Antibodies against low density lipoprotein conjugated to a detectable label and uses thereof

Abstract

The present disclosure features antibodies and antibody fragments capable of binding to oxidized-low density lipoprotein, wherein the antibody is conjugated to a detectable label. The disclosure also provides methods for using the antibodies conjugated to a detectable label to detect the presence for atherosclerotic plaques in a subject as well as methods for diagnosing a subject with a cardiovascular disease.

Description

[0001]PATENT ATTORNEY DOCKET NO: 51473-027WO2 ANTIBODIES AGAINST LOW DENSITY LIPOPROTEIN CONJUGATED TO A DETECTABLE LABEL AND USES THEREOF SEQUENCE LISTING This application contains a Sequence Listing which has been submitted electronically in XML format and is hereby incorporated by reference in its entirety. Said XML copy, created on September 18, 2025, is named “51473-027WO2_Sequence_Listing_9_18_25” and is 29,457 bytes in size. BACKGROUND Coronary heart disease is a common heart condition where the major blood vessels that supply the heart struggle to send enough blood, oxygen and nutrients to the heart muscle. About 20.1 million adults aged 20 and older suffer from this disease which is usually caused by cholesterol deposits, also known as plaques, in the heart arteries and inflammation. Signs and symptoms of coronary artery disease occur when the heart does not get enough oxygen-rich blood. Coronary heart disease patients with vulnerable atherosclerotic plaque are at a higher risk of experiencing severe cardiovascular events. Identifying these patients remains a key clinical challenge, with existing imaging approaches utilized to visualize plaque characteristics to evaluate the severity of disease. There remains a need to develop tools to identify atherosclerotic plaques in patients so they may receive the care they need. SUMMARY OF THE INVENTION In an aspect, the disclosure provides a composition comprising an antibody conjugated to one or more detectable labels, wherein the antibody comprises heavy chain complementarity determining regions (HCDRs) HCDR1, HCDR2, and HCDR3 comprising the sequences of SEQ ID NOs: 4, 5 and 6, respectively, and light chain complementarity determining regions (LCDRs) LCDR1, LCDR2, and LCDR3comprising the sequences of SEQ ID NOs: 7, 8 and 9, respectively. In some embodiments, the antibodycomprises a variable heavy region (VH) of SEQ ID NO.: 10, a variable light region (VL) of SEQ ID NO.: 11, or both. In some embodiments, the antibody is conjugated to the label by way of a bond. In some embodiments, the antibody is conjugated to the label by way of a linker. In some embodiments, the linker comprises a polymer, a polypeptide, a polysaccharide, a polynucleotide, or a combination thereof. In some embodiments, the detectable label comprises a fluorescent, chemiluminescent, chromophoric, radioactive, electron-dense, magnetic, or echogenic label. In some embodiments, the detectable label comprises a magnetic label. In some embodiments, the detectable label comprises fludeoxyglucose (FDG). In some embodiments, the detectable label comprises gadolinium. In some embodiments, the detectable label comprises iohexol. In some embodiments, the detectable label is a near-infrared fluorophore. In some embodiments, the near-infrared fluorophore absorbs light at 800 nm. In another aspect, the disclosure provides a pharmaceutical composition comprising any one of the compositions described herein and one or more pharmaceutically acceptable excipients. In another aspect, the disclosure provides a method for detecting the presence of an atherosclerotic plaque in a subject comprising (i) administering any one of the compositions described PATENT ATTORNEY DOCKET NO: 51473-027WO2 herein to the subject; and (ii) detecting the presence of the detectable label present in the subject; wherein the presence of the detectable label indicates the presence of an atherosclerotic plaque in the subject. In another aspect, the disclosure provides a method of diagnosing a cardiovascular disease in a subject comprising (i) administering any one of the compositions described herein to the subject; and (ii) detecting the presence of the detectable label present in the subject, wherein the presence of the detectable label indicates the subject has a cardiovascular disease. In some embodiments, the cardiovascular disease comprises aortic valve stenosis, aortic valve sclerosis, or atherosclerosis. In some embodiments, the composition is administered subcutaneously or intravenously. In another aspect, the disclosure provides a method for detecting the presence of an atherosclerotic plaque in a subject comprising (i) obtaining a sample from the subject; (ii) contacting the sample with any one of the compositions described herein; and (iii) detecting the presence of the detectable label present in the sample, wherein the presence of the detectable label indicates the presence of an atherosclerotic plaque. In some embodiments, the sample is a blood sample, serum sample, or tissue sample. In some embodiments, detecting the presence of the detectable label is performed using radiography, ultrasound, or tomography. In some embodiments, detecting the presence of the detectable label is performed using magnetic resonance imaging. In some embodiments, detecting the presence of the detectable label is performed using intravascular ultrasound. In some embodiments, detecting thepresence of the detectable label is performed using fluorescence molecular tomography, opticalcoherence tomography, computed tomography, or a positron emission tomography. In some embodiments, the subject is a human. BRIEF DESCRIPTION OF THE FIGURES Exemplary embodiments are illustrated in referenced figures. It is intended that the embodiments and figures disclosed herein are to be considered illustrative rather than restrictive. FIG.1A shows an image generated using fluorescent molecular reflectance showing a murine en face aorta sample stained ex vivo with orticumab conjugated with a fluorophore which fluoresces at 800 nm which colocalized generally with the atherosclerotic plaque stained by Oil Red O. FIG.1B shows an image generated using fluorescent molecular reflectance showing a human femoral artery sample stained ex vivo with orticumab conjugated with a fluorophore which fluoresces at 800 nm FIG.2A is a bar graph showing the region of interest (ROI) signal determined using fluorescence molecular tomography (FMT) imaging to visualize orticumab conjugated with a fluorophore which fluoresces at 800 nm 4 hours after administration to Ldlr- / - mice who were fed a high fat diet for up to 45 weeks prior to administration in comparison to a control of IgG1 conjugated to the fluorophore. FIG.2B is a computed tomography (CT) image obtained 4 hours after administering orticumab conjugated with a fluorophore which fluoresces at 800 nm to Ldlr- / - mice who were fed a high fat diet for up to 45 weeks a in comparison to a control of IgG1 conjugated to the fluorophore. PATENT ATTORNEY DOCKET NO: 51473-027WO2 FIG.3A is a bar graph showing the binding affinity of oxidized low-density lipoprotein (ox-LDL) with orticumab, orticumab labelled with LI-COR® IRDye 800CW Mal, or orticumab labelled with LI-COR IRDye® 800CW NHS Ester when labelled using the protocol developed May 12, 2018. FIG.3B is a bar graph showing the binding affinity ox-LDL with orticumab, orticumab labelled with LI-COR IRDye 800CW Mal, or orticumab labelled with LI-COR IRDye® 800CW NHS Ester when labelled using the protocol developed June 12, 2018. FIG.4 is an image of the fluorescence resulting from excitation at 700 nm or 800 nm of humanfemoral artery samples incubated with orticumab labelled with a fluorophore which fluoresces at 800 nm.FIG.5A is a fluorescent gel image of orticumab (A), orticumab labelled with a fluorophore which fluoresces at 800 nm (B), an IgG1 control (C), and IgG1 labelled with a fluorophore which fluoresces at 800 nm (D). FIG.5B is an image of a Coomassie stained gel of orticumab (A), orticumab labelled with a fluorophore which fluoresces at 800 nm (B), an IgG1 control (C), and IgG1 labelled with a fluorophore which fluoresces at 800 nm (D). FIG.5C shows the results of an ELISA assay to detect binding of orticumab, orticumab labelled with a fluorophore which fluoresces at 800 nm, IgG1, and IgG1 labelled with a fluorophore which fluoresces at 800 nm to ox-LDL. FIG.6A and FIG.6B are FMT images of Ldlr- / - mice 4 hours post-injection with 50 µg IgG1 labelled with a fluorophore that fluoresces at 800 nm (IgG1-800) (FIG.6A) or 50 µg of orticumab labelledwith a fluorophore that fluoresces at 800 nm (orticumab-800) (FIG. 6B) who were fed a high fat diet for upto 45 weeks prior to administration of orticumab-800 or IgG1-800. FIGS.7A-7D show FMT images overlaid with CT scans of Ldlr- / - mice 4 hours post-injection with 50 µg IgG1 labelled with a fluorophore that fluoresces at 800 nm (IgG1-800) (FIG.7A) or 50 µg of orticumab labelled with a fluorophore that fluoresces at 800 nm (orticumab-800) (FIG.7B) who were fed a high fat diet for up to 45 weeks prior to administration of orticumab-800 or IgG1-800 along with the corresponding zoomed in images (FIGS.7C and 7D), respectively. FIG.8A is a bar graph showing the total fluorescence detected at 800 nm for the ROI in the aorta of mice who were administered either orticumab labelled with a fluorophore which fluoresces at 800 nm (orticumab-800) or IgG1 labelled with a fluorophore which fluoresces at 800 nm (control-800). FIG.8B are FMT images of the aorta prepared en face of mice who were administered either orticumab labelled with a fluorophore which fluoresces at 800 nm (orticumab-800) or IgG1 labelled with a fluorophore which fluoresces at 800 nm (control-800). FIG.9 shows confocal microscope images of the aorta harvested from mice that were administered either orticumab labelled with a fluorophore which fluoresces at 800 nm (orticumab-800) or IgG1 labelled with a fluorophore which fluoresces at 800 nm (control-800) and comparing them to adjacent aorta sections stained with Oil Red O. FIG.10A shows the results of an ELISA assay to detect binding of orticumab or orticumab labelled with a fluorophore which fluoresces at 647 nm to ox-LDL. FIG.10B shows a white light confocal microscope image of en face aorta from mice that wereadministered orticumab labelled with a fluorophore which fluoresces at 647 nm (orticumab-647) or IgG1 PATENT ATTORNEY DOCKET NO: 51473-027WO2 labelled with a fluorophore which fluoresces at 647 nm (control-647) where the imaged lesions are shown in the box. FIG.10C shows a side view of Z-stack confocal microscope image of lesions found in the aortas of mice that were administered orticumab labelled with a fluorophore which fluoresces at 647 nm (orticumab-647) or IgG1 labelled with a fluorophore which fluoresces at 647 nm (control-647) where green shows autofluorescence and red shows the 647 nm signal. FIG.10D shows a top-down view of Z-stack confocal microscope image of lesions found in the aortas of mice were administered orticumab labelled with a fluorophore which fluoresces at 647 nm (orticumab-647) or IgG1 labelled with a fluorophore which fluoresces at 647 nm (control-647) where green shows autofluorescence and red shows the 647 nm signal. Definitions Terms used in the claims and specification are defined as set forth below unless otherwise specified. It must be noted that, as used in the specification and the appended claims, the singular forms "a," "an," and "the" include plural referents unless the context clearly dictates otherwise. As used herein, "about" will be understood by persons of ordinary skill and will vary to some extent depending on the context in which it is used. If there are uses of the term which are not clear to persons of ordinary skill given the context in which it is used, "about" will mean up to plus or minus 10% of the particular value. “Administering” and “administer” as used herein refer to any route for delivering a pharmaceutical composition to a patient. Routes of delivery may include non-invasive peroral (through the mouth), topical (skin), transmucosal (nasal, buccal / sublingual, vaginal, ocular and rectal) and inhalation routes, as well as parenteral routes, and other methods known in the art. Parenteral refers to a route of delivery thatis generally associated with injection, including intraorbital, infusion, intraarterial, intracarotid,intracapsular, intracardiac, intradermal, intramuscular, intraperitoneal, intrapulmonary, intraspinal, intrasternal, intrathecal, intrauterine, intravenous, subarachnoid, subcapsular, subcutaneous, transmucosal, or transtracheal. Via the parenteral route, the compositions may be in the form of solutions or suspensions for infusion or for injection, or as lyophilized powders. As used herein, the term “antibody” or “antibodies” as used herein are meant in a broad sense and includes immunoglobulin molecules including polyclonal antibodies, monoclonal antibodies including murine, human, human-adapted, humanized and chimeric monoclonal antibodies, antibody fragments, bispecific or multispecific antibodies, dimeric, tetrameric or multimeric antibodies, and single chain antibodies. Immunoglobulins can be assigned to five major classes, namely IgA, IgD, IgE, IgG and IgM, depending on the heavy chain constant domain amino acid sequence. IgA and IgG are further sub- classified as the isotypes IgA1, IgA2, IgG1, IgG2, IgG3 and IgG4. Antibody light chains of any vertebrate species can be assigned to one of two clearly distinct types, namely kappa (κ) and lambda (λ), based on the amino acid sequences of their constant domains. As used herein, the term “antibody fragment” refers to a portion of an immunoglobulin molecule that retains the heavy chain and / or the light chain antigen binding site, such as heavy chain PATENT ATTORNEY DOCKET NO: 51473-027WO2 complementarity determining regions (HCDR) 1, 2 and 3, light chain complementarity determining regions (LCDR) 1, 2 and 3, a heavy chain variable region (VH), or a light chain variable region (VL). Antibody fragments include a Fab fragment, a monovalent fragment consisting of the VL, VH, CL and CHI domains; a F(ab)2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge region; a Fd fragment consisting of the VH and CHI domains; a Fv fragment consisting of the VL and VH domains of a single arm of an antibody; a domain antibody (dAb) fragment (Ward et al (1989) Nature 341:544-546), which consists of a VH domain. VH and VL domains can be engineered and linked together via a synthetic linker to form various types of single chain antibody designs where the VH / VL domains pair intramolecularly, or intermolecularly in those cases when the VH and VL domains are expressed by separate single chain antibody constructs, to form a monovalent antigen binding site, such as single chain Fv (scFv) or diabody; described for example in PCT Intl. Publ. Nos. WO1998 / 44001, WO1988 / 01649, WO1994 / 13804, and WO1992 / 01047. These antibody fragments are obtained using well known techniques known to those of skill in the art, and the fragments are screened for utility in the same manner as are full length antibodies. “Aortic sclerosis” is the deposition of calcium and thickening of the aortic wall or aortic valve. “Aortic valve sclerosis” refers to the deposition of calcium and thickening of the aortic valve, typically in the absence of obstruction of ventricular outflow. Clinically, aortic valve sclerosis can be suspected in the presence of symptoms such as soft ejection systolic murmur at the aortic area, normal split of the second heart sound, and normal volume carotid pulse, but it can be best detected by echocardiography. “Aortic stenosis” refers to increased blood flow velocity across a narrowed valve orifice, which is acommon cause of left ventricular outflow tract obstruction. A common cause of aortic stenosis is calcific valvular disease, followed by congenital bicuspid aortic valve. Another common cause of rheumatic heart disease. Aortic stenosis is usually suspected on the basis of a systolic murmur on routine cardiac examination. The presence of the following findings can indicate the likelihood of severe aortic stenosis: long ejection systolic murmur with radiation to carotids; delayed carotid upstroke; single or paradoxical splitting of second heart sound. Transthoracic echocardiography (TTE) is commonly used in diagnosing aortic stenosis. “Bind” in reference to the interaction between antibody and epitope, “selectively binds” or “specifically binds” refers to the ability of an antibody or antibody fragment thereof described herein to bind to a target, such as a molecule present on the cell-surface, with a KD 10-5M (10000 nM) or less, e.g., 10-6M, 10-7M, 10-8M, 10-9M, 10-10M, 10-11M, 10-12M, or less. Specific binding can be influenced by, for example, the affinity and avidity of the polypeptide agent and the concentration of polypeptide agent. The person of ordinary skill in the art can determine appropriate conditions under which the polypeptide agents described herein selectively bind the targets using any suitable methods, such as titration of a polypeptide agent in a suitable cell binding assay. A “cardiovascular disease,” as used herein, refers to a disorder of the heart and blood vessels, and includes disorders of the arteries, veins, arterioles, venules, and capillaries. Non-limiting examples of cardiovascular diseases include congestive heart failure, arrhythmia, pericarditis, acute myocardial infarction, infarcted myocardium, coronary artery disease, coronary heart disease, ischemic heartdisease, cardiomyopathy, stroke, hypertensive heart disease, heart failure, pulmonary heart disease,ischemic syndrome, coronary microvascular disease, cardiac dysrhythmias, rheumatic heart disease, PATENT ATTORNEY DOCKET NO: 51473-027WO2 aortic aneurysms, atrial fibrillation, congenital heart disease, endocarditis, inflammatory heart disease, endocarditis, inflammatory cardiomegaly, myocarditis, valvular heart disease, cerebrovascular disease, and peripheral artery disease, or any combination thereof. The terms “diagnose,” “diagnosing,” and “diagnosis” are used herein to refer to the identification or classification of a molecular or pathological state, disease or condition (e.g., cardiovascular disease). For example, “diagnosis” may refer to identification of a particular type of cardiovascular disease. An antibody variable region consists of a “framework” region interrupted by three “antigen binding sites”. The antigen binding sites are defined using various terms such as Complementarity Determining Regions (CDRs), three in the VH (HCDR1, HCDR2, HCDR3), and three in the VL (LCDR1, LCDR2, LCDR3), are based on sequence variability (Wu and Kabat J Exp Med 132:211-50, 1970; Kabat et al Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md., 1991) or “Hypervariable regions”, “HVR”, or “HV”, three in the VH (H1, H2, H3) and three in the VL (L1, L2, L3), refer to the regions of an antibody variable domains which are hypervariable in structure as defined by Chothia and Lesk (Chothia and Lesk Mol Biol 196:901-17, 1987). Other terms include “IMGT-CDRs” (Lefranc et al., Dev Comparat Immunol 27:55-77, 2003) and “Specificity Determining Residue Usage” (SDRU) (Almagro, Mol Recognit 17:132-43, 2004). The International ImMunoGeneTics (IMGT) database provides a standardized numbering and definition of antigen-binding sites. The correspondence between CDRs, HVs and IMGT delineations is described in Lefranc et al., Dev Comparat Immunol 27:55-77, 2003. The term “effective amount” as used herein refers to the amount of a composition to bedetectable using the desired detection technique. In various embodiments, the compositions described herein further comprise a pharmaceutically acceptable carrier. In some embodiments, a composition is used, for example, to diagnose a cardiovascular disease in a subject or to detect atherosclerotic plaques in a subject. It will be understood, however, that the total usage of the compositions and formulations as disclosed herein will be decided by the attending physician within the scope of sound medical judgment. The term “epitope” as used herein means a portion of an antigen to which an antibody specifically binds. Epitopes usually consist of chemically active (such as polar, non-polar or hydrophobic) surface groupings of moieties such as amino acids or polysaccharide side chains and can have specific three- dimensional structural characteristics, as well as specific charge characteristics. An epitope can be composed of contiguous and / or discontiguous amino acids that form a conformational spatial unit. For a discontiguous epitope, amino acids from differing portions of the linear sequence of the antigen come in close proximity in 3-dimensional space through the folding of the protein molecule. As used herein, the term “Fc domain” refers to a dimer of two Fc domain monomers that is capable of binding an Fc receptor through the interaction between the two CH3 antibody constant domains. “Framework” or “framework sequences” are the remaining sequences of a variable region other than those defined to be antigen binding sites. Because the antigen binding sites can be defined by various terms as described above, the exact amino acid sequence of a framework depends on how the antigen-binding site was defined. PATENT ATTORNEY DOCKET NO: 51473-027WO2 “Human antibody” refers to an antibody having heavy and light chain variable regions in which both the framework and the antigen binding sites are derived from sequences of human origin. If the antibody contains a constant region, the constant region also is derived from sequences of human origin. “Humanized antibody” refers to an antibody in which the antigen binding sites are derived from non-human species and the variable region frameworks are derived from human immunoglobulin sequences. Humanized antibodies may include substitutions in the framework regions so that the framework may not be an exact copy of expressed human immunoglobulin or germline gene sequences. “Human-adapted” antibodies or “human framework adapted (HFA)” antibodies refer to humanized antibodies adapted according to methods described in U.S. Pat. Publ. No. US2009 / 0118127. Human- adapted antibodies are humanized by selecting the acceptor human frameworks based on the maximum CDR and FR similarities, length compatibilities and sequence similarities of CDR1 and CDR2 loops and a portion of light chain CDR3 loops. A human antibody comprises heavy or light chain variable regions that are “derived from” sequences of human origin wherein the variable regions of the antibody are obtained from a system that uses human germline immunoglobulin or rearranged immunoglobulin genes. Such systems include human immunoglobulin gene libraries displayed on phage, and transgenic non-human animals such as mice carrying human immunoglobulin loci as described herein. A “human antibody” may contain amino acid differences when compared to the human germline or rearranged immunoglobulin sequences due to for example naturally occurring somatic mutations or intentional introduction of substitutions in theframework or antigen binding sites. Typically, a human antibody is at least about 80%, 81%, 82%, 83%,84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99% or 100% identical in amino acid sequence to an amino acid sequence encoded by a human germline or rearranged immunoglobulin gene. In some cases, “human antibody” may contain consensus framework sequences derived from human framework sequence analyses, for example as described in Knappik et al., J Mol Biol 296:57-86, 2000), or synthetic HCDR3 incorporated into human immunoglobulin gene libraries displayed on phage, for example as described in Shi et al., J Mol Biol 397:385-96, 2010 and Intl. Pat. Publ. No. WO2009 / 085462. Antibodies in which antigen binding sites are derived from a non-human species are not included in the definition of human antibody. The term “in combination with” as used herein means that two or more therapeutics can be administered to a subject together in a mixture, concurrently as single agents or sequentially as single agents in any order. The term “recombinant antibody” as used herein, includes all antibodies that are prepared, expressed, created or isolated by recombinant means, such as antibodies isolated from an animal (e.g., a mouse) that is transgenic or transchromosomal for human immunoglobulin genes or a hybridoma prepared therefrom (described further below), antibodies isolated from a host cell transformed to express the antibody, antibodies isolated from a recombinant, combinatorial antibody library, and antibodies prepared, expressed, created or isolated by any other means that involve splicing of human immunoglobulin gene sequences to other DNA sequences, or antibodies that are generated in vitro using Fab arm exchange such as bispecific antibodies. PATENT ATTORNEY DOCKET NO: 51473-027WO2 The term “statistically significant” or “significantly” refers to statistical evidence that there is a difference. It is defined as the probability of making a decision to reject the null hypothesis when the null hypothesis is actually true. The decision is often made using the p-value. “Subject” or “individual” or “animal” or “patient” or “mammal,” is meant any subject, particularly a mammalian subject, for whom diagnosis, prognosis, or therapy is desired. Mammalian subjects include, but are not limited to, humans, domestic animals, farm animals, zoo animals, sport animals, pet animals such as dogs, cats, guinea pigs, rabbits, rats, mice, horses, cattle, cows; primates such as apes, monkeys, orangutans, and chimpanzees; canids such as dogs and wolves; felids such as cats, lions, and tigers; equids such as horses, donkeys, and zebras; food animals such as cows, pigs, and sheep; ungulates such as deer and giraffes; rodents such as mice, rats, hamsters and guinea pigs; and so on. In certain embodiments, the mammal is a human subject. DETAILED DESCRIPTION The present disclosure features compositions including antibodies and antibody fragments capable of binding to oxidized-low density lipoproteins (ox-LDL) which are conjugated to at least one detectable label, as well as methods of using such composition. The antibodies conjugated to a detectable label described herein may be used to identify atherosclerotic plaques in a subject using a detection technique such as radiography, tomography, or ultrasound. Additionally, the antibodies conjugated to a detectable label described herein may be used to visualize atherosclerotic plaques in asample obtained from a subject. Accordingly, the antibodies conjugated to a detectable label describedherein may be used to diagnose a cardiovascular disease in a subject. It has presently been discovered that conjugating a detectable label to the antibody orticumab which is capable of binding ox-LDL, a key driver of atherosclerosis, allows for detection of atherosclerosis in a subject. The following sections provide a detailed description of the antibodies conjugated to a detectable label, as well as exemplary methods of using such antibodies. Anti-Ox-LDL Antibodies The disclosure provides antibodies or antibody fragments capable of binding to ox-LDL conjugated to at least one detectable probe, wherein the ox-LDL is ApoB100. In some embodiments, the antibody or antibody fragment binds to a fragment of oxidized ApoB100. In some embodiments, the antibody or antibody fragment binds to a fragment of malondialdehyde (MDA) modified ApoB100. In some embodiments, ApoB100 has an amino acid sequence of IEIGLEGKGFEPTLEALFGK (SEQ ID NO: 1). As discussed herein, the disclosure provides anti- ox-LDL antibodies conjugated to one or more detectable labels. In some embodiments, the anti- oxLDL antibody is an anti- ApoB100 antibody. FIG.2 of WO 2010 / 102241describes the amino acid sequence of the 2D03 heavy chain and the 2D03 light chain, underlining the complementarity determining regions (CDRs). WO 2007 / 025781, which is hereby incorporated by reference in its entirety, discloses an antibody that selectively binds to the oxidized-LDL epitope that is selectively bound by antibody 2D03 and furtherincludes an antibody comprising at least one, two, three, four, five, or all six-complementarity determiningregion(s) (CDRs) that has the amino acid sequence of the corresponding CDR of antibody 2D03. PATENT ATTORNEY DOCKET NO: 51473-027WO2 Furthermore, an antibody with three or four CDRs having sequences corresponding to the 2D03 antibody CDRs preferably has all three heavy chain or all three light chain CDRs that have the sequence of the corresponding CDRs of antibody 2D03; that thus this aspect of the disclosure includes an antibody comprising three light chain CDRs that have the sequence of the corresponding three light chain CDRs of antibody 2D03, or three heavy chain CDRs that have the sequence of the corresponding three heavy chain CDRs of antibody 2D03; that yet more preferably, the antibody comprises three light chain CDRs and three heavy chain CDRs that have the sequence of the corresponding CDRs of antibody 2D03; that if the antibody does not comprise all six CDRs that have the sequence of the corresponding CDRs of antibody 2D03, it is preferred if some or all of the 1, 2, 3, 4 or 5 “non-identical” CDRs comprise a variant of the sequence of the corresponding CDRs of antibody 2D03, (by “a variant” WO 2007 / 025781 includes the meaning that the variant has at least 50% sequence identity with the sequence of the corresponding CDR, more preferably at least 70%, yet more preferably at least 80% or at least 90% or at least 95%; most preferably, the variant has 96% or 97% or 98% or 99% sequence identity with the sequence of the corresponding CDR of antibody 2D03; typically the “variant” CDR sequence has 5 or 4 or 3 or 2 or only 1 amino acid residue difference from the sequence of the corresponding CDR of antibody 2D03); and that this aspect of the disclosure includes antibody 2D03. The heavy chain complementarity determining region (HCDR) 1 (HCDR1), 2 (HCDR2) and 3 (HCDR3) are set forth in SEQ ID NOs: 4, 5 and 6, respectively; and light chain complementarity determining regions (LCDR) 1 (LCDR1), 2 (LCDR2) and 3 (LCDR3) are set forth in SEQ ID NOs: 7, 8 and9, respectively.HCDR1 is FSNAWMSWVRQAPG (SEQ ID NO: 4). HCDR2 is SSISVGGHRTYYADSVKGR (SEQ ID NO: 5). HCDR3 is ARIRVGPSGGAFDY (SEQ ID NO: 6). LCDR1 is CSGSNTNIGKNYVS (SEQ ID NO: 7). LCDR2 is ANSNRPS (SEQ ID NO: 8). LCDR3 is CASWDASLNGWV (SEQ ID NO: 9). In one embodiment, the antibody contains a variable heavy region (VH) amino acid sequence of SEQ ID NO: 10, and a variable light region (VL) amino acid sequence of SEQ ID NO: 11. The antibody may contain between one and five (e.g., one, two, three, four, or five) amino acid substitutions in the heavy chain amino acid sequence of SEQ ID NO: 2, which includes a VH, a hinge region, and three constant heavy chain regions. In some embodiments, the antibody includes a light chain amino acid sequence of SEQ ID NO: 3, including a VL and constant light chain region. EVQLLESGGGLVQPGGSLRLSCAASGFTFSNAWMSWVRQAPGKGLEWVSSISVGGHRTYYADSVKGR STISRDNSKNTLYLQMNSLRAEDTAVYYCARIRVGPSGGAFDYWGQGTLVTVSSASTKGPSVFPLAPSS KSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNV NHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKG PATENT ATTORNEY DOCKET NO: 51473-027WO2 QPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLT VDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK (SEQ ID NO: 2) QSVLTQPPSASGTPGQRVTISCSGSNTNIGKNYVSWYQQLPGTAPKLLIYANSNRPSGVPDRFSGSKSG TSASLAISGLRSEDEADYYCASWDASLNGWVFGGGTKLTVLGQPKAAPSVTLFPPSSEELQANKATLVC LISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVE KTVAPTECS (SEQ ID NO: 3) EVQLLESGGGLVQPGGSLRLSCAASGFTFSNAWMSWVRQAPGKGLEWVSS ISVGGHRTYY ADSVKGRSTISRDNSKNTLYLQMNSLRAEDTAVYYCARIRVGPSGGAFDYWGQGTLVTVS (SEQ ID NO: 10), QSVLTQPPSASGTPGQRVTISCSGSNTNIGKNYVSWYQQLPGTAPKLLIYANSNRPSGVPDRFSGSKSG TSASLAISGLRSEDEADYYCASWDASLNGWVFGGGTKLTVL (SEQ ID NO: 11). In some embodiments, the disclosure provides an antibody or antibody fragment that binds to oxLDL and one or more of HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4-9, respectively. In some embodiments, the disclosure provides an antibody comprising at least one CDR that hasthe amino acid sequence of the corresponding CDR of orticumab. More preferably, the antibody has twoor three or four or five CDRs that have the sequence of the corresponding CDRs of orticumab. If the antibody has three or four CDRs that have the sequence of the corresponding CDRs of orticumab, it is preferred if the antibody has all three heavy chain or all three light chain CDRs that have the sequence of the corresponding CDRs of orticumab. Thus, this aspect of the methods includes an antibody comprising three light chain CDRs that have the sequence of the corresponding three light chain CDRs of orticumab, or three heavy chain CDRs that have the sequence of the corresponding three heavy chain CDRs of orticumab. Yet more preferably, the antibody includes three light chain CDRs and three heavy chain CDRs that have the sequence of the corresponding CDRs of orticumab. If the antibody does not include all six CDRs that have the sequence of the corresponding CDRs of orticumab, it is preferred if some or all of the 1, 2, 3, 4 or 5 “non-identical” CDRs comprise a variant of the sequence of the corresponding CDRs of orticumab. By “a variant,” we include the meaning that the variant has at least 50% sequence identity with the sequence of the corresponding CDR, more preferably at least 70%, yet more preferably at least 80% or at least 90% or at least 95%. Most preferably, the variant has 96% or 97% or 98% or 99% sequence identity with the sequence of the corresponding CDR of orticumab. Typically, the “variant” CDR sequence has 5 or 4 or 3 or 2 or only 1 amino acid residue difference from the sequence of the corresponding CDR of orticumab. In particular, the disclosure provides an antibody containing “one or more of HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3” encompasses embodiments that the antibody contains one, any two, any three, any four, any five or all six of the CDRs (i.e., HCDR1, HCDR2, HCDR3, LCDR1, LCDR2and LCDR3). For example, one aspect of the embodiment provides that the antibody contains HCDR1 asset forth in SEQ ID NO: 4. Another aspect provides that the antibody contains HCDR2 as set forth in SEQ PATENT ATTORNEY DOCKET NO: 51473-027WO2 ID NO: 5. Another aspect provides that the antibody contains HCDR3 as set forth in SEQ ID NO: 6. Yet another aspect provides that the antibody contains LCDR1 as set forth in SEQ ID NO: 7. Another aspect provides that the antibody contains LCDR2 as set forth in SEQ ID NO: 8. Another aspect provides that the antibody contains LCDR3 as set forth in SEQ ID NO:9. Yet another aspect provides that the antibody contains HCDR1 as set forth in SEQ ID NO:4 and HCDR2 as set forth in SEQ ID NO: 5. Another aspect provides that the antibody contains HCDR1 as set forth in SEQ ID NO:4 and HCDR3 as set forth in SEQ ID NO: 6. Another aspect provides that the antibody contains HCDR1 as set forth in SEQ ID NO:4 and LCDR1 as set forth in SEQ ID NO: 7. Another aspect provides that the antibody contains HCDR1 as set forth in SEQ ID NO:4 and LCDR2 as set forth in SEQ ID NO: 8. Another aspect provides that the antibody contains HCDR1 as set forth in SEQ ID NO:4 and LCDR3 as set forth in SEQ ID NO: 9. Another aspect provides that the antibody contains HCDR2 as set forth in SEQ ID NO:5 and HCDR3 as set forth in SEQ ID NO: 6. Another aspect provides that the antibody contains HCDR2 as set forth in SEQ ID NO:5 and LCDR1 as set forth in SEQ ID NO: 7 Another aspect provides that the antibody contains HCDR2 as set forth in SEQ ID NO:5 and LCDR2 as set forth in SEQ ID NO: 8. Another aspect provides that the antibody contains HCDR2 as set forth in SEQ ID NO:5 and LCDR3 as set forth in SEQ ID NO: 9. Another aspect provides that the antibody contains HCDR3 as set forth in SEQ ID NO:6 and LCDR1 as set forth in SEQ ID NO: 7. Another aspect provides that the antibody contains HCDR3 as set forth in SEQ ID NO:6 and LCDR2 as set forth in SEQ ID NO: 8. Another aspect provides that the antibody contains HCDR3 as set forth in SEQ ID NO:6 and LCDR3 as set forth in SEQ ID NO: 9. Another aspect provides that the antibodycontains LCDR1 as set forth in SEQ ID NO:7 and LCDR2 as set forth in SEQ ID NO: 8. Another aspectprovides that the antibody contains LCDR1 as set forth in SEQ ID NO:7 and LCDR3 as set forth in SEQ ID NO: 9. Another aspect provides that the antibody contains LCDR2 as set forth in SEQ ID NO:8 and LCDR3 as set forth in SEQ ID NO: 9. Another aspect provides that the antibody contains HCDR1, HCDR2 and HCDR3 as set forth in SEQ ID NOs.: 4-6, respectively. Another aspect provides that the antibody contains HCDR1, HCDR2 and LCDR1 as set forth in SEQ ID NOs.: 4, 5 and 7, respectively. Another aspect provides that the antibody contains HCDR1, HCDR2 and LCDR2 as set forth in SEQ ID Nos.: 4, 5 and 8, respectively. Another aspect provides that the antibody contains HCDR1, HCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4, 5 and 9, respectively. Another aspect provides that the antibody contains HCDR1, HCDR3 and LCDR1 as set forth in SEQ ID NOs.: 4, 6 and 7, respectively. Another aspect provides that the antibody contains HCDR1, HCDR3 and LCDR2 as set forth in SEQ ID NOs.: 4, 6 and 8, respectively. Another aspect provides that the antibody contains HCDR1, HCDR3 and LCDR3 as set forth in SEQ ID NOs.: 4, 6 and 9, respectively. Another aspect provides that the antibody contains HCDR1, LCDR1 and LCDR2 as set forth in SEQ ID NOs.: 4, 8 and 9, respectively. Another aspect provides that the antibody contains HCDR1, LCDR1 and LCDR3 as set forth in SEQ ID NOs.: 4, 7 and 9, respectively. Another aspect provides that the antibody contains HCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4, 8 and 9, respectively. Another aspect provides that the antibody contains HCDR2, HCDR3 and LCDR1 as set forth in SEQ ID NOs.: 5, 6 and 7, respectively. Another aspect provides that the antibody contains HCDR2, HCDR3 and LCDR2 as set forth in SEQ ID NOs.: 5, 6 and 8, respectively. Another aspect provides that the antibody contains HCDR2, HCDR3 and LCDR3 as setforth in SEQ ID NOs.: 5, 6 and 9, respectively. Another aspect provides that the antibody containsHCDR2, LCDR1 and LCDR2 as set forth in SEQ ID NOs.: 5, 7 and 9, respectively. Another aspect PATENT ATTORNEY DOCKET NO: 51473-027WO2 provides that the antibody contains HCDR2, LCDR1 and LCDR3 as set forth in SEQ ID NOs.: 5, 7 and 9, respectively. Another aspect provides that the antibody contains HCDR2, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 5, 8 and 9, respectively. Another aspect provides that the antibody contains HCDR3, LCDR1 and LCDR2 as set forth in SEQ ID NOs.: 6, 7 and 8, respectively. Another aspect provides that the antibody contains HCDR3, LCDR1 and LCDR3 as set forth in SEQ ID NOs.: 6, 7 and 9, respectively. Another aspect provides that the antibody contains HCDR3, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 6, 8 and 9, respectively. Another aspect provides that the antibody contains LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 7-9, respectively. Yet another aspect provides that the antibody contains HCDR1, HCDR2, HCDR3 and LCDR1 as set forth in SEQ ID NOs.: 4-7, respectively. Another aspect provides that the antibody contains HCDR1, HCDR2, HCDR3 and LCDR2 as set forth in SEQ ID NOs.: 4-6 and 9, respectively. Another aspect provides that the antibody contains HCDR1, HCDR2, HCDR3 and LCDR3 as set forth in SEQ ID NOs.: 4-6 and 9, respectively. Another aspect provides that the antibody contains HCDR1, HCDR2, LCDR1 and LCDR2 as set forth in SEQ ID NOs.: 4, 5, 7 and 8, respectively. Another aspect provides that the antibody contains HCDR1, HCDR2, LCDR1 and LCDR3 as set forth in SEQ ID NOs.: 4, 5, 7 and 9, respectively. Another aspect provides that the antibody contains HCDR1, HCDR2, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4, 5, 8 and 9, respectively. Another aspect provides that the antibody contains HCDR1, HCDR3, LCDR1 and LCDR2 as set forth in SEQ ID NOs.: 4, 6, 7 and 8, respectively. Another aspect provides that the antibody contains HCDR1, HCDR3, LCDR1 and LCDR3 as set forth in SEQ ID NOs.: 4, 6, 7 and 9, respectively. Another aspect provides thatthe antibody contains HCDR1, HCDR3, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4, 6, 8 and 9,respectively. Another aspect provides that the antibody contains HCDR1, LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4, 7, 8 and 9, respectively. Another aspect provides that the antibody contains HCDR2, HCDR3, LCDR1 and LCDR2 as set forth in SEQ ID NOs.: 5-8, respectively. Another aspect provides that the antibody contains HCDR2, HCDR3, LCDR1 and LCDR3 as set forth in SEQ ID NOs.: 5- 7 and 9, respectively. Another aspect provides that the antibody contains HCDR2, HCDR3, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 5, 6, 8 and 19 respectively. Another aspect provides that the antibody contains HCDR2, LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID Nos.: 5, 7, 8 and 9, respectively. Another aspect provides that the antibody contains HCDR3, LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 6-9, respectively. Yet another aspect provides that the antibody contains HCDR1, HCDR2, HCDR3, LCDR1 and LCDR2 as set forth in SEQ ID NOs.: 4-8 respectively. Another aspect provides that the antibody contains HCDR1, HCDR2, HCDR3, LCDR1 and LCDR3 as set forth in SEQ ID NOs.: 4-7 and 9 respectively. Another aspect provides that the antibody contains HCDR1, HCDR2, HCDR3, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4-6, 8 and 9 respectively. Another aspect provides that the antibody contains HCDR1, HCDR2, LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.:4, 5, 7-9, respectively. Another aspect provides that the antibody contains HCDR1, HCDR3, LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4, 6-9, respectively. Another aspect provides that the antibody contains HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 5- 9, respectively. Yet another aspect provides that the antibody contains HCDR1, HCDR2, HCDR3, LCDR1, LCDR2 and LCDR3 as set forth in SEQ ID NOs.: 4-9, respectively. When making and using variants of any of the polypeptide sequences (e.g., CDRs) providedherein, it is understood that a given amino acid can be replaced by a residue having similar PATENT ATTORNEY DOCKET NO: 51473-027WO2 physiochemical characteristics, e.g., substituting one aliphatic residue for another (such as Ile, Val, Leu, or Ala for one another), or substitution of one polar residue for another (such as between Lys and Arg; Glu and Asp; or Gln and Asn). Other such conservative substitutions, e.g., substitutions of entire regions having similar hydrophobicity characteristics or substitutions of residues with similar side chain volume are well known. Isolated antibodies comprising conservative amino acid substitutions can be tested in any one of the assays described herein to confirm that a desired activity, as determined by the assays described elsewhere herein. Amino acids can be grouped according to similarities in the properties of their side chains (in A. L. Lehninger, in Biochemistry, second ed., pp.73-75, Worth Publishers, New York (1975)): (1) non-polar: Ala (A), Val (V), Leu (L), Ile (I), Pro (P), Phe (F), Trp (W), Met (M); (2) uncharged polar: Gly (G), Ser (S), Thr (T), Cys (C), Tyr (Y), Asn (N), Gln (Q); (3) acidic: Asp (D), Glu (E); (4) basic: Lys (K), Arg (R), His (H). Alternatively, naturally occurring residues can be divided into groups based on common side-chain properties: (1) hydrophobic: Norleucine, Met, Ala, Val, Leu, Ile, Phe, Trp; (2) neutral hydrophilic: Cys, Ser, Thr, Asn, Gln, Ala, Tyr, His, Pro, Gly; (3) acidic: Asp, Glu; (4) basic: His, Lys, Arg; (5) residues that influence chain orientation: Gly, Pro; (6) aromatic: Trp, Tyr, Phe, Pro, His, or hydroxyproline. Non- conservative substitutions will entail exchanging a member of one of these classes for another class. Particularly preferred conservative substitutions for use in the variants described herein are as follows: Ala into Gly or into Ser; Arg into Lys; Asn into Gln or into His; Asp into Glu or into Asn; Cys into Ser; Gln into Asn; Glu into Asp; Gly into Ala or into Pro; His into Asn or into Gln; Ile into Leu or into Val;Leu into Ile or into Val; Lys into Arg, into Gln or into Glu; Met into Leu, into Tyr or into Ile; Phe into Met,into Leu or into Tyr; Ser into Thr; Thr into Ser; Trp into Tyr or into Phe; Tyr into Phe or into Trp; and / or Phe into Val, into Tyr, into Ile or into Leu. In general, conservative substitutions encompass residue exchanges with those of similar physicochemical properties (i.e., substitution of a hydrophobic residue for another hydrophobic amino acid). Any cysteine residue not involved in maintaining the proper conformation of the isolated peptide as described herein can also be substituted, generally with serine, to improve the oxidative stability of the molecule and prevent aberrant crosslinking. Conversely, cysteine bond(s) can be added to the isolated peptide as described herein to improve its stability or facilitate multimerization. In some embodiments, an antibody as described herein can comprise naturally occurring amino acids commonly found in polypeptides and / or proteins produced by living organisms, e.g., Ala (A), Val (V), Leu (L), Ile (I), Pro (P), Phe (F), Trp (W), Met (M), Gly (G), Ser (S), Thr (T), Cys (C), Tyr (Y), Asn (N), Gln (Q), Asp (D), Glu (E), Lys (K), Arg (R), and His (H). In some embodiments, the antibody can comprise alternative amino acids. Non-limiting examples of alternative amino acids include, D-amino acids; beta- amino acids; homocysteine, phosphoserine, phosphothreonine, phosphotyrosine, hydroxyproline, gamma-carboxyglutamate; hippuric acid, octahydroindole-2-carboxylic acid, statine, 1,2,3,4,- tetrahydroisoquinoline-3-carboxylic acid, penicillamine (3-mercapto-D-valine), ornithine, citruline, alpha- methyl-alanine, para-benzoylphenylalanine, para-amino phenylalanine, p-fluorophenylalanine, phenylglycine, propargylglycine, sarcosine, and tert-butylglycine), diaminobutyric acid, 7-hydroxy- tetrahydroisoquinoline carboxylic acid, naphthylalanine, biphenylalanine, cyclohexylalanine, amino-isobutyric acid, norvaline, norleucine, tert-leucine, tetrahydroisoquinoline carboxylic acid, pipecolic acid,phenylglycine, homophenylalanine, cyclohexylglycine, dehydroleucine, 2,2-diethylglycine, 1-amino-1- PATENT ATTORNEY DOCKET NO: 51473-027WO2 cyclopentanecarboxylic acid, 1-amino-1-cyclohexanecarboxylic acid, amino-benzoic acid, amino- naphthoic acid, gamma-aminobutyric acid, difluorophenylalanine, nipecotic acid, alpha-amino butyric acid, thienyl-alanine, t-butylglycine, trifluorovaline; hexafluoroleucine; fluorinated analogs; azide-modified amino acids; alkyne-modified amino acids; cyano-modified amino acids; and derivatives thereof. In some embodiments, an antibody can be modified, e.g., a moiety can be added to one or more of the amino acids. In some embodiments, the antibody can comprise one or more moiety molecules, e.g., one or more moiety molecules per peptide, two or more moiety molecules per peptide, five or more moiety molecules per peptide, 10 or more moiety molecules per antibody or more moiety molecules per antibody. In some embodiments, an antibody as described herein can comprise one or more types of modifications and / or moieties, e.g., one type of modification, two types of modifications, three types of modifications or more types of modifications. Non-limiting examples of modifications and / or moieties include PEGylation; glycosylation; HESylation; ELPylation; lipidation; acetylation; amidation; end-capping modifications; cyano groups; phosphorylation; and cyclization. In some embodiments, an end-capping modification can comprise acetylation at the N-terminus, N-terminal acylation, and N-terminal formylation. In some embodiments, an end-capping modification can comprise amidation at the C-terminus, introduction of C-terminal alcohol, aldehyde, ester, and thioester moieties. Detectable Label Detectable labels disclosed herein may be conjugated or otherwise linked to any of the antibodiesdisclosed herein. Detectable labels disclosed herein may be used in conjunction with a variety ofdetection techniques known in the art, including optical imaging (e.g., fluorescence-based imaging), magnetic resonance imaging (MRI), positron-emission tomography (PET), computed tomography (CT), and ultrasound. Detectable labels include, but are not limited to, moieties that are detected directly (such as fluorescent, chemiluminescent, chromophoric, radioactive, electron-dense, magnetic, or echogenic detectable labels), as well as moieties, such as enzymes or ligands, that are detected indirectly, e.g., through an enzymatic reaction or molecular interaction. In certain embodiments, the label moiety may include an opacifying label moiety including bromine, iodine, barium, lanthanide, or bismuth. The opacifying label moiety may act as a contrast agent in radiography or tomography including CT scans. Exemplary detectable labels suitable for use with each of these detection techniques are provided below. For fluorescent detectable labels, preferred fluorophores typically exhibit good quantum yields, long excited state lifetimes, and large extinction coefficients; are resistant to collisional quenching and bleaching; and should be easily conjugated to a peptide. In some instances, preferred fluorophores function in the near infrared (NIR) spectral region. Examples of illustrative fluorophores include pyrrolopyrrole cyanines, hydrocyanines, cyanines, oxazines, thiazines, porphyrins, phthalocyanines, borondipyrromethanes, tetraarylazadipyrromethenes, isobenzofurans, isothianaphthenes, xanthenes, fluorescent infrared-emitting polynuclear aromatic hydrocarbons such as violanthrones, near IR squaraine dyes. Specific fluorophores include, without limitation, fluorescein isothiocyanate, 5-FAM (5- carboxyfluorescein), 6-FAM (6-carboxyfluorescein), 5,6-FAM, 7-hydroxycoumarin-3-carboxamide, 6-chloro-7-hydroxycoumarin-3-carboxamide, dichlorotriazinylaminofluorescein, tetramethylrhodamine-5(and -6)-isothiocyanate, 1,3-bis- (2-diakylamino-5-thienyl)-substituted squarines, the succinimidyl esters PATENT ATTORNEY DOCKET NO: 51473-027WO2 of 5 (and 6) carboxyfluoroscein, 5 (and 6)-carboxytetramethylrhodamine, and 7-amino-4-methylcoumarin- 3-acetic acid. In some embodiments, the fluorophore is a near-infrared fluorophore. In some embodiments, the fluorophore absorbs light at about 800 nm. In some embodiments, the fluorophore absorbs light at about 647 nm. In some embodiments, the fluorescent detectable label is LI-COR IRDye® 800CW Maleimide. In some embodiments, the fluorescent detectable label is LI-COR IRDye® 800CW NHS Ester. Genetically encoded fluorescent detectable labels that may be used in the methods and uses of this disclosure include, but are not limited to, any one of the following: near-infrared fluorescent protein (iRFP; e.g., iRFP670, iRFP702, iRFP713, iRFP682, iRFP713, and iRFP720), infrared fluorescent protein (IFP; e.g., IFP1.4, IFP2.0, WiPhy), green fluorescent protein (GFP), yellow fluorescent protein (YFP), blue fluorescent protein (BFP), cyan fluorescent protein (CFP), red fluorescent protein (RFP), mCherry, dsRed, luciferase (Luc), β-galactosidase (lacZ), chloramphenicol acetyltransferase (CAT), mTagBFP2, mTurquoise2, mCerulean3, EGFP, mWasabi, Superfolder GFP, mNeonGreen, mClover3, Venus, Citrine, mKOκ, tdTomato, TagRFP-T, mRuby3, mScarlet, FusionRed, mCherry, mStable, mKate2, mMaroon1, mCardinal, T-Sapphire, mCyRFP1, LSSmOrange, or mBeRFP. Additional detectable labels suitable for optical detection include fluorophores such as rare earth chelates or fluorescein and its derivatives, rhodamine and its derivatives, dansyl, umbelliferone, luceriferases, e.g., firefly luciferase and bacterial luciferase, luciferin, 2,3-dihydrophthalazinediones, horseradish peroxidase (HRP), alkaline phosphatase, β-galactosidase, glucoamylase, lysozyme,saccharide oxidases, e.g., glucose oxidase, galactose oxidase, and glucose-6-phosphatedehydrogenase, heterocyclic oxidases such as uricase and xanthine oxidase, coupled with an enzyme that employs hydrogen peroxide to oxidize a dye precursor such as HRP, lactoperoxidase, or microperoxidase. Radioactive detectable labels include radioactive elements whose radioactivity can be detected, e.g., via PET imaging. Radioactive detectable labels may include molecules, complexes, chelates, nanoparticles, etc., which contain radioactive elements suitable for detection. Suitable radioactive elements include, but are not limited to, a radioactive isotope of carbon (e.g.,11C), nitrogen (e.g.,13N), oxygen(e.g.,15O), fluorine (e.g.,18F), gallium (Ga) (e.g.,67Ga,68Ga), copper (e.g.,64Cu,67Cu), manganese(e.g.,52Mn), iron (e.g.,59Fe), zirconium (e.g.,89Zr), scandium (e.g.,44Sc), indium (e.g.,111In), yttrium (e.g.,90Y) rubidium (e.g.,82Rb), cobalt (e.g.,60Co or59Co), lutetium (e.g.,177Lu), gadolinium (e.g.,153Gd,155Gd,157Gd), bismuth (e.g.,213Bi), strontium (e.g.,90Sr), actinium (e.g.,225Ac), or technetium (e.g.,99mTc). In some instances, the radioactive half-life of the radioactive element may be on the order of minutes, hours, days, or weeks. In particular instances, the radioactive half-life of the radioactive element may be similar to the biological half-life of the antibodies described herein, e.g., on the order of tens of hours (e.g., from 1-5 hours, from 5-10 hours, from 10-15 hours, from 15-20 hours, or from 20-24 hours) to days (e.g., about 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 days). In some instances, the radioactive half-life of the radioactive element is no longer than four days, no longer than one day, no longer than 12 hours, no longer than 6 hours, no longer than 3 hours, no longer than 2.5 hours, no longer than 120 min, no longer than 100 min, no longer than 80 min, or no longer than 70 min. Magnetic detectable labels, which may be suitable for detection using MRI, include spin labelssuch as iodine-123, iodine-131, indium-111, fluorine-19, carbon-13, nitrogen-15, oxygen-17, gadolinium, PATENT ATTORNEY DOCKET NO: 51473-027WO2 fludeoxyglucose, manganese or iron. A magnetic label moiety may include a peptide, nucleotide, saccharide, or small molecule wherein one or more non-radioactive atoms is replaced with a radioactive atom. For example, the probe may include fludeoxyglucose, wherein the sugar includes an18F atom. Magnetic detectable labels also include magnetic nanoparticles, including, but not limited to nanoparticles containing Fe3O4, γ Fe2O3, CoFe2O4, MnFe2O4, and NiFe2O4. Metallic nanoparticles may further include polymeric coating materials, such as dextran, carboxymethylated dextran, carboxydextran, chitosan, starch, PEG, heparin, albumin, arabinogalactan, glycosaminoglycan, sulfonated styrene–divinylbenzene, organic siloxane, polyvinyl alcohol, poloxamers, and polyoxamines, e.g., to prevent aggregation. The polymeric coating may be further functionalized to allow conjugation to targeting molecules, e.g., the antibodies disclosed herein. Commonly used magnetic detectable labels for detection using MRI include gadolinium-based contrast agents. These contrast agents include gadolinium, such as gadoterate, gadobutrol, gadoteridol, gadopentetate, gadobenate, gadopentetic acid dimeglumine, gadoversetamide, gadodiamide, gadofoveset, gaocoletic acid, gadomelitol, gadomer 17. Metallic nanoparticles may also be used as labeling moieties for X-ray and CT. Metallic nanoparticles suitable for use as labeling moieties for CT may include Ag, Cu, Fe, Pt, Au, Bi, Pd, Ta, W, Gd, and Yb. These metallic nanoparticles may further include polymeric coating materials, such as dextran, carboxymethylated dextran, carboxydextran, chitosan, starch, PEG, heparin, albumin, arabinogalactan, glycosaminoglycan, sulfonated styrene–divinylbenzene, organic siloxane, polyvinyl alcohol, poloxamers, and polyoxamines, e.g., to prevent aggregation. The polymeric coating may befurther functionalized to allow conjugation to targeting molecules, e.g., the antibodies disclosed herein.Opacifying detectable labels include compounds having bromine, iodine, barium, lanthanides or bismuth Suitable iodine-containing opacifying detectable labels include, for example, compounds that contain triiodine aromatic compounds, such as, for example, amidotrizoate, iohexol, iopamidol, iopanoic acid, iopodinic acid, iopromide, iopronic acid, iopydone, iotalaminic acid, iopentol, ioversol, ioxaglat, iotrolan, iodixanol, iotroxinic acid, ioxaglinicic acid and ioxitalaminic acid (INN). Trade names for x-ray contrast media that contain iodine are Urografin® (Schering), Gastrografin® (Schering), Biliscopin® (Schering), Ultravist® (Schering) and Isovist® (Schering). Opacifying detectable labels may also include metal complexes, for example Gd-DTPA (Magnevist® (Schering)), Gd-DOTA (Gadoterate, Dotarem), Gd- HP-DO3A (Gadoteridol, Prohance® (Bracco)), Gd-EOB-DTPA (Gadoxetat, Primavist), Gd-BOPTA (Gadobenat, MultiHance), Gd-DTPA-BMA (Gadodiamide, Omniscan® (Amersham Health), Dy-DTPA- BMA, Gd-DTPA-polylysine, and Gd-DTPA-cascade polymers. Echogenic detectable labels enhance contrast for ultrasounds. Echogenic detectable labels include microbubbles, including, but not limited to perflutren lipid microspheres, perfluorocarbon emulsions, and perflexane lipid microspheres. Microbubbles may further be encapsulated in a lipid monolayer, e.g., having a polyethylene glycol shell, which may be further functionalized or used to conjugate to targeting molecules, e.g., the antibodies disclosed herein. Conjugation Methods Detectable labels moieties may be linked to the antibodies disclosed herein via non-covalent orcovalent methods. For example, affinity binding pairs may be used to link two or more moieties (e.g., alabeling moiety and an antibody) non-covalently. Any suitable affinity binding pair known in the art or PATENT ATTORNEY DOCKET NO: 51473-027WO2 described herein may be used. Exemplary, non-limiting affinity binding pairs include biotin-biotin binding protein (e.g., biotin-streptavidin, biotin-avidin, and biotin-NeutrAvidin™), antigen-antibody or antigen binding fragment, ligand-receptor, hapten-anti-hapten, and Ig binding protein-Ig. Biotin binding proteins, including avidin, streptavidin, and NeutrAvidin™, are commercially available and can be conjugated using routine approaches (including covalent linking methods disclosed herein) to proteins or chemical moieties (e.g., a polymer, e.g., a polyether such as polyethylene glycol (PEG)). Detectable labels may also be linked to antibodies covalently using methods known in the art, for example, a cycloaddition (e.g., an azide-alkyne Huisgen cycloaddition (e.g., a copper(I)-catalyzed azide- alkyne cycloaddition (CuAAC) or a strain-promoted azide-alkyne cycloaddition (SPAAC))), a pericyclic reaction, amide or thioamide bond formation, sulfonamide bond formation, a Diels-Alder reaction, alcohol or phenol alkylation, a condensation reaction, disulfide bond formation, or a nucleophilic substitution. To covalently link detectable labels and antibodies disclosed herein, the labeling moiety and / or antibody may be functionalized by the addition of a conjugating moiety, including at least one functional group that is capable of undergoing a conjugation reaction, for example, any conjugation reaction described in the preceding paragraph. The conjugation moiety can include, without limitation, a 1,3- diene, an alkene, an alkylamino, an alkyl halide, an alkyl pseudohalide, an alkyne, an amino, an anilido, an aryl, an azide, an aziridine, a carboxyl, a carbonyl, an episulfide, an epoxide, a heterocycle, an organic alcohol, an isocyanate group, a maleimide, a succinimidyl ester, a sulfosuccinimidyl ester, a sulfhydryl, a thiol, or a thioisocyanate group. Linkers In some embodiments, the antibody is conjugated to the detectable label by way of a linker. In some embodiments, the linker is a bond, such as a covalent bond. The covalent bond may be a non- cleavable linkage or a cleavable linkage. The non-cleavable linkage can include an amide bond or phosphate bond, and the cleavable linkage can include a disulfide bond, acid-cleavable linkage, ester bond, anhydride bond, biodegradable bond, or enzyme-cleavable linkage. In some embodiments, the linker includes a polymer, a polypeptide, a polysaccharide, a polynucleotide, or a combination thereof. The length and composition of the linker can be adjusted based on the detectable label and the antibody selected. Suitable linkers include, but are not limited to, oligonucleotides such as those discussed above, including a polynucleotide, a polymer including but not limited to poly(ethylene glycol) (MW: 500 Da to 20,000 Da); a polypeptide, or combinations thereof; polysaccharides, including but not limited to, dextran (MW: 1,000 Da to 2,000,000 Da), or combinations thereof. In some embodiments, the linker is one or more ethylene glycol (EG) units, more preferably two or more EG units (i.e., polyethylene glycol (PEG)). The linker may include between about 1 and about 100 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, or 100) PEG units. In some embodiments, the linker may be a PEG linker having between about 20 and about 80, between about 30 and about 70, or between about 40 and about 60 PEG units. In some embodiments, the number of PEG units is between PATENT ATTORNEY DOCKET NO: 51473-027WO2 24 and 50 units (e.g., between 24 and 45, 24 and 40, 24 and 35, 24 and 30, 30 and 50, 35 and 50, 40 and 50, and 45 and 50 units). As discussed above, in some embodiments, the linker is a polynucleotide which includes a string of nucleic acids. The linker can be any sequence, for example, the sequence of the oligonucleotide can be a random sequence, or a sequence specifically chosen for its molecular or biochemical properties (e.g., highly polar). In some embodiments, the linker includes 20 one or more series of consecutive adenine (A), cytosine (C), guanine (G), thymine (T), uracil (U), or analog thereof. In some embodiments, the linker consists of a series of consecutive adenine (A), cytosine (C), guanine (G), thymine (T), uracil (U), or analog thereof. In some embodiments, the string of polynucleotide includes between 1 and 50 nucleic acid residues. In some embodiments, the string of nucleic acids includes between 5 and 30 nucleic acid residues. In some embodiments, the linker includes one or more guanines, for example between 1-10 guanines. In some embodiments, the linker is an oligonucleotide that includes a polypeptide. The linker can have any amino acid sequence, for example, the sequence of the oligonucleotide can be a random sequence, or a sequence chosen for its molecular or biochemical properties (e.g., high flexibility). In some embodiments, the linker includes a series of glycine residue to form a polyglycine linker. In some embodiments, the linker includes an amino acid sequence of (Gly)n, wherein n may be between 2 and 20 residues. Examples of polyglycine linkers include but are not limited to GGG, GGGA (SEQ ID NO: 12),GGGG (SEQ ID NO: 13), GGGAG (SEQ ID NO: 14), GGGAGG (SEQ ID NO: 15), GGGAGGG (SEQ IDNO: 16), GGAG (SEQ ID NO: 17),GGSG (SEQ ID NO: 18), AGGG (SEQ ID NO: 19), SGGG (SEQ ID NO: 20), GGAGGA (SEQ ID NO: 21), GGSGGS (SEQ ID NO: 22), GGAGGAGGA (SEQ ID NO: 23), GGSGGSGGS (SEQ ID NO: 24), GGAGGAGGAGGA (SEQ ID NO: 25), GGSGGSGGSGGS (SEQ ID NO: 26), GGAGGGAG (SEQ ID NO: 27), GGSGGGSG (SEQ ID NO: 28), GGAGGGAGGGAG (SEQ ID NO: 29), GGSGGGSGGGSG (SEQ ID NO: 30), GGGGAGGGGAGGGGA (SEQ ID NO: 31), and GGGGSGGGGSGGGGS (SEQ ID NO: 32). DIAGNOSTIC METHODS The disclosure also provides methods for identifying atherosclerotic plaques in a subject by either administering to a subject the antibody conjugated to a detectable label described herein and then detecting the label. The disclosure also provides methods of identifying atherosclerotic plaques or by contacting a sample obtained from the subject with the antibody conjugated to a detectable label described herein and detecting the label. The disclosure provides methods of detecting the presence of an atherosclerotic plaque in a subject. In some embodiments, the method includes administering the any one of the compositions described herein including an antibody conjugated to a detectable label to the subject; and then detecting the presence of the detectable label present in the subject; wherein the presence of the detectable label indicates the presence of an atherosclerotic plaque in the subject. In some embodiments, the detection of the presence of the detectable label is performed between 1 min and 10 hours after administering thecomposition to the subject, for example, between 1 min and 10 min, 1 min and 30 minutes, 1 minute and1 hour, 1 minute and 5 hours, 1 hour and 5 hours, 1 hour and 8 hours, 1 hour and 10 hours, 4 hours and PATENT ATTORNEY DOCKET NO: 51473-027WO2 10 hours, 6 hours and 10 hours, or 8 hours and 10 hours). In some embodiments, the detection of the presence of the detectable label is performed between 1 min and 10 hours after administering the composition to the subject, for example, between 1 min and 10 min, 1 min and 30 minutes, 1 minute and 1 hour, 1 minute and 5 hours, 1 hour and 5 hours, 1 hour and 8 hours, 1 hour and 10 hours, 4 hours and 10 hours, 6 hours and 10 hours, or 8 hours and 10 hours). In some embodiments, the cardiovascular disease is aortic valve stenosis, aortic valve sclerosis, or atherosclerosis. The detectable label may be detected using any method known to one of skill in the art. In some embodiments, the detectable label is detected using radiography, ultrasound, or tomography. For example, the detectable label may be detected using magnetic resonance imaging (MRI). In some embodiments, the detectable label is detected using computed tomography (CT). In some embodiments, the detectable label is detected using positron emission tomography (PET). In some embodiments, the detectable label is detected using ultrasound. In some embodiments the detectable label is detected using optical coherence tomography. In some embodiments, the detectable label is detected using fluorescence molecular tomography. In various embodiments, the composition to be administered in the disclosed methods are formulated for delivery via any route of administration. For example, the methods include administration via an aerosol, nasal, oral, transmucosal, transdermal, parenteral or enteral route. “Parenteral” refers to a route of administration that is generally associated with injection, including intraorbital, infusion, intraarterial, intracapsular, intracardiac, intradermal, intramuscular, intraperitoneal, intrapulmonary,intraspinal, intrasternal, intrathecal, intrauterine, intravenous, subarachnoid, subcapsular, subcutaneous,transmucosal, or transtracheal. Via the parenteral route, the compositions may be in the form of solutions or suspensions for infusion or for injection, or as lyophilized powders. Via the parenteral route, the compositions may be in the form of solutions or suspensions for infusion or for injection. Via the enteral route, the pharmaceutical compositions can be in the form of tablets, gel capsules, sugar-coated tablets, syrups, suspensions, solutions, powders, granules, emulsions, microspheres or nanospheres or lipid vesicles or polymer vesicles allowing controlled release. Typically, the compositions are administered by injection. PHARMACEUTICAL COMPOSITIONS In various embodiments, the present disclosure provides a pharmaceutical composition for use in the methods. The pharmaceutical composition includes the anti-oxLDL antibody or fragment thereof conjugated to a detectable label and a pharmaceutically acceptable carrier. “Pharmaceutically acceptable carrier” as used herein refers to a pharmaceutically acceptable material, composition, or vehicle that is involved in carrying or transporting a compound of interest from one tissue, organ, or portion of the body to another tissue, organ, or portion of the body. For example, the carrier may be a liquid or solid filler, diluent, excipient, solvent, or encapsulating material, or a combination thereof. Examples of excipients include but are not limited to starches, sugars, microcrystalline cellulose, diluents, granulating agents, lubricants, binders, disintegrating agents, wetting agents, emulsifiers, coloring agents, release agents, coating agents, sweetening agents, flavoring agents, perfuming agents, preservatives,antioxidants, plasticizers, gelling agents, thickeners, hardeners, setting agents, suspending agents,surfactants, humectants, carriers, stabilizers, and combinations thereof. Generally, each component of PATENT ATTORNEY DOCKET NO: 51473-027WO2 the carrier must be “pharmaceutically acceptable” in that it must be compatible with the other ingredients of the formulation. It must also be suitable for use in contact with any tissues or organs with which it may come in contact, meaning that it must not carry a risk of toxicity, irritation, allergic response, immunogenicity, or any other complication that excessively outweighs its therapeutic benefits. The pharmaceutical compositions may be delivered in a therapeutically or diagnostically effective amount. The precise diagnostically or therapeutically effective amount is that amount of the composition that will yield the most effective results in terms of efficacy of detection of atherosclerosis in a given subject. This amount will vary depending upon a variety of factors, including but not limited to the characteristics of the compound (including activity, pharmacokinetics, pharmacodynamics, and bioavailability), the physiological condition of the subject (including age, sex, disease type and stage, general physical condition, responsiveness to a given dosage, and type of medication), the nature of the pharmaceutically acceptable carrier or carriers in the formulation, and the route of administration. One skilled in the clinical and pharmacological arts will be able to determine a therapeutically effective amount through routine experimentation, for instance, by monitoring a subject's response to administration of a compound and adjusting the dosage accordingly. For additional guidance, see Remington: The Science and Practice of Pharmacy (Gennaro ed.20th edition, Williams & Wilkins PA, USA) (2000). ANTIBODY PREPARATION In some embodiments, the aforementioned methods involve antibodies that bind to a specificantigen epitope, where the antibodies contain one or more defined sequences. For example, modernrecombinant library technology is used to prepare therapeutic antibodies against native ApoB or oxidized ApoB. While murine hybridomas cells produce large amounts of identical antibodies, these non-human antibodies are recognized by human body as foreign, and as a consequence, their efficacy and plasma half-lives are decreased in addition to eliciting allergic reactions. To solve this problem, one approach is to make chimeric antibodies where the murine variable domains of the antibody are transferred to human constant regions resulting in an antibody that is mainly human. A further refinement of this approach is to develop humanized antibodies where the regions of the murine antibody that contacted the antigen, the Complementarity Determining Regions (CDRs) are transferred to a human antibody framework, resulting in a humanized antibody. Another approach is to produce completely human antibodies using recombinant technologies, which do not rely on immunization of animals to generate the specific antibody. Instead, recombinant libraries comprise a huge number of pre-made antibody variants and it is likely that a library will have at least one antibody specific for any antigen. A phage display system may be used where antibody fragments are expressed, displayed, as fusions with phage coat proteins on the surface of filamentous phage particles, while the phage display system simultaneously carries the genetic information encoding the displayed molecule. Phage displaying antibody fragments specific for a particular antigen may be selected through binding to the antigen in question. Isolated phage may then be amplified and the gene encoding the selected antibody variable domains may optionally be transferred to other antibody formats as e.g., full length immunoglobulin and expressed in high amounts using appropriate vectors and host cells well known in the art. The format of displayed antibody specificities onphage particles may differ. The most commonly used formats are Fab and single chain (scFv) bothcontaining the variable antigen binding domains of antibodies. The single chain format is composed of a PATENT ATTORNEY DOCKET NO: 51473-027WO2 variable heavy domain (VH) linked to a variable light domain (VL) via a flexible linker. Before use as analytical reagents, or therapeutic agents, the displayed antibody specificity is transferred to a soluble format, e.g., Fab or scFv, and analyzed as such. In later steps the antibody fragment identified to have desirable characteristics may be transferred into yet other formats such as full-length antibodies. Antibody Production from Hybridomas The cell fusions are accomplished by standard procedures well known to those skilled in the field of immunology. Fusion partner cell lines and methods for fusing and selecting hybridomas and screening for mAbs are well known in the art. See, e.g., Ausubel, Harlow, and Colligan, the contents of which references are incorporated entirely herein by reference. An anti-MDA-ApoB100 antibody, or an anti-apo(a) antibody, can be produced in large quantities by injecting hybridoma or transfectoma cells secreting the antibody into the peritoneal cavity of mice and, after appropriate time, harvesting the ascites fluid which contains a high titer of the mAb, and isolating the mAb therefrom. For such in vivo production of the mAb with a non-murine hybridoma (e.g., rat or human), hybridoma cells are preferably grown in irradiated or athymic nude mice. Alternatively, the antibodies can be produced by culturing hybridoma or transfectoma cells in vitro and isolating secreted mAb from the cell culture medium or recombinantly, in eukaryotic or prokaryotic cells. Recombinant Expression of Antibodies Recombinant murine or chimeric murine-human or human-human antibodies that inhibit oxidizedLDL can be provided according to the present disclosure using known techniques based on the teaching provided herein. See, e.g., Ausubel et al., eds. Current Protocols in Molecular Biology, Wiley Interscience, N.Y. (1987, 1992, 1993); and Sambrook et al. Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press (1989). The DNA encoding an anti- oxLDL antibody can be genomic DNA or cDNA which encodes at least one of the heavy chain constant region (Hc), the heavy chain variable region (Hc), the light chain variable region (Lv) and the light chain constant regions (Lc). A convenient alternative to the use of chromosomal gene fragments as the source of DNA encoding the murine V region antigen-binding segment is the use of cDNA for the construction of chimeric immunoglobulin genes, e.g., as reported by Liu et al. (Proc. Natl. Acad. Sci., USA 84:3439 (1987) and J. Immunology 139:3521 (1987). The use of cDNA requires that gene expression elements appropriate for the host cell be combined with the gene in order to achieve synthesis of the desired protein. The use of cDNA sequences is advantageous over genomic sequences (which contain introns), in that cDNA sequences can be expressed in bacteria or other hosts which lack appropriate RNA splicing systems. EXAMPLES The following examples are provided to better illustrate the claimed invention and are not to be interpreted as limiting the scope of the invention. To the extent that specific materials are mentioned, it is merely for purposes of illustration and is not intended to limit the invention. One skilled in the art maydevelop equivalent means or reactants without the exercise of inventive capacity and without departingfrom the scope of the invention. PATENT ATTORNEY DOCKET NO: 51473-027WO2 Example 1: Orticumab conjugated to a fluorescent label to detect atherosclerosis This example demonstrates that orticumab conjugated to a detectable label can be used ex vivo and in vivo to identify atherosclerosis is a subject. Ex Vivo A fluorophore (800nm) was conjugated to orticumab or an IgG1 control antibody to generate orticumab-800 or Control-800. These two antibodies both included the detectable label, and both had been confirmed to have the capacity to bind ox-LDL. Murine atherosclerotic en face aorta and human femoral artery samples were stained ex vivo with orticumab-800. Both samples were positive for 800 nm signal when imaged with fluorescent molecular reflectance (FIGs.1A and 1B). The murine orticumab-800 signal colocalized generally with atherosclerotic plaque stained by Oil Red O. In Vivo The in vivo experiments utilized fluorescence molecular tomography (FMT) imaging to visualize the near-infrared (NIRF) detectable labels. Ldlr- / -mice (n=6 per group) that were fed a high fat diet for up to 45 weeks were intravenously injected with orticumab or the IgG1 control conjugated to the fluorophore (800nm). After 4 hours, the mice were imaged by FMT with an excitation of 800nm. After imaging, the signal for all animals were analyzed in TrueQuant software with the molar concentration of 800nm signalin the aortic region was determined. The ROI signal for mice that were administer the orticumab-800 was4 times higher than the control group (mean 107.0pmol vs.26.85pmol, p=0.0495, unpaired t-test with Welch’s correction) (FIG.2A). CT imaging was also performed in animals immediately after FMT to generate reference skeletal data for anatomical FMT signal figures. Orticumab corresponded with anatomical features of the murine aorta, and when compared to this control animal, confirmed specificity of Orticumab-800 (FIG.2B). When comparing the aorta from injected animals prepared en face, 800nm signal was much stronger in Orticumab injected animals compared to control and signal localized to the aortic arch. This data shows orticumab-800 binds mouse atherosclerotic lesions in vivo as detectable through live Example 2. : Orticumab conjugated to a fluorescent label for detection of oxidized low-density lipoprotein Orticumab was labelled with different fluorophores using two different protocols and the resulting degree of labelling of orticumab and subsequent binding affinity to ox-LDL was measured. Multiple fluorophores were tested with various protocols to optimise molar ratio of reaction and incubation time. The subsequent binding affinity of the orticumab labelled with a fluorophore that fluoresces at 800 nm with a maleimide conjugation site which reacts to free sulfhydryl groups (LI-COR® IRDye® 800CW Maleimide (LI-COR 800 Mal)), and orticumab labelled with a fluorophore that fluoresces at 800 nm with an ester conjugation site that reacts with primary and secondary amines (LI-COR® IRDye® 800CW NHS Ester (LICOR 800 Lys)) with ox-LDL was measured in comparison to unlabelled orticumab. Enzyme-linked immunosorbent assays (ELISAs) were performed against ox-LDL and detection was performedusing anti-CH1-biotin, where the labelled orticumab was in an amount of 2 µg / mL and the ox-LDL was in PATENT ATTORNEY DOCKET NO: 51473-027WO2 an amount of 5 µg / mL. The resulting measured absorbance at 450 nm is shown in FIGS.3A and 3B. Orticumab labelled with LICOR 800 Mal had a degree of labelling of 0.17 fluorophores to antibody, using the May 12, 2024 protocol. Orticumab labelled with LICOR 800 Lys had a degree of labelling of 2.82 fluorophores to antibody, using the May 12, 2024 protocol. Orticumab labelled with LICOR 800 Lys had a degree of labelling of 2 fluorophores to antibodies using the June 12, 2024, protocol. For translational purposes, it was also demonstrated that labelled orticumab could bind to human atherosclerosis lesions ex vivo. A human femoral artery sample was incubated with orticumab labelled with LICOR 800 Lys (orticumab-800), washed and then imaged. This experiment demonstrated binding of orticumab-800 to the sample when exciting at 790 nm+ (FIG.4). For in vivo studies, prior to injection, each labelled antibody and unlabelled antibody was run in a gel and read fluorescently (800 nm) (FIG.5A) and stained with Coomassie (FIG.5B) to visualise the protein and confirm the presence of the fluorescent tag. Unlabelled antibody was used as a control. A band was confirmed at ~150 kDa. A sandwich ox-LDL ELISA was also performed, coating with antibodies in a dilution series and adding ox-LDL (FIG.5C) to confirm the orticumab was functional. Anti-ApoB-Biotin used for detection. For in vivo imaging experiments, ldlr- / -mice were fed high fat diet from 10 weeks old for 38-44 weeks (n=6 per group). Orticumab and the IgG1 control were labelled with LICOR 800 Lys.50 µg of orticumab labelled with LICOR 800 Lys (orticumab-800) or 50 µg of IgG1 labelled with LICOR 800 Lys (IgG1-800) were intravenously injected into the mice. The mice were them imaged using fluorescencemolecular tomography (FMT) 4 hours post-injection, using 790 nm excitation (FIG. 6A and FIG. 6B). Twomice were imaged with computed tomography (CT) in order to be able to reference the skeletal data (FIGS.7A-7D). Following the imaging, the aorta was harvested for ex vivo studies. FMT images were collected to measure the total fluorescence signal in the region of interest of the aorta for mice that were administered labelled orticumab (n=6) in comparison to mice that were administered labelled IgG1 (n=6). The aorta from imaged animals was prepared en face and imaged with FMT to confirm signal presence in the vessel (FIG.8B). Data was analysed in TrueQuant software using a region of interest (ROI) of the aortic region to determine the pmol concentration of the fluorophore (FIG.8A). The signal was thresholded to the background signal of each individual mouse and adjusted to account for degree of labelling of each labelled antibody. The Data was analysed using an unpaired two-tailed students t-test with Welch correction, p=0.0386 and error bars represent standard error from the mean (FIG.8A). To show ex vivo retention of the fluorescent signal in the aorta from FMT imaged mice, sections of the aorta were made from injected animals and imaged by confocal microscopy comparing the 5 µm adjacent sections from animals that were administered the labelled orticumab to sections from animals that were stained with Oil Red O, which stains fat (FIG.9). Some differences were seen, with slightly higher 800 nm signal in the animals injected with the labelled orticumab. To further study ex vivo retention, orticumab was labelled with a 647 nm fluorophore for better detection using the confocal microscope. Mice were injected with 50 µg of orticumab labelled with the 647 nm fluorophore (orticumab-647) or IgG1 labelled with the 647 nm fluorophore (control-647).4 hours lateranimals were culled, perfused with PBS and 2% formalin, aortas extracted and prepared en face. Aortaswere mounted on slides and imaged by confocal microscopy using both white light (FIG.10B ) and PATENT ATTORNEY DOCKET NO: 51473-027WO2 fluorescence imaging (FIG.10C and FIG.10D). An ELISA was performed to demonstrate retention of function of the orticumab after labelling with the fluorophore (FIG.10A). The results of this experiment demonstrated that orticumab could be labelled with near-infrared fluorophores, retaining function and binding mouse and human atheroma ex vivo samples. The FMT images demonstrated that orticumab preferentially bound murine atherosclerosis in vivo, compared to a labelled non-specific antibody. The signal from the fluorophore labelled orticumab was observed in the aortic region and confirmed to be present in the aorta. Through confocal Z-stacking experiments, it was demonstrated that orticumab targets lesions protruding into the vessel, beneath the endothelium. OTHER EMBODIMENTS Various modifications and variations of the described disclosure will be apparent to those skilled in the art without departing from the scope and spirit of the disclosure. Although the disclosure has been described in connection with specific embodiments, it should be understood that the disclosure as claimed should not be unduly limited to such specific embodiments. Indeed, various modifications of the described modes for carrying out the disclosure that are obvious to those skilled in the art are intended to be within the scope of the disclosure. Other embodiments are in the claims.

Claims

PATENT ATTORNEY DOCKET NO: 51473-027WO2 What is claimed is: CLAIMS 1. A composition comprising an antibody conjugated to one or more detectable label, wherein the antibody comprises heavy chain complementarity determining regions (HCDRs) HCDR1, HCDR2, and HCDR3 comprising the sequences of SEQ ID NOs: 4, 5 and 6, respectively, and light chain complementarity determining regions (LCDRs) LCDR1, LCDR2, and LCDR3 comprising the sequences of SEQ ID NOs: 7, 8 and 9, respectively.

2. The antibody of either of claim 1, wherein the antibody comprises a variable heavy region (VH) of SEQ ID NO.: 10, a variable light region (VL) of SEQ ID NO.: 11, or both.

3. The composition of claim 1 or 2, wherein the antibody is conjugated to the label by way of a bond.

4. The composition of claim 1 or 2, wherein the antibody is conjugated to the label by way of a linker.

5. The composition of claim 4, wherein the linker comprises a polymer, a polypeptide, a polysaccharide, a polynucleotide, or a combination thereof.

6. The composition of any one of claims 1-5, wherein the detectable label comprises a fluorescent, chemiluminescent, chromophoric, radioactive, electron-dense, magnetic, or echogenic label.

7. The composition of claim 6, wherein the detectable label comprises a magnetic label.

8. The composition of claim 7, wherein the detectable label comprises fluoxyglucose.

9. The composition of claim 7, wherein the detectable label comprises gadolinium.

10. The composition of claim 7, wherein the detectable label comprises iohexol.

11. The composition of claim 7, wherein the detectable label is a near-infrared fluorophore.

12. The composition of claim 11, wherein the near-infrared fluorophore absorbs light at 800 nm.

13. A pharmaceutical composition comprising the composition of any one of claims 1-12 and one or more pharmaceutically acceptable excipients.

14. A method for detecting the presence of an atherosclerotic plaque in a subject, wherein the method comprises: (i) administering the composition of any one of claims 1-13 to the subject; andPATENT ATTORNEY DOCKET NO: 51473-027WO2 (ii) detecting the presence of the detectable label present in the subject; wherein the presence of the detectable label indicates the presence of an atherosclerotic plaque in the subject.

15. A method of diagnosing a cardiovascular disease in a subject, the method comprising: (i) administering the composition of any one of claims 1-13 to the subject; and (ii) detecting the presence of the detectable label present in the subject, wherein the presence of the detectable label indicates the subject has a cardiovascular disease.

16. The method of claim 15, wherein the cardiovascular disease comprises aortic valve stenosis, aortic valve sclerosis, or atherosclerosis.

17. The method of any one of claims 14-16, wherein the composition is administered subcutaneously or intravenously.

18. A method for detecting the presence of an atherosclerotic plaque in a subject, wherein the method comprises: (i) obtaining a sample from the subject; (ii) contacting the sample with the composition of any one of claims 1-13; and (iii) detecting the presence of the detectable label present in the sample, wherein the presence of the detectable label indicates the presence of an atherosclerotic plaque.

19. The method of claim 18, wherein the sample is a blood sample, serum sample, or tissue sample.

20. The method of any one of claims 14-19, wherein detecting the presence of the detectable label is performed using radiography, ultrasound, or tomography.

21. The method of any one of claims 14-19, wherein detecting the presence of the detectable label is performed using magnetic resonance imaging.

22. The method of claim 20, wherein detecting the presence of the detectable label is performed using intravascular ultrasound.

23. The method of claim 20, wherein detecting the presence of the detectable label is performed using fluorescence molecular tomography, optical coherence tomography, computed tomography, or a positron emission tomography.

24. The method of any one of claims 14-23, wherein the subject is a human.

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