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Application of Nano-antibody in the Prevention, Diagnosis and Treatment of Infectious Diseases |
MEI Ya-xian,WANG Yue,LUO Wen-xin() |
State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics & National Institute of Diagnostics and Vaccine Development in Infectious Disease, School of Public Health, Xiamen University, Xiamen 361102, China |
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Abstract Infectious disease mainly refer to transmissible diseases caused by pathogenic microorganisms. It can affect human health and even cause serious social crisis. In recent years, the outbreaks of infectious diseases like COVID-19 and ebola have prompted people to seek more efficient and convenient means to control and prevent infectious diseases. As an effective way currently, antibody has drawn people’s attention. However, palivizumab, for the prevention and treatment of respiratory syncytial virus, is the only one monoclonal antibody approved for infectious diseases. Nano-antibody (Nb) is the smallest known functional antibody capable of stably binding to antigens. Nb has the advantages of high stability, strong hydrophilicity, easy production through microbial systems, easy modification, etc. Due to its unique molecular properties, Nb has shown promising application prospects in the prevention, diagnosis and treatment of infectious diseases caused by viruses, bacteria, parasites, etc. Related studies have shown that Nb has good therapeutic effects on AIDS, influenza, novel coronavirus, etc. This paper focuses on the structural characteristics of Nb and its research progress in infectious diseases.
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Received: 30 June 2020
Published: 10 November 2020
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Corresponding Authors:
Wen-xin LUO
E-mail: wxluo@xmu.edu.cn
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[1] |
Sanaei M, Setayesh N, Sepehrizadeh Z, et al. Nanobodies in human infections: prevention, detection, and treatment. Immunological Investigations, 2019: 1-22.
doi: 10.1080/08820139.2020.1817934
pmid: 32954867
|
|
|
[2] |
Statistics N B O. National data.[2020-06-03]. http://data.stats.gov.cn/search.htm?s=%E4%BC%A0%E6%9F%93%E7%97%85.
doi: 10.3390/data4010020
pmid: 30956970
|
|
|
[3] |
Worldmeter. Covid-19 coronavirus pandemic. [2020-06-03]. https://www.worldometers.info/coronavirus/.
|
|
|
[4] |
百度. 疫情实时大数据报告. [2020-06-03]. https://voice.baidu.com/act/newpneumonia/newpneumonia#tab4.
|
|
|
[5] |
Hey A. History and practice: Antibodies in infectious diseases. Microbiology Spectrum, 2015, 3(2): AID-0026-2014.
doi: 10.1128/microbiolspec.MDNA3-0058-2014
pmid: 26104699
|
|
|
[6] |
Steeland S, Vandenbroucke R E, Libert C. Nanobodies as therapeutics: Big opportunities for small antibodies. Drug Discovery Today, 2016,21(7):1076-1113.
doi: 10.1016/j.drudis.2016.04.003
pmid: 27080147
|
|
|
[7] |
Hassanzadeh-Ghassabeh G, Devoogdt N, De Pauw P, et al. Nanobodies and their potential applications. Nanomedicine, 2013,8(6):1013-1026.
doi: 10.2217/nnm.13.86
pmid: 23730699
|
|
|
[8] |
D’huyvetter M, Vincke C, Xavier C, et al. Targeted radionuclide therapy with a 177lu-labeled anti-her2 nanobody. Theranostics, 2014,4(7):708-720.
doi: 10.7150/thno.8156
pmid: 24883121
|
|
|
[9] |
Oliveira S, Van Dongen G a M S, Walsum M S-V, et al. Rapid visualization of human tumor xenografts through optical imaging with a near-infrared fluorescent anti-epidermal growth factor receptor nanobody. Molecular Imaging, 2012, 11(1): 7290.2011.00025.
pmid: 22418021
|
|
|
[10] |
Abulrob A, Sprong H, Van Bergen En Henegouwen P, et al. The blood-brain barrier transmigrating single domain antibody: mechanisms of transport and antigenic epitopes in human brain endothelial cells. Journal of Neurochemistry, 2005,95(4):1201-1214.
doi: 10.1111/j.1471-4159.2005.03463.x
pmid: 16271053
|
|
|
[11] |
Bannas P, Hambach J, Koch-Nolte F. Nanobodies and nanobody-based human heavy chain antibodies as antitumor therapeutics. Frontiers in Immunology, 2017,8:1603-1603.
doi: 10.3389/fimmu.2017.01603
pmid: 29213270
|
|
|
[12] |
Muyldermans S, Baral T N, Retarnozzo V C, et al. Camelid immunoglobulins and nanobody technology. Veterinary Immunology and Immunopathology, 2009,128(1-3):178-183.
doi: 10.1016/j.vetimm.2008.10.299
pmid: 19026455
|
|
|
[13] |
Harmsen M M, De Haard H J. Properties, production, and applications of camelid single-domain antibody fragments. Applied Microbiology and Biotechnology, 2007,77(1):13-22.
doi: 10.1007/s00253-007-1142-2
pmid: 17704915
|
|
|
[14] |
Stijlemans B, Conrath K, Cortez-Retamozo V, et al. Efficient targeting of conserved cryptic epitopes of infectious agents by single domain antibodies - african trypanosomes as paradigm. Journal of Biological Chemistry, 2004,279(2):1256-1261.
doi: 10.1074/jbc.M307341200
pmid: 14527957
|
|
|
[15] |
Saerens D, Conrath K, Govaert J, et al. Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains. Journal of Molecular Biology, 2008,377(2):478-488.
doi: 10.1016/j.jmb.2008.01.022
pmid: 18262543
|
|
|
[16] |
Li M, Fan X D, Liu J, et al. Selection by phage display of nanobodies directed against hypoxia inducible factor-1 alpha (hif-1 alpha). Biotechnology and Applied Biochemistry, 2015,62(6):738-745.
doi: 10.1002/bab.1340
pmid: 25556956
|
|
|
[17] |
Dumoulin M, Conrath K, Van Meirhaeghe A, et al. Single-domain antibody fragments with high conformational stability. Protein Science, 2002,11(3):500-515.
doi: 10.1110/ps.34602
pmid: 11847273
|
|
|
[18] |
Omidfar K, Daneshpour M. Advances in phage display technology for drug discovery. Expert Opinion on Drug Discovery, 2015,10(6):651-669.
doi: 10.1517/17460441.2015.1037738
pmid: 25910798
|
|
|
[19] |
Van Audenhove I, Boucherie C, Pieters L, et al. Stratifying fascin and cortactin function in invadopodium formation using inhibitory nanobodies and targeted subcellular delocalization. FASEB Journal, 2014,28(4):1805-1818.
doi: 10.1096/fj.13-242537
pmid: 24414419
|
|
|
[20] |
Van Den Abbeele A, De Clercq S, De Ganck A, et al. A llama-derived gelsolin single-domain antibody blocks gelsolin-g-actin interaction. Cellular and Molecular Life Sciences, 2010,67(9):1519-1535.
doi: 10.1007/s00018-010-0266-1
pmid: 20140750
|
|
|
[21] |
Van Audenhove I, Van Impe K, Ruano-Gallego D, et al. Mapping cytoskeletal protein function in cells by means of nanobodies. Cytoskeleton, 2013,70(10):604-622.
doi: 10.1002/cm.21122
pmid: 23818458
|
|
|
[22] |
Su C, Nguyen V K, Nei M. Adaptive evolution of variable region genes encoding an unusual type of immunoglobulin in camelids. Molecular Biology and Evolution, 2002,19(3):205-215.
doi: 10.1093/oxfordjournals.molbev.a004073
pmid: 11861879
|
|
|
[23] |
Harmsen M M, Ruuls R C, Nijman I J, et al. Llama heavy-chain v regions consist of at least four distinct subfamilies revealing novel sequence features. Molecular Immunology, 2000,37(10):579-590.
doi: 10.1016/s0161-5890(00)00081-x
pmid: 11163394
|
|
|
[24] |
Vincke C, Loris R, Saerens D, et al. General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold. Journal of Biological Chemistry, 2009,284(5):3273-3284.
doi: 10.1074/jbc.M806889200
pmid: 19010777
|
|
|
[25] |
Vaneycken I, Govaert J, Vincke C, et al. In vitro analysis and in vivo tumor targeting of a humanized, grafted nanobody in mice using pinhole spect/micro-ct. Journal of Nuclear Medicine, 2010,51(7):1099-1106.
doi: 10.2967/jnumed.109.069823
pmid: 20554727
|
|
|
[26] |
Liu W, Song H, Chen Q, et al. Recent advances in the selection and identification of antigen-specific nanobodies. Molecular Immunology, 2018,96:37-47.
doi: 10.1016/j.molimm.2018.02.012
pmid: 29477934
|
|
|
[27] |
Salvador J P, Vilaplana L, Marco M P. Nanobody: outstanding features for diagnostic and therapeutic applications. Analytical and Bioanalytical Chemistry, 2019,411(9):1703-1713.
doi: 10.1007/s00216-019-01633-4
pmid: 30734854
|
|
|
[28] |
Sheehan J, Marasco W A. Phage and yeast display, 2015,3(1).
|
|
|
[29] |
Hussack G, Baral T N, Baardsnes J, et al. A novel affinity tag, abtag, and its application to the affinity screening of single-domain antibodies selected by phage display. Frontiers in Immunology, 2017,8:1406-1406.
doi: 10.3389/fimmu.2017.01406
pmid: 29163485
|
|
|
[30] |
Koide A, Tereshko V, Uysal S, et al. Exploring the capacity of minimalist protein interfaces: interface energetics and affinity maturation to picomolar kd of a single-domain antibody with a flat paratope. Journal of Molecular Biology, 2007,373(4):941-953.
doi: 10.1016/j.jmb.2007.08.027
pmid: 17888451
|
|
|
[31] |
Li M, Fan X, Liu J, et al. Selection by phage display of nanobodies directed against hypoxia inducible factor-1α (hif-1α). Biotechnology and Applied Biochemistry, 2015,62(6):738-45.
doi: 10.1002/bab.1340
pmid: 25556956
|
|
|
[32] |
Vanmarsenille C, Del Olmo I D, Elseviers J, et al. Nanobodies targeting conserved epitopes on the major outer membrane protein of campylobacter as potential tools for control of campylobacter colonization. Veterinary Research, 2017,48(1):86.
doi: 10.1186/s13567-017-0491-9
pmid: 29216932
|
|
|
[33] |
Keller M A, Stiehm E R. Passive immunity in prevention and treatment of infectious diseases. Clinical Microbiology Reviews, 2000,13(4):602-614.
doi: 10.1128/cmr.13.4.602-614.2000
pmid: 11023960
|
|
|
[34] |
Ruano-Gallego D, Yara D A, Di Ianni L, et al. A nanobody targeting the translocated intimin receptor inhibits the attachment of enterohemorrhagic E. Coli to human colonic mucosa. PLoS Pathogens, 2019,15(8):e1008031.
doi: 10.1371/journal.ppat.1008031
pmid: 31465434
|
|
|
[35] |
Bakshi S, Garcia R S, Van Der Weken H, et al. Evaluating single-domain antibodies as carriers for targeted vaccine delivery to the small intestinal epithelium. Journal of Controlled Release, 2020,321:416-429.
doi: 10.1016/j.jconrel.2020.01.033
pmid: 31981657
|
|
|
[36] |
Van Der Vaart J M, Pant N, Wolvers D, et al. Reduction in morbidity of rotavirus induced diarrhoea in mice by yeast produced monovalent llama-derived antibody fragments. Vaccine, 2006,24(19):4130-4137.
doi: 10.1016/j.vaccine.2006.02.045
pmid: 16616802
|
|
|
[37] |
Martin M C, Pant N, Ladero V, et al. Integrative expression system for delivery of antibody fragments by lactobacilli. Applied and Environmental Microbiology, 2011,77(6):2174-2179.
doi: 10.1128/AEM.02690-10
pmid: 21257814
|
|
|
[38] |
Tokuhara D, Alvarez B, Mejima M, et al. Rice-based oral antibody fragment prophylaxis and therapy against rotavirus infection. Journal of Clinical Investigation, 2013,123(9):3829-3838.
doi: 10.1172/JCI70266
pmid: 23925294
|
|
|
[39] |
Gray E R, Brookes J C, Caillat C, et al. Unravelling the molecular basis of high affinity nanobodies against hiv p24: in vitro functional, structural, and in silico insights. ACS Infectious Diseases, 2017,3(7):479-491.
doi: 10.1021/acsinfecdis.6b00189
pmid: 28591513
|
|
|
[40] |
Zhu M, Gong X, Hu Y, et al. Streptavidin-biotin-based directional double nanobody sandwich elisa for clinical rapid and sensitive detection of influenza h5n1. Journal of Translational Medicine, 2014,12:352.
doi: 10.1186/s12967-014-0352-5
pmid: 25526777
|
|
|
[41] |
Rasoulinejad S, Gargari S L M. Aptamer-nanobody based elasa for specific detection of acinetobacter baumannii isolates. Journal of Biotechnology, 2016,231:46-54.
doi: 10.1016/j.jbiotec.2016.05.024
pmid: 27234880
|
|
|
[42] |
Deckers N, Saerens D, Kanobana K, et al. Nanobodies, a promising tool for species-specific diagnosis of taenia solium cysticercosis. International Journal for Parasitology, 2009,39(5):625-633.
doi: 10.1016/j.ijpara.2008.10.012
pmid: 19041315
|
|
|
[43] |
He Y, Ren Y, Guo B, et al. Development of a specific nanobody and its application in rapid and selective determination of salmonella enteritidis in milk. Food Chemistry, 2020,310:125942.
doi: 10.1016/j.foodchem.2019.125942
pmid: 31830714
|
|
|
[44] |
Melli L J, Zylberman V, Hiriart Y, et al. Development and evaluation of a novel vhh-based immunocapture assay for high-sensitivity detection of shiga toxin type 2 (stx2) in stool samples. Journal of Clinical Microbiology, 2020,58(3):e01566-19.
doi: 10.1128/JCM.01566-19
pmid: 31826960
|
|
|
[45] |
Cao J, Zhong N, Wang G, et al. Nanobody-based sandwich reporter system for living cell sensing influenza a virus infection. Scientific Reports, 2019,9(1):15899.
doi: 10.1038/s41598-019-52258-7
pmid: 31685871
|
|
|
[46] |
Caljon G, Caveliers V, Lahoutte T, et al. Using microdialysis to analyse the passage of monovalent nanobodies through the blood-brain barrier. British Journal of Pharmacology, 2012,165(7):2341-2353.
doi: 10.1111/j.1476-5381.2011.01723.x
pmid: 22013955
|
|
|
[47] |
Nye S, Whitley R J, Kong M. Viral infection in the development and progression of pediatric acute respiratory distress syndrome. Frontiers in Pediatrics, 2016,4:128.
doi: 10.3389/fped.2016.00128
pmid: 27933286
|
|
|
[48] |
Detalle L, Stohr T, Palomo C, et al. Generation and characterization of alx-0171, a potent novel therapeutic nanobody for the treatment of respiratory syncytial virus infection. Antimicrobial Agents and Chemotherapy, 2016,60(1):6-13.
doi: 10.1128/AAC.01802-15
pmid: 26438495
|
|
|
[49] |
Mora A L, Detalle L, Gallup J M, et al. Delivery of alx-0171 by inhalation greatly reduces respiratory syncytial virus disease in newborn lambs. mAbs, 2018,10(5):778-795.
doi: 10.1080/19420862.2018.1470727
pmid: 29733750
|
|
|
[50] |
Palomo C, Mas V, Detalle L, et al. Trivalency of a nanobody specific for the human respiratory syncytial virus fusion glycoprotein drastically enhances virus neutralization and impacts escape mutant selection. Antimicrobial Agents and Chemotherapy, 2016,60(11):6498-6509.
doi: 10.1128/AAC.00842-16
pmid: 27550346
|
|
|
[51] |
Broadbent L, Parke H G, Ferguson L J, et al. Comparative therapeutic potential of alx-0171 and palivizumab against rsv clinical isolate infection of well-differentiated primary pediatric bronchial epithelial cell cultures. Bio Rxiv, 2019: 800326.
|
|
|
[52] |
Tillib S V, Ivanova T I, Vasilev L A, et al. Formatted single-domain antibodies can protect mice against infection with influenza virus (h5n2). Antiviral Research, 2013,97(3):245-254.
doi: 10.1016/j.antiviral.2012.12.014
pmid: 23274623
|
|
|
[53] |
Tome-Amat J, Ramos I, Amanor F, et al. Influenza a virus utilizes low-affinity, high-avidity interactions with the nuclear import machinery to ensure infection and immune evasion. Journal of Virology, 2019,93(1):e01046.
doi: 10.1128/JVI.01046-18
pmid: 30305352
|
|
|
[54] |
Ibanez L I, De Filette M, Hultberg A, et al. Nanobodies with in vitro neutralizing activity protect mice against h5n1 influenza virus infection. The Journal of Infectious Diseases, 2011,203(8):1063-1072.
doi: 10.1093/infdis/jiq168
pmid: 21450996
|
|
|
[55] |
Wei G, Meng W, Guo H, et al. Potent neutralization of influenza a virus by a single-domain antibody blocking m2 ion channel protein. PLoS One, 2011,6(12):e28309.
doi: 10.1371/journal.pone.0028309
pmid: 22164266
|
|
|
[56] |
Laursen N S, Friesen R H E, Zhu X, et al. Universal protection against influenza infection by a multidomain antibody to influenza hemagglutinin. Science, 2018,362(6414):598-602.
doi: 10.1126/science.aaq0620
pmid: 30385580
|
|
|
[57] |
Stalin Raj V, Okba N M A, Gutierrez-Alvarez J, et al. Chimeric camel/human heavy-chain antibodies protect against mers-cov infection. Science Advances, 2018, 4(8): eaas9667.
doi: 10.1126/sciadv.aas9667
pmid: 30101189
|
|
|
[58] |
Wrapp D, De Vlieger D, Corbett K S, et al. Structural basis for potent neutralization of betacoronaviruses by single-domain camelid antibodies. Cell, 2020,181(5):1004-1015.
doi: 10.1016/j.cell.2020.04.031
pmid: 32375025
|
|
|
[59] |
Zhao G Y, He L, Sun S H, et al. 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, 2018,92(18):e00837.
doi: 10.1128/JVI.00837-18
pmid: 29950421
|
|
|
[60] |
Dong J, Huang B, Jia Z, et al. Development of multi-specific humanized llama antibodies blocking sars-cov-2/ace2 interaction with high affinity and avidity. Emerg Microbes Infect, 2020,9(1):1034-1036.
doi: 10.1080/22221751.2020.1768806
pmid: 32403995
|
|
|
[61] |
Limited B G. Beroni group r&d team identifies 24 types of nanobodies for rapid detection and treatment of coronavirus (covid-19). [2020-05-08]. https://www.globenewswire.com/news-release/2020/05/08/2030400/0/en/Beroni-Group-R-D-Team-Identifies-24-Types-of-Nanobodies-for-Rapid-Detection-and-Treatment-of-Coronavirus-COVID-19.html.
|
|
|
[62] |
Wrapp D, De Vlieger D, Corbett K S, et al. Structural basis for potent neutralization of betacoronaviruses by single-domain camelid antibodies. Cell, 2020, 181(5): 1004-1015.e15.
doi: 10.1016/j.cell.2020.04.031
pmid: 32375025
|
|
|
[63] |
Huo J, Le Bas A, Ruza R R, et al. Neutralizing nanobodies bind sars-cov-2 spike rbd and block interaction with ace2. Nature Structural & Molecular Biology, 2020.
doi: 10.1038/s41594-020-0504-7
pmid: 32958947
|
|
|
[64] |
Walter J D, Hutter C a J, Zimmermann I, et al. Synthetic nanobodies targeting the sars-cov-2 receptor-binding domain. Bio Rxiv, 2020: 2020.04.16.045419.
|
|
|
[65] |
Nieto G V, Jara R, Himelreichs J, et al. Fast isolation of sub-nanomolar affinity alpaca nanobody against the spike rbd of sars-cov-2 by combining bacterial display and a simple single-step density gradient selection. Bio Rxiv, 2020: 2020.06.09.137935.
|
|
|
[66] |
Li T, Cai H, Yao H, et al. Potent synthetic nanobodies against sars-cov-2 and molecular basis for neutralization. Bio Rxiv, 2020: 2020.06.09.143438.
|
|
|
[67] |
Custódio T F, Das H, Sheward D J, et al. Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize sars-cov-2. Bio Rxiv, 2020: 2020.06.23.165415.
|
|
|
[68] |
Hanke L, Vidakovics M, Sheward D, et al. An alpaca nanobody neutralizes sars-cov-2 by blocking receptor interaction. 2020.
|
|
|
[69] |
Matz J, Kessler P, Bouchet J, et al. Straightforward selection of broadly neutralizing single-domain antibodies targeting the conserved cd4 and coreceptor binding sites of hiv-1 gp120. Journal of Virology, 2013,87(2):1137-1149.
doi: 10.1128/JVI.00461-12
pmid: 23152508
|
|
|
[70] |
Koch K, Kalusche S, Torres J L, et al. Selection of nanobodies with broad neutralizing potential against primary hiv-1 strains using soluble subtype c gp140 envelope trimers. Scientific Reports, 2017,7(1):8390.
doi: 10.1038/s41598-017-08273-7
pmid: 28827559
|
|
|
[71] |
Weiss R A, Verrips C T. Nanobodies that neutralize hiv. Vaccines, 2019,7(3):77.
doi: 10.3390/vaccines7030077
|
|
|
[72] |
Van Hout A, Klarenbeek A, Bobkov V, et al. Cxcr4-targeting nanobodies differentially inhibit cxcr4 function and hiv entry. Biochemical Pharmacology, 2018,158:402-412.
doi: 10.1016/j.bcp.2018.10.015
pmid: 30342024
|
|
|
[73] |
Boons E, Li G, Vanstreels E, et al. A stably expressed llama single-domain intrabody targeting rev displays broad-spectrum anti-hiv activity. Antiviral Research, 2014,112:91-102.
doi: 10.1016/j.antiviral.2014.10.007
pmid: 25453342
|
|
|
[74] |
Lutje Hulsik D, Liu Y Y, Strokappe N M, et al. A gp41 mper-specific llama vhh requires a hydrophobic cdr3 for neutralization but not for antigen recognition. PLoS Pathogens, 2013,9(3):e1003202.
doi: 10.1371/journal.ppat.1003202
pmid: 23505368
|
|
|
[75] |
Daka A, Peer D. Rnai-based nanomedicines for targeted personalized therapy. Advanced Drug Delivery Reviews, 2012,64(13):1508-1521.
doi: 10.1016/j.addr.2012.08.014
pmid: 22975009
|
|
|
[76] |
Cunha-Santos C, Perdigao P R L, Martin F, et al. Inhibition of hiv replication through sirna carried by cxcr4-targeted chimeric nanobody. Cellular and Molecular Life Sciences, 2019.
doi: 10.1007/s00018-020-03678-6
pmid: 33078208
|
|
|
[77] |
Li S F, Zhang W, Jiang K P, et al. Nanobody against the e7 oncoprotein of human papillomavirus 16. Molecular Immunology, 2019,109:12-19.
doi: 10.1016/j.molimm.2019.02.022
pmid: 30849663
|
|
|
[78] |
Woodham A W, Cheloha R W, Ling J J, et al. Nanobody-antigen conjugates elicit hpv-specific antitumor immune responses. Cancer Immunology Research, 2018,6(7):870-880.
doi: 10.1158/2326-6066.CIR-17-0661
pmid: 29792298
|
|
|
[79] |
De Martel C, Ferlay J, Franceschi S, et al. Global burden of cancers attributable to infections in 2008: a review and synthetic analysis. The Lancet Oncology, 2012,13(6):607-615.
doi: 10.1016/S1470-2045(12)70137-7
pmid: 22575588
|
|
|
[80] |
Walsh R, Nuttall S, Revill P, et al. Targeting the hepatitis b virus precore antigen with a novel ignar single variable domain intrabody. Virology, 2011,411(1):132-141.
doi: 10.1016/j.virol.2010.12.034
pmid: 21239030
|
|
|
[81] |
Tarr A W, Lafaye P, Meredith L, et al. An alpaca nanobody inhibits hepatitis c virus entry and cell-to-cell transmission. Hepatology, 2013,58(3):932-939.
doi: 10.1002/hep.26430
pmid: 23553604
|
|
|
[82] |
Koromyslova A D, Hausman G S. Nanobodies targeting norovirus capsid reveal functional epitopes and potential mechanisms of neutralization. Biophysical Journal, 2018,114(3):219a-219a.
|
|
|
[83] |
Geoghegan E M, Zhang H, Desai P J, et al. Antiviral activity of a single-domain antibody immunotoxin binding to glycoprotein d of herpes simplex virus 2. Antimicrobial Agents and Chemotherapy, 2015,59(1):527-535.
doi: 10.1128/AAC.03818-14
pmid: 25385102
|
|
|
[84] |
Conrath K E, Lauwereys M, Galleni M, et al. Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae. Antimicrobial Agents and Chemotherapy, 2001,45(10):2807-2812.
doi: 10.1128/AAC.45.10.2807-2812.2001
pmid: 11557473
|
|
|
[85] |
Barta M L, Shearer J P, Arizmendi O, et al. Single-domain antibodies pinpoint potential targets within shigella invasion plasmid antigen d of the needle tip complex for inhibition of type iii secretion. Journal of Biological Chemistry, 2017,292(40):16677-16687.
doi: 10.1074/jbc.M117.802231
pmid: 28842484
|
|
|
[86] |
King M T, Huh I, Shenai A, et al. Structural basis of vhh-mediated neutralization of the food-borne pathogen listeria monocytogenes. Journal of Biological Chemistry, 2018,293(35):13626-13635.
doi: 10.1074/jbc.RA118.003888
pmid: 29976754
|
|
|
[87] |
Ebrahimizadeh W, Mousavi Gargari S, Rajabibazl M, et al. Isolation and characterization of protective anti-lps nanobody against v. Cholerae o1 recognizing inaba and ogawa serotypes. Applied Microbiology and Biotechnology, 2013,97(10):4457-4466.
doi: 10.1007/s00253-012-4518-x
pmid: 23135228
|
|
|
[88] |
Baral T N, Magez S, Stijlemans B, et al. Experimental therapy of african trypanosomiasis with a nanobody-conjugated human trypanolytic factor. Nature Medicine, 2006,12(5):580-584.
doi: 10.1038/nm1395
pmid: 16604085
|
|
|
[89] |
Arias J L Unciti-Broceta J D Maceira J, et al. Nanobody conjugated plga nanoparticles for active targeting of african trypanosomiasis. Journal of Controlled Release, 2015,197:190-198.
doi: 10.1016/j.jconrel.2014.11.002
pmid: 25445702
|
|
|
[90] |
Unciti-Broceta J D, Arias J L, Maceira J, et al. Specific cell targeting therapy bypasses drug resistance mechanisms in african trypanosomiasis. PLoS Pathogens, 2015,11(6):e1004942.
doi: 10.1371/journal.ppat.1004942
pmid: 26110623
|
|
|
[91] |
Wu Y, Jiang S, Ying T. Single-domain antibodies as therapeutics against human viral diseases. Frontiers in Immunology, 2017,8:1802.
doi: 10.3389/fimmu.2017.01802
pmid: 29326699
|
|
|
[92] |
Keyaerts M, Xavier C, Heemskerk J, et al. Phase i study of 68ga-her2-nanobody for pet/ct assessment of her2 expression in breast carcinoma. Journal of Nuclear Medicine, 2016,57(1):27-33.
doi: 10.2967/jnumed.115.162024
pmid: 26449837
|
|
|
[93] |
Lemke J, Von Karstedt S, Zinngrebe J, et al. Getting trail back on track for cancer therapy. Cell Death and Differentiation, 2014,21(9):1350-1364.
doi: 10.1038/cdd.2014.81
pmid: 24948009
|
|
|
[94] |
Wu Y, Li C, Xia S, et al. Identification of human single-domain antibodies against sars-cov-2. Cell Host & Microbe, 2020, 27(6): 891-898.e5.
doi: 10.1016/j.chom.2020.04.023
pmid: 32413276
|
|
|
[95] |
Dolk E, Van Der Vaart M, Lutje Hulsik D, et al. Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo. Applied and Environmental Microbiology, 2005,71(1):442-450.
doi: 10.1128/AEM.71.1.442-450.2005
pmid: 15640220
|
|
|
[96] |
2018新型抗体药物论坛. 传遍了朋友圈的羊驼-纳米抗体平台究竟是什么.[ 2018-10-26]. http://meeting.bioon.com/2018NA/news-detail/c8098462ec0323e6.
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