The structural basis for monoclonal antibody 5D2 binding to the tryptophan-rich loop of lipoprotein lipase

Abstract

For three decades, the LPL–specific monoclonal antibody 5D2 has been used to investigate LPL structure/function and intravascular lipolysis. 5D2 has been used to measure LPL levels, block the triglyceride hydrolase activity of LPL, and prevent the propensity of concentrated LPL preparations to form homodimers. Two early studies on the location of the 5D2 epitope reached conflicting conclusions, but the more convincing report suggested that 5D2 binds to a tryptophan (Trp)-rich loop in the carboxyl terminus of LPL. The same loop had been implicated in lipoprotein binding. Using surface plasmon resonance, we showed that 5D2 binds with high affinity to a synthetic LPL peptide containing the Trp-rich loop of human (but not mouse) LPL. We also showed, by both fluorescence and UV resonance Raman spectroscopy, that the Trp-rich loop binds lipids. Finally, we used X-ray crystallography to solve the structure of the Trp-rich peptide bound to a 5D2 Fab fragment. The Trp-rich peptide contains a short α-helix, with two Trps projecting into the antigen recognition site. A proline substitution in the α-helix, found in mouse LPL, is expected to interfere with several hydrogen bonds, explaining why 5D2 cannot bind to mouse LPL. For three decades, the LPL–specific monoclonal antibody 5D2 has been used to investigate LPL structure/function and intravascular lipolysis. 5D2 has been used to measure LPL levels, block the triglyceride hydrolase activity of LPL, and prevent the propensity of concentrated LPL preparations to form homodimers. Two early studies on the location of the 5D2 epitope reached conflicting conclusions, but the more convincing report suggested that 5D2 binds to a tryptophan (Trp)-rich loop in the carboxyl terminus of LPL. The same loop had been implicated in lipoprotein binding. Using surface plasmon resonance, we showed that 5D2 binds with high affinity to a synthetic LPL peptide containing the Trp-rich loop of human (but not mouse) LPL. We also showed, by both fluorescence and UV resonance Raman spectroscopy, that the Trp-rich loop binds lipids. Finally, we used X-ray crystallography to solve the structure of the Trp-rich peptide bound to a 5D2 Fab fragment. The Trp-rich peptide contains a short α-helix, with two Trps projecting into the antigen recognition site. A proline substitution in the α-helix, found in mouse LPL, is expected to interfere with several hydrogen bonds, explaining why 5D2 cannot bind to mouse LPL. The LPL–specific mouse monoclonal antibody 5D2, created by the laboratory of John Brunzell (1Babirak S.P. Iverius P.H. Fujimoto W.Y. Brunzell J.D. Detection and characterization of the heterozygote state for lipoprotein lipase deficiency.Arteriosclerosis. 1989; 9: 326-334Crossref PubMed Google Scholar, 2Chang S-F. Reich B. Brunzell J.D. Will H. Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2.J. Lipid Res. 1998; 39: 2350-2359Abstract Full Text Full Text PDF PubMed Google Scholar, 3Peterson J. Fujimoto W.Y. Brunzell J.D. Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.J. Lipid Res. 1992; 33: 1165-1170Abstract Full Text PDF PubMed Google Scholar), has been a key reagent for investigating LPL for more than 30 years. 5D2 was generated by immunizing mice with bovine LPL but binds LPL from multiple vertebrate species (including rat LPL but not mouse LPL) (2Chang S-F. Reich B. Brunzell J.D. Will H. Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2.J. Lipid Res. 1998; 39: 2350-2359Abstract Full Text Full Text PDF PubMed Google Scholar, 3Peterson J. Fujimoto W.Y. Brunzell J.D. Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.J. Lipid Res. 1992; 33: 1165-1170Abstract Full Text PDF PubMed Google Scholar). 5D2 was initially used to develop immunoassays for LPL in human plasma (1Babirak S.P. Iverius P.H. Fujimoto W.Y. Brunzell J.D. Detection and characterization of the heterozygote state for lipoprotein lipase deficiency.Arteriosclerosis. 1989; 9: 326-334Crossref PubMed Google Scholar). Subsequently, the epitope for 5D2 was localized to the carboxyl-terminal domain of LPL (downstream from the larger N-terminal domain containing LPL's catalytic triad) (3Peterson J. Fujimoto W.Y. Brunzell J.D. Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.J. Lipid Res. 1992; 33: 1165-1170Abstract Full Text PDF PubMed Google Scholar). Nevertheless, 5D2 was shown to block 95% of LPL's catalytic activity against a triolein substrate (4Wong H. Davis R.C. Thuren T. Goers J.W. Nikazy J. Waite M. Schotz M.C. Lipoprotein lipase domain function.J. Biol. Chem. 1994; 269: 10319-10323Abstract Full Text PDF PubMed Google Scholar). That observation, together with the observation that 5D2 does not block LPL's activity against a soluble substrate, suggested that 5D2 could bind to lipid-binding in LPL and interfere with to LPL's catalytic domain (4Wong H. Davis R.C. Thuren T. Goers J.W. Nikazy J. Waite M. Schotz M.C. Lipoprotein lipase domain function.J. Biol. Chem. 1994; 269: 10319-10323Abstract Full Text PDF PubMed Google Scholar). the location of epitope has had a the laboratory of John Brunzell on with a LPL synthetic that 5D2 binds to LPL Brunzell J.D. of the epitope on lipoprotein lipase by a monoclonal antibody lipase 1992; PubMed Google Scholar), but studies on that For T. of tryptophan in lipoprotein on and catalytic Biol. Chem. Full Text Full Text PDF PubMed Google found that two in a carboxyl-terminal Trp-rich 5D2 binding as as LPL's to the in triglyceride by H. Iverius The carboxyl-terminal domain of lipoprotein lipase binds to the lipoprotein and binding of to Biol. Chem. 1994; 269: Full Text PDF PubMed Google that and the of the carboxyl terminus of LPL to bind The of the Trps for was by H. J.D. is for the of in Full Text Full Text PDF PubMed Google Scholar). studies that the Trp-rich loop is to 5D2 binding as as lipoprotein by the conformation of the T. of tryptophan in lipoprotein on and catalytic Biol. Chem. Full Text Full Text PDF PubMed Google showed that LPL and for 5D2 (2Chang S-F. Reich B. Brunzell J.D. Will H. Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2.J. Lipid Res. 1998; 39: 2350-2359Abstract Full Text Full Text PDF PubMed Google that 5D2 bound to a synthetic peptide to LPL's Trp-rich but not to the initially by 5D2 not bind to a synthetic peptide to the Trp-rich of mouse LPL, a substitution M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google synthetic and surface plasmon resonance that 5D2 binds to LPL's Trp-rich and on to the of in the Trp-rich loop for 5D2 binding 5D2 to LPL structure also had a laboratory that LPL could with a in 5D2 was used both to LPL and to the bound LPL (3Peterson J. Fujimoto W.Y. Brunzell J.D. Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.J. Lipid Res. 1992; 33: 1165-1170Abstract Full Text PDF PubMed Google Scholar). That observation to that LPL a studies with antibody 5D2 to that LPL's catalytic activity on the of LPL into (3Peterson J. Fujimoto W.Y. Brunzell J.D. Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.J. Lipid Res. 1992; 33: 1165-1170Abstract Full Text PDF PubMed Google Scholar). The that LPL was a had been P.H. Lipoprotein lipase from bovine and Biol. Chem. Full Text PDF PubMed Google Scholar, Nikazy J. Schotz M.C. Lipoprotein lipase: of the by Lipid Res. Full Text PDF PubMed Google Scholar, T. of bovine lipoprotein lipase as by Biol. Chem. Full Text PDF PubMed Google Scholar), but the studies by Brunzell and (3Peterson J. Fujimoto W.Y. Brunzell J.D. Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.J. Lipid Res. 1992; 33: 1165-1170Abstract Full Text PDF PubMed Google for The that LPL is as a was (4Wong H. Davis R.C. Thuren T. Goers J.W. Nikazy J. Waite M. Schotz M.C. Lipoprotein lipase domain function.J. Biol. Chem. 1994; 269: 10319-10323Abstract Full Text PDF PubMed Google Scholar, M. in lipoprotein lipase and of the Biol. Chem. Full Text Full Text PDF PubMed Google Scholar, of lipoprotein lipase into Biol. Chem. Full Text Full Text PDF PubMed Google Scholar, H. Lipoprotein lipase: from to J. PubMed Google Scholar), and in the the of LPL a T. lipoprotein lipase to and lipase activity in PubMed Google Scholar, M. of lipase PubMed Google Scholar). both of the early from LPL is a and that is for catalytic to Using and M. lipase is as a PubMed Google showed that LPL is Detection of LPL in a 5D2 was with LPL a M. lipase is as a PubMed Google Scholar). The that LPL, as as of LPL, was by studies M. lipase is as a PubMed Google Scholar). X-ray studies and X-ray crystallography studies B. B. M. of the lipoprotein that plasma triglyceride PubMed Google that LPL, high a conformation B. B. M. of the lipoprotein that plasma triglyceride PubMed Google Scholar). Two LPL a the Trp-rich loop in the carboxyl terminus of LPL was in the catalytic in the terminus of the LPL B. B. M. of the lipoprotein that plasma triglyceride PubMed Google Scholar). The same LPL by in LPL J.D. The structure of lipoprotein lipase in lipase PubMed Google Scholar). conformation is with LPL activity, as not of with the Trp-rich triglyceride by the catalytic domain M. lipase is as a PubMed Google Scholar, B. B. M. of the lipoprotein that plasma triglyceride PubMed Google Scholar). The that 5D2 binds to LPL's carboxyl-terminal Trp-rich loop M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google to that the binding of 5D2 to LPL the in the structure and LPL in a preparations of LPL, high in the of 5D2 Fab and the LPL against a soluble substrate M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar). the of LPL structure had studies with 5D2 as that LPL is a and that for catalytic activity (3Peterson J. Fujimoto W.Y. Brunzell J.D. Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.J. Lipid Res. 1992; 33: 1165-1170Abstract Full Text PDF PubMed Google Scholar). The more studies with 5D2 that LPL is M. lipase is as a PubMed Google and that 5D2 LPL's propensity for M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar). three antibody 5D2 was two the for 5D2 binding to the Trp-rich loop in LPL has been been into why 5D2 to bind to mouse LPL. A is the of LPL's Trp-rich loop in binding lipids. The Trp-rich loop is for lipoprotein binding and triglyceride in the of LPL T. of tryptophan in lipoprotein on and catalytic Biol. Chem. Full Text Full Text PDF PubMed Google Scholar), but that the Trps in binding has been the we both The for 5D2 was a from John Brunzell of The and in a of and containing and from was to and a in the concentrated by with and for 30 the was and against for to the was a The was with a of of and with The was with The of the antibody was by and the binding of the antibody to human LPL was by of the 5D2 antibody was by the The (including the of human mouse and LPL in with a into the for in a J. the of the high domain in binding lipoprotein Biol. Chem. 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M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar). that from the human We used to 5D2 binding to and LPL We 5D2 binding to the binding of a to human LPL, but was binding of 5D2 to LPL three of species in the that is for 5D2 binding (2Chang S-F. Reich B. Brunzell J.D. Will H. Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2.J. Lipid Res. 1998; 39: 2350-2359Abstract Full Text Full Text PDF PubMed Google Scholar, M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar). We 5D2 binding to LPL but the binding was than we expected from the studies that the of 5D2 binding to LPL from the a is with from M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar), that 5D2 binds to the carboxyl-terminal domain of human LPL with affinity than to the that affinity of 5D2 binding to synthetic and LPL we 5D2 binding to mouse and human LPL. We with a mouse LPL with a in had been to found in human 5D2 to bind to mouse LPL but bound to the mouse LPL with the substitution we 5D2 binding to human LPL and a human LPL containing a 5D2 bound to the human LPL, but was binding to the human LPL with the substitution We Fab of 5D2, that bound LPL and used X-ray crystallography to solve the Fab both in the and of The structure a Fab of two from the and two from the and Fab and of for the 5D2 structure by and to and the and for of and the for the 5D2 structure showed for two in the of of the of the antigen binding from in the the and 5D2 the with a of in The two that to with a of in the was in the site the the and and by from the The peptide was to the of the antigen recognition with a of from and the and a of from and the The terminus of the of the with the of in to form a hydrogen with the of the in the 5D2 A in was into the of the antigen binding site binding site of the 5D2 Fab hydrogen the Fab and the peptide as and by to The of LPL and in the of and in the form a that is the The N-terminal of the peptide of the antigen binding site and the with LPL a hydrogen with the of the in the of and hydrogen with the of and The of with 5D2 is A of and the a by from the of the and Biol. 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M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar), LPL to binding by The substitution a hydrogen the of and the of The substitution with the of The conformation of the peptide to by a of hydrogen bonds, the two in the for that with the of The carboxyl-terminal is by hydrogen and and and that 5D2 does not bind to mouse LPL contains a than a in the of the synthetic LPL peptide LPL in human LPL is with a the binding of 5D2 is by the and of in human hydrogen of the of of with a hydrogen and a with the of the of is hydrogen to the of to the of the bound structure the with 5D2 is to that interfere with the of the Trp-rich loop in the J. A for peptide and structure Chem. Google a short in the mouse LPL with in to the structure and the for human and The of three the of the a from to to in was in and not the for that the in a more in the of of in the of and J. 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The for in the of is is larger than the in and for the that the in with the more of the We the structure of 5D2 bound to a peptide to the Trp-rich loop the carboxyl terminus of human LPL. of the LPL in the The carboxyl-terminal of the peptide a short that was in the of the antigen recognition with the and a the and a and the a short was in the peptide bound to is is in LPL of several that is and by 5D2 binding. the is the observation that in LPL the peptide is not from in studies the LPL is bound to Fab 5D2 M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar). the conformation of LPL, we expected to that the LPL from in the of bound The Trp-rich loop in LPL was in a LPL structure J.D. The structure of lipoprotein lipase in lipase PubMed Google and to that conformation was a of the LPL in the the Trp-rich loop is in the catalytic of a LPL X-ray structure of the B. B. M. of the lipoprotein that plasma triglyceride PubMed Google Scholar), LPL's Trp-rich loop was also in the catalytic of a LPL and not the is to that binding conformation of the LPL's Trp-rich the Trp-rich loop and the binding site for on of the LPL B. B. M. of the lipoprotein that plasma triglyceride PubMed Google Scholar). 5D2 binds to LPL, as shown in studies M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar, M. T. M. monoclonal that the binding of LPL to Lipid Res. Full Text Full Text PDF PubMed Google and in of the studies that LPL's Trp-rich loop is a of the 5D2 but is that LPL the of 5D2 binding. by 5D2 bound with affinity to the carboxyl-terminal of human LPL than to the synthetic peptide M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar). by the for 5D2 binding to the human and was but by 5D2 binds more to human LPL than to LPL. by H. Iverius The carboxyl-terminal domain of lipoprotein lipase binds to the lipoprotein and binding of to Biol. Chem. 1994; 269: Full Text PDF PubMed Google that and in the carboxyl terminus of LPL LPL's to bind studies by T. of tryptophan in lipoprotein on and catalytic Biol. Chem. Full Text Full Text PDF PubMed Google that and triglyceride that the Trps in binding that the had LPL studies the we with the by fluorescence from to to the of the Trp-rich loop with is with the that Trps in the binding of to B. in by resonance Raman and fluorescence J. Full Text Full Text PDF PubMed Google Scholar). that the Trps in with lipids. The of LPL's Trp-rich loop also the propensity of LPL, high to form B. B. M. of the lipoprotein that plasma triglyceride PubMed Google Scholar). the of the Trp-rich loop with the catalytic the Trps from the B. B. M. of the lipoprotein that plasma triglyceride PubMed Google Scholar). The binding of 5D2 to LPL also the Trp-rich loop and the of M. M. of lipoprotein lipase by into the of plasma triglyceride PubMed Google Scholar). 5D2 was generated by immunizing laboratory mice with bovine LPL. For that is not that 5D2 does not mouse LPL. of 5D2 binding to LPL that the substitution of a for in the Trp-rich loop of mouse LPL a in the of 5D2 binding to mouse LPL (2Chang S-F. Reich B. Brunzell J.D. Will H. Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2.J. Lipid Res. 1998; 39: 2350-2359Abstract Full Text Full Text PDF PubMed Google Scholar), but was not that substitution was in the of LPL. studies that in mouse LPL was to 5D2 bound to mouse LPL and in human LPL was with 5D2 binding to human LPL was The structure to of with the hydrogen and a with the of of the 5D2 the substitution in the Trp-rich loop of LPL is found in multiple mouse species and and in the was binding of 5D2 to a synthetic peptide to the Trp-rich loop from LPL. The of a in the Trp-rich loop in the LPL as that more to than to mice J.W. of into the of and PubMed Google Scholar). mice and both a of in in the form of The into and used for but plasma triglyceride in both mice and the of and plasma for of in PubMed Google Scholar, B. H. M. for and Google Scholar). is to that the in the Trp-rich loop with triglyceride the proline in mouse and LPL LPL by LPL's to bind and is in the the and in the for 5D2 and been in the The John Brunzell for the 5D2 and for The to the the the the and for with X-ray with binding LPL peptide surface plasmon resonance UV resonance Raman

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