{"id":5690,"date":"2020-08-11T09:05:39","date_gmt":"2020-08-11T13:05:39","guid":{"rendered":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/?p=5690"},"modified":"2024-10-31T09:02:42","modified_gmt":"2024-10-31T13:02:42","slug":"vhh-antibodies-hope-for-covid-treatment","status":"publish","type":"post","link":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/trending-topics\/vhh-antibodies-hope-for-covid-treatment\/","title":{"rendered":"Heavy-Chain Variable (VHH) Antibodies: Diagnosis, Treatment and Prevention of Covid-19 and Novel Viral Infections"},"content":{"rendered":"\n\n\n\t<div class=\"dkpdf-button-container\" style=\" text-align:right \">\n\n\t\t<a class=\"dkpdf-button\" href=\"\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts\/5690?pdf=5690\" target=\"_blank\"><span class=\"dkpdf-button-icon\"><i class=\"fa fa-file-pdf-o\"><\/i><\/span> Download PDF<\/a>\n\n\t<\/div>\n\n\n\n\n\n<style>.post h3 {color:#009fe3;font-size:17.5px;line-height:28px;} .redesign-btn-container .fad,.redesign-btn-container .fal,.redesign-btn-container .far,.redesign-btn-container .fas{margin-right:10px}.redesign-btn-container{width:100%;display:-webkit-box;display:-ms-flexbox;display:flex;-webkit-box-pack:justify;-ms-flex-pack:justify;justify-content:space-between;margin:1.3rem 0}.redesign-btn-container a{text-decoration:none}.redesign-btn-container a:hover{text-decoration:none}.redesign-btn{border:2px solid #ed7004;padding:7px 13px;font-size:.9rem;font-weight:600;background:#ed7004;color:#fff;cursor:pointer;text-align:center;line-height:1.5rem;margin:0 auto}.redesign-btn:hover{background:#fff;color:#ed7004}@media (max-width:768px){.redesign-btn{font-size:1.05rem}}.jir-b-table{font-family:'Open Sans', sans-serif;}.jir-b-table td,.jir-b-table th{border:2px solid #fff;padding:9px 12px}.jir-b-table th{background:#009fe3;color:#fff;font-weight:600;vertical-align:top;border-left:none}.jir-b-table td{color:#333;background:#f2f2f2;border-right:none}.jir-b-table tr:first-child td,.jir-b-table tr:first-child th{border-top:none}.jir-b-table tr:last-child td,.jir-b-table tr:last-child th{border-bottom:none}@media (max-width:600px){.jir-b-container{margin-left:0;margin-right:0;}}@media (max-width:490px){.jir-b-table td,.jir-b-table th{font-size:.8rem;padding:4px 6px}.jir-b-table th{line-height:20px}}<\/style>\n\n\n<figure class=\"wp-block-image size-full\"><img decoding=\"async\" loading=\"lazy\" width=\"350\" height=\"350\" src=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/serothumb.jpg\" alt=\"\" class=\"wp-image-5860\" srcset=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/serothumb.jpg 350w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/serothumb-300x300.jpg 300w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/serothumb-150x150.jpg 150w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/serothumb-45x45.jpg 45w\" sizes=\"(max-width: 350px) 100vw, 350px\" \/><\/figure>\n\n\n\n<p>Coronaviruses are a family of enveloped,\npositive-sense RNA viruses affecting the upper-respiratory tract, usually\ncausing only mild illnesses, similar to the common cold. However, three\nzoonotic pathogens, severe acute respiratory syndrome coronavirus (SARS-CoV)-1,\nMiddle East respiratory syndrome coronavirus (MERS-CoV), and SARS-CoV-2, that\nhave emerged in the past two decades lead to severe and often fatal outcomes in\nhumans.<sup>1<\/sup> As of July 22nd 2020, the current coronavirus SARS-CoV-2\npandemic has infected more than 15 million people in 188 countries and the\ndeath toll has surpassed 600,000.<sup>2<\/sup> <\/p>\n\n\n\n<p>This novel virus was transmitted to humans\nin late 2019 and as of July 2020 there are no approved therapeutic\ninterventions available. Millions of people are being advised to stay at home\nto reduce the spread of SARS-CoV-2 and limit the death toll. However, to fully\ncombat this virus, effective vaccines and treatments for this disease are\nessential.<sup>1<\/sup><\/p>\n\n\n<hr>\n<h3>Treatment Targets for SARS-CoV-2<\/h3>\n\n\n<p>One promising therapeutic target is the spike (S) glycoprotein found on the surface of the outer membrane envelope of coronaviruses. This S protein forms a trimeric complex with two subunits, S1 and S2, separated by a protease cleavage site. The S1 subunit contains the receptor-binding domain (RBD), which interacts with a receptor protein on the surface of the host cell \u2013 angiotensin converting enzyme 2 (ACE2) for SARS-CoV-1 and SARS-CoV-2 and dipeptidyl peptidase 4 (DPP4) for MERS-CoV.<sup>1 <\/sup>The S2 subunit is then responsible for fusing the viral envelope and host membranes to allow the virus particle to enter the host cell.<sup>4<\/sup><\/p>\n\n\n<div class=\"wp-block-image\">\n<figure class=\"aligncenter size-large\"><img decoding=\"async\" loading=\"lazy\" width=\"1024\" height=\"818\" src=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/7bwj-sars-ab-rbd-1024x818.png\" alt=\"\" class=\"wp-image-6169\" srcset=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/7bwj-sars-ab-rbd-1024x818.png 1024w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/7bwj-sars-ab-rbd-300x240.png 300w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/7bwj-sars-ab-rbd-1536x1227.png 1536w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/7bwj-sars-ab-rbd-2048x1636.png 2048w\" sizes=\"(max-width: 1024px) 100vw, 1024px\" \/><figcaption class=\"wp-element-caption\"> <em>Figure 1. Crystal structure of SARS-CoV-2 antibody with RBD. PDB ID: 7BWJ(Zhang et al 2020). Image generated with Molsoft ICM Browser. <\/em> <\/figcaption><\/figure><\/div>\n\n\n<p>Drugs that bind to the RBD on the S1\nsubunit of the S protein inhibit binding to the ACE2 receptor and can prevent\nfusion of the virus envelope with the host cell, resulting in neutralization of\nthe coronavirus. Interestingly, cryoelectron microscopy has demonstrated that\nthe RBD frequently changes conformation. Two major configurations have been\ncharacterized; the up conformation, where the RBD is accessible and can readily\nengage with the host-cell receptor, and the down conformation, where binding is\nprevented as the RBD is hidden by the top of the S2 subunit. Therefore, drug\nbinding is also thought to only be possible in the up conformation.<sup>3,4<\/sup>\n<\/p>\n\n\n<hr>\n<h3>VHH Antibodies Demonstrate Efficient Neutralizing Activity<\/h3>\n\n\n<p>Several RBD-specific human monoclonal antibodies derived from former patients have been isolated and reported for use against coronaviruses. They have shown strong neutralizing activities in animal models by binding with coronavirus spike protein to inhibit their abilities to infect cells. This method is used to interact with and augment the host\u2019s immune systems which contributes to efficacy in fighting the coronavirus as it has been suggested that only 1% may have naturally high levels of antibodies that could neutralize the virus without intervention.<sup>5<\/sup> <\/p>\n\n\n\n<p>These conventional antibodies are relatively large in size (~160 kDa), have poor pharmacokinetics, high production costs and are difficult to store and transport.<sup>3,4<\/sup> Given these challenges, smaller biologicals like heavy-chain variable (VHH) antibodies, also referred to as nanobodies, are being investigated as alternatives to canonical antibodies because of their higher stability and ability to bind to epitopes that are inaccessible to conventional antibodies.<sup>6<\/sup><\/p>\n\n\n\n<p>Zhao <em>et al. <\/em>(2018) developed a novel\nVHH antibody, NbMS10, designed for the therapeutic treatment of MERS-CoV.\nNbMS10 bound to the RBD of the S protein with a high binding affinity (<em>K<sub>d<\/sub><\/em>,\n8.71 x 10<sup>-10 <\/sup>M), which prevented MERS-CoV from binding to the\nhost-cell receptor DPP4 in mice. In addition, a relatively low dose (ND<sub>50<\/sub>,\n3.52 \u03bcg\/mL) was found to be sufficient to\nneutralize the virus, suggesting that NbMS10 could be a potential therapeutic\nfor MERS-CoV.<sup>4<\/sup><\/p>\n\n\n\n<p>However, due to their small size, VHH\nantibodies tend to have a fast-renal clearance, which may limit their\napplications. Researchers found that NbMS10 was cleared from the serum quickly\nin mice, with the binding affinity for MERS-CoV RBD completely lost 10 days\npost injection. <\/p>\n\n\n\n<p>A human-Fc-fused version, NbMS10-Fc, was\nconstructed increasing the size of the VHH antibody from 16 kDa to 50 kDa to\ntry and overcome this issue. NbMS10-Fc demonstrated comparable binding affinity\n(8.71 x 10<sup>-10<\/sup> and 3.46 x 10<sup>-10 <\/sup>M, respectively) and\nneutralizing activity (3.52 and 2.33 \u03bcg\/mL,\nrespectively) to NbMS10, but had a much slower clearance rate, with stable\nbinding for MERS-CoV RBD still observed 10 days post injection.<sup>4<\/sup><\/p>\n\n\n\n<p>These data were comparable to those\nobserved for RBD-specific conventional immunoglobulin Gs (IgG) (<em>K<sub>d<\/sub><\/em>,\n7.12 x 10<sup>-10<\/sup>\u20134.47 x 10<sup>-10 <\/sup>M; ND<sub>50\u00ad<\/sub>, \u03bcg\/mL\u2013ng\/mL). The cross-neutralizing activity of both VHH antibodies\nagainst divergent MERS-CoV strains was also found to be high, with the ND<sub>50<\/sub>\nranging from 0.003\u20130.979 \u03bcg\/mL and\n0.003\u20130.067 \u03bcg\/mL for NbMS10 and\nNbMS10-Fc, respectively. This research indicates VHH antibodies show promise as\nbroad-spectrum antivirals and may be beneficial in the current SARS-CoV-2\npandemic.<sup>4<\/sup><\/p>\n\n\n\n<p>More recently, Wrapp <em>et al.<\/em> isolated the VHH antibody SARS VHH-72 from a llama immunized with prefusion-stabilized coronavirus spikes directed against SARS-CoV-1 RBD. SARS VHH-72 demonstrated nanomolar binding affinity and was capable of neutralizing pseudotyped SARS-CoV-1 viruses <em>in vitro.<\/em> These promising results led to the researchers investigating the effect of this VHH antibody on SARS-CoV-2. <\/p>\n\n\n\n<p>Surface plasmon resonance analysis\nindicated SARS VHH-72 had high affinity to SARS-CoV-2 RBD, however no\ninteraction was detected using ELISA and the VHH antibody was not able to\nneutralize SARS-CoV-2 pseudoviruses. Therefore, using a similar approach to\nZhao <em>et al.<\/em>, the group engineered SARS VHH-72 into a bivalent Fc-fusion,\nSARS-VHH-72-Fc. This modified VHH antibody showed a high binding affinity to\nSARS-CoV-2 RBD and was able to neutralize SARS-CoV-2-(S) spike glycoprotein pseudoviruses,\nproviding&nbsp;further evidence of VHH antibodies as\npromising therapeutics in the fight against the current SARS-CoV-2 pandemic.<sup>1<\/sup><\/p>\n\n\n<hr>\n<h3>Benefits of VHH Antibodies<\/h3>\n\n\n<p>VHH antibodies are the isolated VHH domains of heavy-chain only IgG2 and IgG3 antibodies produced by camelid species, such as alpaca, llama, and camel. These proteins consist of framework regions and three highly variable loops; H1, H2 and H3. Research has shown that it is the H3 loop that enables VHH antibodies to have such a wide range of bind specificities; the H3 loop tends to be 3\u20134 residues longer than that of conventional antibodies, allowing them to use these protrusions to extend into \u201chidden\u201d epitope cavities; the H3 loop also has more variation in amino acid sequences in VHH antibodies than conventional antibodies, leading to ~7% higher sequence diversity per residue.<sup>6<\/sup>&nbsp; <\/p>\n\n\n\n<div class=\"wp-block-image\"><figure style=\"margin:2rem auto;width: 100%;\" class=\"aligncenter size-large\"><img decoding=\"async\" loading=\"lazy\" width=\"382\" height=\"500\" style=\"margin:auto;display:block;\" src=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/figure-2-vhh-covid.jpg\" alt=\"\" class=\"wp-image-6172\" srcset=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/figure-2-vhh-covid.jpg 382w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/figure-2-vhh-covid-229x300.jpg 229w\" sizes=\"(max-width: 382px) 100vw, 382px\" \/><figcaption style=\"font-style:italic;\"> <br> Figure 2. Structural features of conventional and camelid heavy\u2010chain antibodies (Ab). A, In an Ab, the antigen binds to the VH\u2010VL interface, while in the camelid heavy\u2010chain antibody the VH\u2010homologous VHH domain binds the antigen. In Abs, the VH and VL domains bind to each other and can only be produced in bacterial expression systems when joined by a peptide linker. B, Like the Ab VH domain, the secondary structure of the VHH domain consists of 9 beta-sheets separated by loop regions, 3 of which are hypervariable (shown in blue, green and red). Four framework regions (FRs) separate the variable loops; these are less sequence\u2010variable. Four positions known as the VHH\u2010tetrad are numbered and highlighted in yellow. Right: VHH domain with VHH\u2010tetrad positions in yellow. C, The antigen\u2010binding surface in VHH domains and Ab VH\u2010VL domains (aligned orientations).<em> Image and figure legend courtesy of Mitchell &amp; Cowell (2018)<sup>6<\/sup> <\/em><a href=\"https:\/\/doi.org\/10.1002\/prot.25497\"><em>https:\/\/doi.org\/10.1002\/prot.25497<\/em><\/a><em> CC BY 4.0 <\/em> <\/figcaption><\/figure><\/div>\n\n\n\n<p>In addition to their structural difference, there are several other features of VHH antibodies that make them more advantageous compared to canonical antibodies:<sup>3\u20137<\/sup><\/p>\n\n\n\n<figure class=\"wp-block-table jir-b-container\"><table class=\"jir-b-table\">\n        <tbody>\n            <tr>\n                <th scope=\"row\">Variable functionality<\/th>\n                <td>   VHH domain acts as a   framework for recombinant antibody architecture, allowing the engineering of different structural formats. Tags can be added for purification or functional groups can be attached for the conjugation of drugs or fluorescent probes.      &nbsp;   <\/td>\n            <\/tr>\n            <tr>\n                <th scope=\"row\"> Small size (12\u201315 kDa)<\/th>\n                <td>   Less susceptible to steric hindrance due to their smaller size, conferring improved access to epitopes. VHH antibodies have good tissue permeability and can cross the blood-brain barrier, making them attractive drug delivery options.      &nbsp;   <\/td>\n            <\/tr>\n            <tr>\n                <th scope=\"row\">Low production cost<\/th>\n                <td>   VHH antibodies can be produced recombinantly at high yields using bacterial, yeast, or mammalian expression systems.   <\/td>\n            <\/tr>\n            <tr>\n                <th scope=\"row\">High stability<\/th>\n                <td>   VHH antibodies have good solubility, high thermal and chemical stability, and higher resistance to proteases than conventional antibodies. High stability also allows nebulization and administration via an inhaler to directly reach the site of infection.          &nbsp;   <\/td>\n            <\/tr>\n        <\/tbody>\n    <\/table><\/figure>\n\n\n<hr>\n<h3>Jackson ImmunoResearch Enables the Production of High Affinity VHH Antibodies<\/h3>\n\n\n<p>When engineering VHH antibodies, production\noptimization, isolation and purification are essential to maximizing yield and\ngenerating high affinity, high-quality products that can be used to treat\npatients. <a href=\"https:\/\/www.jacksonimmuno.com\/technical\/products\/antibody-selection\">Jackson\nImmunoResearch Laboratories<ins>,<\/ins> Inc<\/a><ins>.<\/ins> specializes in producing highly specific secondary antibodies and\nimmunoreagents and is committed to supporting manufacturers generating VHH\nantibodies for diagnostics or therapeutics in the treatment of novel viral\ninfections, such as SARS-CoV-2. <\/p>\n\n\n\n<p>Jackson ImmunoResearch has developed a range of products to facilitate the production of VHH antibodies, enabling optimization at each stage of development, from tracking seroconversion through to screening VHH antibody candidates. Their Anti-Alpaca antibodies are suitable for the detection of both alpaca, llama and camel proteins and are available with specificity for IgG (H+L), IgG, subclasses 2+3, or VHH domains. They have utility across multiple techniques such as Western blotting, ELISA, flow cytometry, and immunofluorescence. These products have been designed to optimize VHH antibody discovery to ensure the production of high-quality candidates.<sup>7,8<\/sup> <\/p>\n\n\n\n<p><\/p>\n\n\n<div class=\"redesign-btn-container\">\n<a class=\"redesign-btn\" href=\"\/technical\/products\/VHH-Discovery\"><i class=\"fas fa-graduation-cap\"><\/i>Learn More About VHH Discovery<\/a>\n<\/div>\n<hr>\n<h3>References and Further Reading<\/h3>\n<p><\/p>\n\n\n<ol>\n<li>Wrapp D., <em>et al.<\/em> (2020). Structural Bases for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies. Cell. <a href=\"https:\/\/doi.org\/10.1016\/j.cell.2020.04.031\">https:\/\/doi.org\/10.1016\/j.cell.2020.04.031<\/a>.<\/li>\n\n\n\n<li>www.bbc.com. (2020). Coronavirus Pandemic: Tracking the Global Outbreak. <a href=\"https:\/\/www.bbc.co.uk\/news\/world-51235105?utm_source=dlvr.it&amp;utm_medium=twitter\">https:\/\/www.bbc.co.uk\/news\/world-51235105?utm_source=dlvr.it&amp;utm_medium=twitter<\/a> <\/li>\n\n\n\n<li>Mahase E. (2020). Covid-19: What Treatments are Being Investigated? British Medical Journal. <a href=\"https:\/\/www.bmj.com\/content\/368\/bmj.m1252\/rr-16\">doi: 10.1136\/bmj.m1252<\/a>. <\/li>\n\n\n\n<li>Zhao G., <em>et al. <\/em>(2018). A Novel Nanobody Targeting Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Receptor-Binding Domain Has Potent Cross-Neutralizing Activity and Protective Efficacy Against MERS-COV. Journal of Virology. <a href=\"https:\/\/doi.org\/10.1128\/JVI.00837-18\">https:\/\/doi.org\/10.1128\/JVI.00837-18<\/a>.<\/li>\n\n\n\n<li><a href=\"https:\/\/www.nih.gov\/news-events\/nih-research-matters\/potent-antibodies-found-people-recovered-covid-19\">https:\/\/www.nih.gov\/news-events\/nih-research-matters\/potent-antibodies-found-people-recovered-covid-19<\/a><\/li>\n\n\n\n<li>Mitchell L. S., <em>et al.<\/em> (2017). Comparative Analysis of Nanobody Sequence and Structure Data. Proteins.<a href=\"%20https:\/doi.org\/10.1002\/prot.25497\"> https:\/\/doi.org\/10.1002\/prot.25497<\/a>.<\/li>\n\n\n\n<li>www.jacksonimmuno.com. (2020). Camelid Immunology. <a href=\"https:\/\/www.jacksonimmuno.com\/technical\/products\/groups\/camelid\">https:\/\/www.jacksonimmuno.com\/technical\/products\/groups\/camelid<\/a> <\/li>\n\n\n\n<li>www.jacksonimmuno.com. (2020). Introducing Anti-Alpaca IgG, VHH Domain Secondary Antibodies. <a href=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/Anti-VHH-handout-US-online.pdf\">https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/Anti-VHH-handout-US-online.pdf<\/a> <\/li>\n\n\n\n<li>Zhang Z., <em>et al<\/em> (2020). Human neutralizing antibodies elicited by SARS-CoV-2 infection. Human neutralizing antibodies elicited by SARS-CoV-2 infection. Nature PubMed: 32454513 DOI: 10.1038\/s41586-020-2380-z<\/li>\n<\/ol>\n\n\n\n<p><\/p>\n\n\n<table class=\"table\">\n<thead>\n<tr>\n<th class=\"span6\">Learn more:<\/th>\n<th class=\"span6\">Do more:<\/th>\n<\/tr>\n<\/thead>\n<tbody>\n<tr>\n<td class=\"span6\"><a href=\"\/technical\/products\/protocols\/multiple-labeling\">Multiple labeling using Secondary Antibodies<\/a><\/td>\n<td class=\"span6\"><a href=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/technical-tips\/westernblotting-10tips\/\">Western blotting &#8211; 10 tips for better blots<\/a><\/td>\n<\/tr>\n<tr>\n<td class=\"span6\"><a href=\"\/secondary-antibody-resource\/immuno-techniques\/direct-and-indirect-western-blotting\/\">Direct and Indirect Western blotting<\/a><\/td>\n<td class=\"span6\"><a href=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/technical-tips\/species-on-species-experiments-solutions\/\">Species on species labeling<\/a><\/td>\n<\/tr>\n<tr>\n<td class=\"span6\"><a href=\"\/technical\/products\/antibody-selection\">Choosing your Secondary Antibody<\/a><\/td>\n<td class=\"span6\"><a href=\"https:\/\/www.jacksonimmuno.com\/technical\/products\/VHH-Discovery\">Secondary Antibodies for VHH discovery<\/a><\/td>\n<\/tr>\n<\/tbody>\n<\/table><!-- AddThis Advanced Settings generic via filter on the_content --><!-- AddThis Share Buttons generic via filter on the_content --><!-- AddThis Related Posts generic via filter on the_content -->","protected":false},"excerpt":{"rendered":"<p>Download PDF Coronaviruses are a family of enveloped, positive-sense RNA viruses affecting the upper-respiratory tract, usually causing only mild illnesses, similar to the common cold. However, three zoonotic pathogens, severe acute respiratory syndrome coronavirus (SARS-CoV)-1, Middle East respiratory syndrome coronavirus (MERS-CoV), and SARS-CoV-2, that have emerged in the past two decades lead to severe and [&hellip;]<!-- AddThis Advanced Settings generic via filter on get_the_excerpt --><!-- AddThis Share Buttons generic via filter on get_the_excerpt --><!-- AddThis Related Posts generic via filter on get_the_excerpt --><\/p>\n","protected":false},"author":3,"featured_media":0,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"content-type":""},"categories":[20],"tags":[],"acf":[],"_links":{"self":[{"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts\/5690"}],"collection":[{"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/comments?post=5690"}],"version-history":[{"count":36,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts\/5690\/revisions"}],"predecessor-version":[{"id":11082,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts\/5690\/revisions\/11082"}],"wp:attachment":[{"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/media?parent=5690"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/categories?post=5690"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/tags?post=5690"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}