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Factor H
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<h2 id="structure">Structure</h2> <p>The molecule is made up of 20 <a href="/facts/Complement_control_protein/LJceJgzW">complement control protein</a> (CCP) modules (also referred to as Short Consensus Repeats or sushi domains) connected to one another by short linkers (of between three and eight <a href="/facts/Amino_acid/WDxYwBny">amino acid</a> residues) and arranged in an extended head to tail fashion. Each of the CCP modules consists of around 60 amino acids with four <a href="/facts/Cysteine/kbqvUm6d">cysteine</a> residues <a href="/facts/Disulfide_bond/eDx5Xtlg">disulfide bonded</a> in a 1–3 2–4 arrangement, and a hydrophobic core built around an almost invariant <a href="/facts/Tryptophan/JcUxlxAh">tryptophan</a> residue. The CCP modules are numbered from 1–20 (from the N-terminus of the protein); CCPs 1–4 and CCPs 19–20 engage with <a href="/facts/C3b/gQ2bfe0R">C3b</a> while CCPs 7 and CCPs 19–20 bind to GAGs and <a href="/facts/Sialic_acid/spYNJFbh">sialic acid</a>.<a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a> To date atomic structures have been determined for CCPs 1–3,<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> CCP 5,<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> CCP 7,<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> CCPs 10–11 and CCPs 11–12,<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> CCPs 12–13,<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> CCP 15, CCP 16,<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> CCPs 15–16,<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> CCPs 18–20,<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a> and CCPs 19–20.<a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a><a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> The atomic structure for CCPs 6–8 bound to the GAG mimic sucrose octasulfate,<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> CCPs 1–4 in complex with C3b<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> and CCPs 19–20 in complex with C3d (that corresponds to the thioester domain of C3b)<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a><a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> have also been determined. Although an atomic resolution structure for intact factor H has not yet been determined, low resolution techniques indicate that it may be bent back in solution.<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a> Information available to date indicates that CCP modules 1–4 is responsible for the cofactor and decay acceleration activities of factor H, whereas self/non-self discrimination occurs predominantly through GAG binding to CCP modules 7 and/or GAG or sialic acid binding to 19–20.<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a><a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> </p> <h2 id="clinical-significance">Clinical significance</h2> <p>Due to the central role that factor H plays in the regulation of complement, there are a number of clinical implications arising from aberrant factor H activity. Overactive factor H may result in reduced complement activity on pathogenic cells – increasing susceptibility to microbial infections. Underactive factor H may result in increased complement activity on healthy host cells – resulting in autoimmune diseases. It is not surprising, therefore, that rare <a href="/facts/Mutations/Ee4NnWbY">mutations</a> or common <a href="/facts/Single_nucleotide_polymorphisms/Qy5Y2wom">single nucleotide polymorphisms</a> (SNPs) in the complement factor H gene (CFH) often result in pathologies. Moreover, the complement inhibitory activities of factor H, and other complement regulators, are often used by pathogens to increase <a href="/facts/Virulence/TYmX1Fa6">virulence</a>. </p> <h3>Age-related macular degeneration</h3> <p>In 2005, several independent research groups identified an SNP in CFH, which results in the protein change p.Y402H, as a risk factor for <a href="/facts/Macular_degeneration/9pFARaka">Age Related Macular Degeneration</a> (AMD) present in around a third of Europeans.<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a> Although its allele frequency varies considerably between different populations, Y402H has been consistently associated with AMD onset and progression.<a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a> <a href="/facts/Homozygous/XzEJ5gPp">Homozygous</a> individuals have an approximately seven-fold greater odds of association with AMD while <a href="/facts/Heterozygotes/XzEJ5gPp">heterozygotes</a> have a two-to-three-fold greater odds of association with the disease.<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> This SNP, located in CCP module 7 of factor H, has been shown to affect the ability of factor H protein to localise to sites of inflammation in retinal tissues (e.g. by <a href="/facts/Polyanions/3A3jLXkh">polyanions</a> and pentraxins) and to regulate the activation of complement and immune cells.<a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a> The SNP has also been shown to affect the function of factor H-like protein 1, an alternatively spliced version of factor H consisting of CCPs 1 to 7 only, which is thought to have a greater role in intraocular complement regulation.<a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a> The British complementologist, <a href="/facts/Simon_J._Clark/UBldd2xN">Simon J. Clark</a> demonstrated that FHL-1 was the predominant form of FH protecting <a href="/facts/Bruch%2527s_membrane/VCpPBoRU">Bruch's membrane</a>,<a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a> an integral part of the outer <a href="/facts/Blood-retinal_barrier/fkFfxQJq">Blood-retinal barrier</a> and a major site of early AMD. Further studies suggested that haploinsufficiency of FHL-1 lead to the manifestation of an AMD-like disease at a significantly earlier age.<a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a> However, the genetic variants in CFH with the greatest effect on an individual's risk of AMD have been shown to affect CCPs 1 to 4, which are involved in dampening the effects of the alternative pathway of complement.<a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a> A rare functional coding change, p.R1210C, in CFH results in a functional deficiency in factor H and leads to a substantially higher risk of macular degeneration as well as complement-mediated renal conditions.<a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a><a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a> </p><p>Variation in other genes of the regulators of complement activation locus, such as complement factor H-related genes, as well as in other complement proteins (e.g. factor I, C2/factor B, and C3) have also been associated with greater AMD risk.<a class="footnote-ref" id="fnref:37" href="#fn:37"><sup>37</sup></a> The current theory is that complement dysregulation is a key driver of chronic inflammation in AMD.<a class="footnote-ref" id="fnref:38" href="#fn:38"><sup>38</sup></a> </p> <h3>Atypical hemolytic uremic syndrome</h3> <p><a href="/facts/Hemolytic_uremic_syndrome/ukwcKx3I">Hemolytic uremic syndrome</a> (HUS) is a disease associated with microangiopathic hemolytic anemia, thrombocytopenia, and acute renal failure. It can be either acquired (e.g. following infection with shigatoxigenic <i>Escherichia coli</i>), or inherited (also known as atypical hemolytic uremic syndrome, aHUS). aHUS has been strongly linked to mutations in genes of the complement system, especially factor H.<a class="footnote-ref" id="fnref:39" href="#fn:39"><sup>39</sup></a> In contrast to AMD and C3 glomerulopathy (another complement-mediated renal disorder) which are mainly associated with variation in the N-terminus (CCPs 1 to 4), predisposing mutations in factor H mainly affect the C-terminus of the protein (CCP modules 19 and 20),<a class="footnote-ref" id="fnref:40" href="#fn:40"><sup>40</sup></a> which has been shown to be responsible for adherence to renal tissues and the regulation of complement components and their downstream effectors.<a class="footnote-ref" id="fnref:41" href="#fn:41"><sup>41</sup></a><a class="footnote-ref" id="fnref:42" href="#fn:42"><sup>42</sup></a><a class="footnote-ref" id="fnref:43" href="#fn:43"><sup>43</sup></a> </p> <h3>Schizophrenia</h3> <p>Alterations in the immune response are involved in pathogenesis of many neuropsychiatric disorders including <a href="/facts/Schizophrenia/FMP4lQ57">schizophrenia</a>. Recent studies indicated alterations in the <a href="/facts/Complement_system/vRSrQDUv">complement system</a>, including those which may result in the overactivation of the <a href="/facts/Alternative_complement_pathway/eN5PARpC">alternative complement pathway</a>, may predispose to schizophrenia. For example, the CFH SNP rs424535 (2783-526T>A) was positively associated with schizophrenia.<a class="footnote-ref" id="fnref:44" href="#fn:44"><sup>44</sup></a> </p> <h3>Ischemic stroke</h3> <p>It was found that rs800292(184G >A) SNP was positively associated with stroke and rs800912 minor allele of the CFH gene might be considered as a risk factor for ischemic stroke.<a class="footnote-ref" id="fnref:45" href="#fn:45"><sup>45</sup></a> </p> <h3>Recruitment by pathogens</h3> <p>Given the central role of factor H in protecting cells from complement, it is not surprising that several important human <a href="/facts/Pathogens/axMXtV1M">pathogens</a> have evolved mechanisms for recruiting factor H. This recruitment of factor H by pathogens provides significant resistance to complement attack, and therefore increased virulence. Pathogens that have been shown to recruit factor H include: <i><a href="/facts/Aspergillus/pKhecLTW">Aspergillus</a></i> spp.; <i><a href="/facts/Borrelia_burgdorferi/sSvh5CyA">Borrelia burgdorferi</a></i>; <i>B. duttonii</i>; <i><a href="/facts/B._recurrentis/D14TdE2y">B. recurrentis</a></i>; <i><a href="/facts/Candida_albicans/7o27aEFS">Candida albicans</a></i>;<a class="footnote-ref" id="fnref:46" href="#fn:46"><sup>46</sup></a> <i><a href="/facts/Francisella_tularensis/JcmsRq6m">Francisella tularensis</a></i>; <i><a href="/facts/Haemophilus_influenzae/wqIpoDI1">Haemophilus influenzae</a></i>; <i><a href="/facts/Neisseria_gonorrhoeae/2oq5rccN">Neisseria gonorrhoeae</a></i>;<a class="footnote-ref" id="fnref:47" href="#fn:47"><sup>47</sup></a> <i><a href="/facts/Neisseria_meningitidis/u4SqwHuc">N. meningitidis</a></i>; <i><a href="/facts/Streptococcus_pneumoniae/B5XxK27j">Streptococcus pneumoniae</a></i>;<a class="footnote-ref" id="fnref:48" href="#fn:48"><sup>48</sup></a> and <i><a href="/facts/Streptococcus_pyogenes/qrkSpDz1">Streptococcus pyogenes</a></i>.<a class="footnote-ref" id="fnref:49" href="#fn:49"><sup>49</sup></a> </p><p>The Gram-negative bacterium <i>B. burgdorferi</i> has five factor H–binding proteins: CRASP-1, CRASP-2, CRASP-3, CRASP-4 and CRASP-5.<a class="footnote-ref" id="fnref:50" href="#fn:50"><sup>50</sup></a> Each CRASP protein also binds <a href="/facts/Plasminogen/bfLCyyPt">plasminogen</a>.<a class="footnote-ref" id="fnref:51" href="#fn:51"><sup>51</sup></a> It is possible that the allele frequency of CFH variants across the globe reflects selective pressure from infectious diseases.<a class="footnote-ref" id="fnref:52" href="#fn:52"><sup>52</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>Factor H has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with <a href="/facts/Complement_component_3/pqsRthBP">complement component 3</a>, amongst other complement proteins and factors, leading to regulation of the alternative pathway of complement in particular.<a class="footnote-ref" id="fnref:53" href="#fn:53"><sup>53</sup></a><a class="footnote-ref" id="fnref:54" href="#fn:54"><sup>54</sup></a><a class="footnote-ref" id="fnref:55" href="#fn:55"><sup>55</sup></a> </p> <h2 id="recombinant-production">Recombinant production</h2> <p>Biologically active Factor H has been produced by <a href="/facts/Ralf_Reski/aXUPS6FA">Ralf Reski</a> and coworkers in the <a href="/facts/Moss_bioreactor/Tu5GSoNK">moss bioreactor</a>,<a class="footnote-ref" id="fnref:56" href="#fn:56"><sup>56</sup></a> in a process called <a href="/facts/Molecular_farming/4sI0WlE6">molecular farming</a>. Large quantities of biologically active human Factor H, potentially suitable for therapeutic purposes, were produced using a synthetic <a href="/facts/Codon/zUK0bY1B">codon</a>-optimised gene expressed in the <a href="/facts/Yeast/eGD24nfI">yeast</a> expression host, <i><a href="/facts/Pichia_pastoris/MVfqL0Ad">Pichia pastoris</a></i>.<a class="footnote-ref" id="fnref:57" href="#fn:57"><sup>57</sup></a> </p> <h2 id="potential-use-as-a-therapeutic-drug">Potential use as a therapeutic drug</h2> <h3>Age-related macular degeneration</h3> <p>Gemini Therapeutics Inc. was a Massachusetts based precision medicine company focused on the development of new therapies through a deeper understanding of disease. Based on the biological activity of human factor H, Gemini was developing a recombinant human factor H protein, GEM103, for the treatment of dry AMD. GEM-103 was evaluated in phase I (NCT04246866) and II (NCT04643886) clinical trials in AMD patients, but failed to achieve its clinical end points and the developmental program was terminated<a class="footnote-ref" id="fnref:58" href="#fn:58"><sup>58</sup></a> Gemini Therapeutics merged with Disc Medicine in 2022<a class="footnote-ref" id="fnref:59" href="#fn:59"><sup>59</sup></a> </p><p>Other companies currently focusing on developing FH, FHL-1, or variations thereof, as therapeutics for treating AMD, include Character Biosciences Inc,<a class="footnote-ref" id="fnref:60" href="#fn:60"><sup>60</sup></a> and 4D Molecular Therapeutics<a class="footnote-ref" id="fnref:61" href="#fn:61"><sup>61</sup></a> </p> <h2 id="further-reading">Further reading</h2> <ul><li>Bradley DT, Zipfel PF, Hughes AE (June 2011). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3178140">"Complement in age-related macular degeneration: a focus on function"</a>. <i>Eye</i>. 25 (6): 683–693. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Feye.2011.37">10.1038/eye.2011.37</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3178140">3178140</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/21394116">21394116</a>.</li> <li>Kardys I, Klaver CC, Despriet DD, Bergen AA, Uitterlinden AG, Hofman A, et al. (April 2006). <a href="https://doi.org/10.1016%2Fj.jacc.2005.11.076">"A common polymorphism in the complement factor H gene is associated with increased risk of myocardial infarction: the Rotterdam Study"</a>. <i>Journal of the American College of Cardiology</i>. 47 (8): 1568–1575. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.jacc.2005.11.076">10.1016/j.jacc.2005.11.076</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/16630992">16630992</a>.</li> <li>Pío R, Elsasser TH, Martínez A, Cuttitta F (April 2002). <a href="https://doi.org/10.1002%2Fjemt.10047">"Identification, characterization, and physiological actions of factor H as an adrenomedullin binding protein present in human plasma"</a>. <i>Microscopy Research and Technique</i>. 57 (1): 23–27. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fjemt.10047">10.1002/jemt.10047</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11921353">11921353</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:37608883">37608883</a>.</li> <li>Walport MJ (April 2001). "Complement. First of two parts". <i>The New England Journal of Medicine</i>. 344 (14): 1058–1066. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1056%2FNEJM200104053441406">10.1056/NEJM200104053441406</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11287977">11287977</a>.</li> <li>Walport MJ (April 2001). "Complement. Second of two parts". <i>The New England Journal of Medicine</i>. 344 (15): 1140–1144. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1056%2FNEJM200104123441506">10.1056/NEJM200104123441506</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11297706">11297706</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://www.ncbi.nlm.nih.gov/books/NBK1367/">GeneReviews/NCBI/NIH/UW entry on Atypical Hemolytic-Uremic Syndrome</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/books/NBK1425/">GeneReviews/NCBI/NIH/UW entry on Dense Deposit Disease/Membranoproliferative Glomerulonephritis Type II</a></li> <li><a href="https://www.ncbi.nlm.nih.gov/omim/277400,120700,120920,134370,134371,138470,188040,217030,235400,605336,605337,612922,612923,612924,612925,612926,120700,120920,134370,134371,138470,188040,217030,235400,605336,605337,612922,612923,612924,612925,612926">OMIM entries on Atypical Hemolytic-Uremic Syndrome</a></li> <li><a href="https://meshb.nlm.nih.gov/record/ui?name=Complement+Factor+H">Complement+Factor+H</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Sofat R, Mangione PP, Gallimore JR, Hakobyan S, Hughes TR, Shah T, et al. (April 2013). "Distribution and determinants of circulating complement factor H concentration determined by a high-throughput immunonephelometric assay". Journal of Immunological Methods. 390 (1–2): 63–73. doi:10.1016/j.jim.2013.01.009. PMID 23376722. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Hakobyan S, Harris CL, Tortajada A, Goicochea de Jorge E, García-Layana A, Fernández-Robredo P, et al. (May 2008). "Measurement of factor H variants in plasma using variant-specific monoclonal antibodies: application to assessing risk of age-related macular degeneration". Investigative Ophthalmology & Visual Science. 49 (5): 1983–1990. doi:10.1167/iovs.07-1523. hdl:10261/56608. PMID 18436830. <a href="https://doi.org/10.1167%2Fiovs.07-1523" target="_blank">https://doi.org/10.1167%2Fiovs.07-1523</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>Scholl HP, Charbel Issa P, Walier M, Janzer S, Pollok-Kopp B, Börncke F, et al. (July 2008). "Systemic complement activation in age-related macular degeneration". PLOS ONE. 3 (7): e2593. Bibcode:2008PLoSO...3.2593S. doi:10.1371/journal.pone.0002593. PMC 2440421. PMID 18596911. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2440421" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2440421</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Lewis LA, Carter M, Ram S (May 2012). "The relative roles of factor H binding protein, neisserial surface protein A, and lipooligosaccharide sialylation in regulation of the alternative pathway of complement on meningococci". Journal of Immunology. 188 (10): 5063–5072. doi:10.4049/jimmunol.1103748. PMC 3345070. PMID 22504643. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3345070" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3345070</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Vu DM, Shaughnessy J, Lewis LA, Ram S, Rice PA, Granoff DM (February 2012). Bliska JB (ed.). "Enhanced bacteremia in human factor H transgenic rats infected by Neisseria meningitidis". Infection and Immunity. 80 (2): 643–650. doi:10.1128/IAI.05604-11. PMC 3264313. PMID 22104107. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3264313" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3264313</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Herbert AP, Makou E, Chen ZA, Kerr H, Richards A, Rappsilber J, et al. (November 2015). "Complement Evasion Mediated by Enhancement of Captured Factor H: Implications for Protection of Self-Surfaces from Complement". Journal of Immunology. 195 (10): 4986–4998. doi:10.4049/jimmunol.1501388. PMC 4635569. PMID 26459349. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4635569" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4635569</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Pangburn MK (August 2000). "Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement". Immunopharmacology. 49 (1–2): 149–157. doi:10.1016/S0162-3109(00)80300-8. PMID 10904114. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>Rodríguez de Córdoba S, Esparza-Gordillo J, Goicoechea de Jorge E, Lopez-Trascasa M, Sánchez-Corral P (June 2004). "The human complement factor H: functional roles, genetic variations and disease associations". Molecular Immunology. 41 (4): 355–367. doi:10.1016/j.molimm.2004.02.005. 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