to the progression of inflammation

PMID: 15241548,9199453 A synthetic peptide corresponding to residues 20–44 has been shown to possess the capacity to bind lipid A

indirect

indirect

PMID: 15241548 Like LBP, HBP enhances LPS-induced tumor necrosis factor-alpha (TNF-a) release by monocytes. PMID: 15241548 Furthermore, H2A inhibits the ligation of LPS to macrophages, and the LPS-induced production of TNF-a and nitric oxide.

PMID: 15241548 Another group of neutrophil cationic proteins able to bind LPS involves proline-rich peptides. Indolicidin, Bac5 and prophenin represent three examples of such peptides

PMID: 15241548 Another group of neutrophil cationic proteins able to bind LPS involves proline-rich peptides. Indolicidin, Bac5 and prophenin represent three examples of such peptides

PMID: 15241548 Another group of neutrophil cationic proteins able to bind LPS involves proline-rich peptides. Indolicidin, Bac5 and prophenin represent three examples of such peptides

PMID: 15241548,12928411 Another related component, the C1 inhibitor (a serine inhibitor of the classical complement pathway and of factor XII of the coagulation system), also interacts with LPS via its N-terminal mucin domain

PMID: 15241548 Lysozyme, a major cationic protein of leukocyte polymorphonuclear granules, was also found to bind LPS.

PMID: 15241548,9593692,10456890 In addition, SLPI was found to interact directly with different sulfated polysaccharides (dermatan, heparan and dextran sulfates), and with LPS

PMID: 15241548,9593692,10456890 In addition, SLPI was found to interact directly with different sulfated polysaccharides (dermatan, heparan and dextran sulfates), and with LPS

PMID: 15241548,9593692,10456890 In addition, SLPI was found to interact directly with different sulfated polysaccharides (dermatan, heparan and dextran sulfates), and with LPS

PMID: 15241548,9593692,10456890 In addition, SLPI was found to interact directly with different sulfated polysaccharides (dermatan, heparan and dextran sulfates), and with LPS

PMID: 15241548,1663059 In saliva, histatins are small histidin-rich peptides (HRPs) with antimicrobial activity, secreted by epithelial cells of parotid and submandibular glands. They can bind LPS and neutralize its effects on monocytes

PMID: 15241548,7730641 Human a-defensins (HNP-1 to HNP-4) have been shown to interact with LPS, although less efficiently than BPI

PMID:15241548,9736536 The human cathelicidin hCAP18 carries a 37-residuea-helical peptide termed LL-37, with antimicrobial and LPS-binding activity

PMID: 15241548 SMAP-29 contains two LPS binding sites: the highestaffinity site (RGLRRLGR) is located in the N-terminal region, and the lowest-affinity site (VLRIIRIA) is in the C-terminal region.

PMID: 15241548,11500507 Unlike the membrane form, which requires LBP, sCD14 can directly bind LPS with a dissociation constant of 74 nM PMID: 15241548,12417309 A second function of LBP is to increase the interaction of LPS with soluble CD14 (sCD14) by forming a stable trimolecular complex

PMID: 15241548,11418686 After binding to the cell surface, LPS was found to be internalized and detectable in the cytoplasm of macrophages within seconds

PMID: 15241548, 11489964 It has been shown by Denlinger et al. that the C-terminal region of P2X7, which is located inside the cell after the second transmembrane domain, contains a motif (residues 573–590) which shares strong amino acid homology with the LPS binding sites of LBP and BPI. Furthermore, peptides derived from this sequence were shown to bind LPS in vitro, and to neutralize some LPS responses in macrophages.

PMID: 15241548,11717582 Moesin, a cytoskeletal linker actin-binding protein associated with the cytoplasmic side of plasma membranes, can also bind LPS

PMID: 15241548,1573273 Moesin, a cytoskeletal linker actin-binding protein associated with the cytoplasmic side of plasma membranes, can also bind LPS , and at the cytoskeleton level, tubulin can do so as well

PMID: 15241548,12874245 It has also been suggested that LPS has the capacity to bind to selected subunits (C2 and N3) of the macrophage proteasome, with further activation of the proteasome chymotrypsin- like activity

PMID: 15241548,12667084 Another new class of LPS-binding molecules recently discovered by the present author’s group is that of histones . The authors found that histones H1, H2A, H2B, H3 and H4 can all bind LPS.

PMID: 15241548,12667084 Another new class of LPS-binding molecules recently discovered by the present author’s group is that of histones . The authors found that histones H1, H2A, H2B, H3 and H4 can all bind LPS.

PMID: 15241548,12667084 Another new class of LPS-binding molecules recently discovered by the present author’s group is that of histones . The authors found that histones H1, H2A, H2B, H3 and H4 can all bind LPS.

PMID: 15241548,12667084 Another new class of LPS-binding molecules recently discovered by the present author’s group is that of histones . The authors found that histones H1, H2A, H2B, H3 and H4 can all bind LPS.

PMID: 15241548,12667084 Another new class of LPS-binding molecules recently discovered by the present author’s group is that of histones . The authors found that histones H1, H2A, H2B, H3 and H4 can all bind LPS.

indirect

PMID: 15241548 Furthermore, H2A inhibits the ligation of LPS to macrophages, and the LPS-induced production of TNF-a and nitric oxide.

PMID: 15241548,7730641 Human a-defensins (HNP-1 to HNP-4) have been shown to interact with LPS, although less efficiently than BPI

PMID: 15241548,7730641 Human a-defensins (HNP-1 to HNP-4) have been shown to interact with LPS, although less efficiently than BPI

PMID: 15241548,7730641 Human a-defensins (HNP-1 to HNP-4) have been shown to interact with LPS, although less efficiently than BPI

PMID: 15241548,11036008,1406489 PMB binds to the LPS of Gram-negative bacteria, changes the packing order of LPS and increases the permeability of the outer membrane to a variety of molecules, including PMB itself (self-promoted uptake of PMB)

PMID: 15241548 Another bacterium-derived cyclic antimicrobial peptide, gramicidin S, binds LPS with a fourtimes lower affinity than PMB

PMID: 15241548 A first group of molecules that recognize LPSs are lectins directed against the O-specific polysaccharide chain or the core region of particular LPSs

PMID: 15241548 Other more extensively studied constitutive proteins of Gram-negative bacteria which interact with the lipid A region of LPS are FhuA, OmpT and MsbA.

PMID: 15241548 Other more extensively studied constitutive proteins of Gram-negative bacteria which interact with the lipid A region of LPS are FhuA, OmpT and MsbA.

PMID: 15241548 Other more extensively studied constitutive proteins of Gram-negative bacteria which interact with the lipid A region of LPS are FhuA, OmpT and MsbA.

PMID: 15241548,1918062,2549069 A second group of molecules that interact with LPS are enzymes involved in its degradation, such as the lysosomal phosphatase involved in LPS catabolism and the granule acyloxyacyl hydrolase which removes the secondary acyl chains of LPS

PMID: 15241548,1918062,2549069 A second group of molecules that interact with LPS are enzymes involved in its degradation, such as the lysosomal phosphatase involved in LPS catabolism and the granule acyloxyacyl hydrolase which removes the secondary acyl chains of LPS

PMID: 15241548 Phospholipid transfer protein (PLTP) and cholesteryl ester transfer protein (CETP) are lipid transport proteins found in plasma in association with apo A1.

PMID: 15241548 Phospholipid transfer protein (PLTP) and cholesteryl ester transfer protein (CETP) are lipid transport proteins found in plasma in association with apo A1.

PMID: 15241548,10768924,8647810 PLTP has been reported to bind LPS, and to transfer it from Gram-negative bacterial membranes or LPS aggregates to high-density lipoprotein (HDL) particles