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😷 | The third vaccine is “cross vaccination”, and the distribution in February and March is more than XNUMX% of Moderna Kumamoto Prefecture.


Photo Deputy Governor Kei Kimura explaining the third inoculation of the new coronavirus vaccine = XNUMXth, prefectural office

"Cross-inoculation" for the third vaccine is also available in February and March.

 
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The prefecture said that both companies' products are mRNA vaccines, "It is reported by the national council that cross-vaccination increases the number of neutralizing antibodies that prevent infection and the degree of side reactions does not change."
 

On the XNUMXth, Kumamoto Prefecture said about the third inoculation of the new corona vaccine, what is the first and second vaccine after February next year ... → Continue reading

 Kumamoto Daily Newspaper

The Kumamoto Nichinichi Shimbun is a local newspaper in Kumamoto. Full of information about Kumamoto such as news and sports.


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Cross inoculation

Neutralizing antibody

Neutralizing antibody(Chuwa Kotai,British: neutralizing antibody, NAb) IsPathogenAnd infectious particles細胞Protects cells by neutralizing their biological effects onantibodyIs.Pathogens and infectious particles lose infectivity and pathogenicity due to neutralization[3]..Neutralizing antibodyウ イ ル ス,Intracellular bacteria,(English editionAgainstAdaptive immune system OfFluidPart of the response.Neutralizing antibodies are the surface structure of infectious particles (antigen) By specifically bindingHostPrevents interactions that can infect and destroy cells.By neutralizing antibodyImmunologyBecause the immune system eliminates infected particles before infection occursSterilization immunity(British: sterilizing immunity) Also known as[4].

mechanism

Viral particles and intracellular bacteria utilize molecules on their surface to enter the cell of the target cell.Cell surface receptorInteracts with and invades the cellReplication cycleTo start[5]..Neutralizing antibodies can bind to pathogens, inhibit infectivity, and block molecules required for cell entry.This is due to the static interference of antibodies against the attachment of pathogens and toxins to receptors on host cells.In the case of viral infection, neutralizing antibody (NAb)Envelope virusOf glycoproteins or non-enveloped virusesCapsid proteinCan be combined with.In addition, neutralizing antibodies can act to prevent structural changes that are often required for particles to successfully enter cells.For example, neutralizing antibodies mediate the membrane fusion required for entry into host cells.Viral protein OfStructural changeCan be prevented.In some cases, the virus cannot infect even after the antibody has dissociated.The pathogen-antibody complex is eventually taken up by macrophages and degraded.[6].

Neutralizing antibodies are also important in neutralizing the toxic effects of bacterial toxins.An example of a neutralizing antibodyDiphtheria antitoxinAnd this isDiphtheria toxinCan neutralize the biological effects of[7]..Neutralizing antibodies are not effective against extracellular bacteria because the binding of the antibody does not interfere with bacterial replication.Here, the immune systemOpsonization,complementOther antibodies, such as activationFeaturesKill bacteria using[8].

Difference between neutralizing antibody and binding antibody

Not all antibodies that bind to pathogenic particles are neutralizing antibodies.Non-neutralizing antibodies (ie, binding antibodies) specifically bind to the pathogen but do not interfere with the infectivity of the pathogen.This can be due to not binding to the proper area.The non-neutralizing antibody flagged the particle and that it was targetedImmune CellsPlays an important role in informing against.The particles are then processed and, as a result, destroyed by the mobilized immune cells.[9]..Neutralizing antibodies, on the other hand, can neutralize the biological effects of antigens without the need for immune cells.In some cases, non-neutralizing antibodies or inadequate amounts of neutralizing antibodies bound to viral particles may be utilized by several viral species to facilitate uptake into host cells. ..This mechanismAntibody-dependent enhancement of infectionKnown as[10]. this isDengue virus,Zika virusObserved in[11].

Production

AntibodiesB cellsProduced and secreted by. B cellsBone marrowWhen produced in, the gene encoding the antibody is randomGenetic recombination(V (D) J gene rearrangement), As a result, all mature B cells(English edition Ofamino acidThe array is differentantibodyTo produce.Therefore, all B cells produce antibodies that specifically bind to different antigens.[12]..The strong diversity of the antibody repertoire allows the immune system to recognize pathogens of various morphologies and sizes.At the time of infection, only antibodies that bind with high affinity to pathogenic antigens are produced.This is a single B cell cloneClonal selectionRealized by. B cellsInnate immune responseReleased from infected cells as part ofinterferonIs detected and mobilized to the infected site. B cells are just antibodies immobilized on the cell membraneB cell receptorIs presented on the cell surface. When the B cell receptor binds to a high affinity allogeneic antigen,Intracellular signal transductionCascade is triggered.In addition to binding to antigens, the immune system against pathogens細胞As part of the response, B cellsHelper T cellsProduced byCytokineIt also needs to be stimulated by. When B cells are fully activated, they proliferate rapidly.Plasma cellsDifferentiate into.The plasma cells then secrete large amounts of antigen-specific antibodies.[13]..After the first encounter with the antigen by vaccination or natural infectionImmunological memoryThis allows the neutralizing antibody to be produced more rapidly after the next exposure to the virus.

Virus neutralizing antibody avoidance

Viruses use various mechanisms to produce neutralizing antibodiesAvoidanceTo[14]..Of the virusgenomeIs at a high rateMutationTo do.Mutations that allow the virus to evade neutralizing antibodies are selected, thereby predominant.Conversely, antibodies are in the process of immune responseAffinity maturationEvolves at the same time, thereby improving the recognition of viral particles.Conserved parts of viral proteins that play a central role in viral function are less likely to evolve over time and are therefore more vulnerable to antibody binding.However, the virus has antibodies in these areasThree-dimensionalIt has evolved specific mechanisms for access to, making it difficult to combine.Antibodies are difficult to bind to viruses with a low density of surface structural proteins.Some viral glycoproteins are N- and O-linkedGlycosIs highly glycosylated to form the so-called glycan shield.This may reduce antibody binding affinity and promote avoidance of neutralizing antibodies.HumanAIDSIs the cause ofHIV-1Utilizes both of these mechanisms[15][16].

Medical use of neutralizing antibodies

Neutralizing antibodyPassive immunityIt can be used in patients without having a healthy immune system. In the early 20th century, infected patientsAntiserumWas being injected.Antisera against infectious pathogensPolyclonal antibodyOf patients who have previously been infected and recovered, includingserumIs.This indicates that the antibody can be used as an effective treatment for viral infections and toxins.[17]..Antisera are a very crude treatment because antibodies in plasma have not been purified or standardized and plasma can be rejected by donors.[18]..It also depends on donations from recovered patients and cannot be easily scaled up.However, because serum therapy is available relatively quickly, it is still used today as the first line of defense in the event of an outbreak.[19][20]..Serum therapy2009 Swine Flu Global Epidemic[21]AndWest African Ebola hemorrhagic fever epidemic[22]At that time, it was shown to reduce patient mortality.Also,COVID-19Is being tested as a promising treatment for[23][24]..Use a mixture of antibodies obtained from a healthy personImmunoglobulin therapyTo fight infectious diseasesImmunodeficiencyorImmunosuppressionIt is administered to patients who have been treated.   

Purified for more specific and robust treatmentPolyclonal antibodyorMonoclonal antibody(MAb) can be used.Polyclonal antibodies target the same pathogen, but differEpitopeA collection of antibodies that bind to.Polyclonal antibodies are obtained from human donors or animals exposed to the antigen.Antigens injected into animal donors are designed to produce neutralizing antibodies as much as possible.[25]..Polyclonal antibodyCytomegalovirus(CMV),Hepatitis B virus(HBV),Rabies virus,Measles virus,Respiratory syncytial virusHas been used as a remedy for (RSV)[18].Diphtheria antitoxinIsDiphtheria toxinContains polyclonal antibodies against[26]..By treating with an antibody that binds a plurality of epitopes, a therapeutic effect is exhibited even when the virus is mutated and one of the epitopes changes its structure.However, treatment using polyclonal antibodies is convenient for production reasons.(English edition(English editionThere is a problem that is low.Monoclonal antibodies, on the other hand, all bind to the same epitope with high specificity.These antibodies allow mass production of mAbsHybridoma technologyCan be produced in[17]..MAbs for infectious diseases cease to function if the virus mutates the target epitope of the mAb or if multiple strains are in circulation.An example of a drug that uses a monoclonal antibody is against Ebola.ZMap[27], Against RSVPalivizumaband so on[28]..Many mAbs for other infections are in clinical trials.

Neutralizing antibodyVaccinationIt also plays a role in active immunization by.Understanding the binding site and structure of neutralizing antibodies in the innate immune response can rationally design vaccines to stimulate the immune system to produce neutralizing antibodies rather than binding antibodies.[29][30]..Introducing a virus weakened by vaccinationB cellsAllows the production of neutralizing antibodies. After the second exposure, it produces virus-specific antibodiesMemory B cellsThe presence of is a faster neutralizing antibody reaction.Effective vaccines induce the production of antibodies that can neutralize most of the viral variants, but viral mutations that result in antibody evasion require the vaccine to be updated accordingly.[31]..Some viruses evolve faster than others, so vaccines need to be updated accordingly.As a well-known exampleinfluenzaThere is a virus vaccine.This should be updated annually taking into account the recent circulating strains of the virus[14].

Neutralizing antibodyMultiple sclerosisMay also be useful in treating[2]..This type of antibodyRetro virusAbility to fight infections, but in some cases given into the body to treat multiple sclerosisMedicineTo attack.Recombinant protein preparations, especially animal-derived medicines, are generally targeted by neutralizing antibodies.Examples include Rebif, Betaseron, and Avonex.

Methods for Detection and Quantification of Neutralizing Antibodies

Neutralization assay (test)(English edition(Compare the number of viral plaques in the control well with the number of inoculated cultures), microneutralized (filled with a small amount of serum)Microtiter plateDo it in), andColorimetric assay(Depends on biomarkers that indicate viral metabolism inhibition) [32]It can be implemented and measured in a variety of ways, including the use of techniques such as.

Widespread neutralizing antibody

Many of the neutralizing antibodies produced by the immune system are highly specific for a single viral strain due to affinity maturation by B cells.[13].. Some highly genetically variable pathogens, such as HIV, constantly alter their surface structure so that neutralizing antibodies with high specificity to the old strain cannot bind to the new viral strain.Such immune avoidance strategies prevent the immune system from developing immunological memory for pathogens.[33]..Widespread neutralizing antibodies (bNAbs), on the other hand, have the special ability to bind and neutralize multiple strains of viral species.[34].

bNAb was initially discovered in HIV patients[35]..However, bNAb is a very rare entity.on-siteScreening studies (intra-living organisms) showed that only 1% of all patients develop bNAb against HIV.[36].. bNAb can neutralize a wide range of viral strains by binding to conserved regions of viral surface proteins (which cannot be mutated because they are functionally essential for viral replication). Most binding sites for bNAb to HIV are the envelope (Env) protein, which is the exposed surface antigen of HIV.gp120andgp41It is on a trimer consisting of subunits).These sites include the CD4 binding site or the gp41-gp120 interface.[37].Los Alamos National LaboratoryHIV Database is a comprehensive resource with a wealth of information on HIV sequences, bNAbs and more.[38].

In addition, bNAb is influenza[39],Hepatitis C[40],Dengue fever[41],West Nile virus[42]It has also been found in other viruses such as.

Research

Preliminary studies are underway to identify and test bNAb against HIV-1[43].. bNAb is used in rationally designed vaccine studies to stimulate bNAb production and boost immunity to the virus.No known antigens that induce bNAb production in animal models or humans[34].

footnote

[How to use footnotes]
  1. ^ Mike Recher; Karl S Lang; Lukas Hunziker; Stefan Freigang; Bruno Eschli; Nicola L Harris; Alexander Navarini; Beatrice M Senn et al. (8 August 2004). “Deliberate removal of T cell help improves virus-neutralizing antibody production”. Nature Immunology 5 (9): 934–942. two:10.1038 / ni1102. PMID 15300247. http://infoscience.epfl.ch/record/143009. 
  2. ^ a b Stachowiak (August 2008, 8). “Neutralizing Antibodies and Disease-Modifying Therapies for Multiple Sclerosis”. About.com. 2009/6/13Browse.
  3. ^ "Neutralising antibody”. Biology-Online (2008). 2009/7/4Browse.
  4. ^ Dutta, A; Huang, CT; Lin, CY; Chen, TC; Lin, YC; Chang, CS; He, YC (6 September 2016). “Sterilizing immunity to influenza virus infection requires local antigen-specific T cell response in the lungs.”. Scientific Reports 6: 32973. bibcode2016NatSR ... 632973D. two:10.1038 / srep32973. PMC 5011745. PMID 27596047. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5011745/. 
  5. ^ Principles of Virology, Volume 1: Molecular Biology (4th ed.). ASM Press. (2015). P. 31. ISBN 978-1555819330  
  6. ^ Principles of Virology, Volume 2: Pathogenesis and Control (4th ed.). ASM Press. (2015). P. 125. ISBN 978-1-555-81951-4 
  7. ^ Treffers, Henry P. (2014). “Neutralizing antibody”. Access Science (McGraw-Hill). two:10.1036/1097-8542.450600. https://www.accessscience.com/content/neutralizing-antibody/450600. 
  8. ^ Janeway's immunobiology (8th ed.). Garland Science. (2012). P. 388. ISBN 978-0-8153-4243-4 
  9. ^ Schmaljohn, AL (July 2013). “Protective antiviral antibodies that lack neutralizing activity: precedents and evolution of concepts.”. Current HIV Research 11 (5): 345–53. two:10.2174 / 1570162x113116660057. PMID 24191933. 
  10. ^ Tirado, SM; Yoon, KJ (2003). “Antibody-dependent enhancement of virus infection and disease.”. Viral Immunology 16 (1): 69–86. two:10.1089/088282403763635465. PMID 12725690. 
  11. ^ Dejnirattisai, Wanwisa; Supasa, Piyada; Wongwiwat, Wiyada; Rouvinski, Alexander; Barba-Spaeth, Giovanna; Duangchinda, Thaneeya; Sakuntabhai, Anavaj; Cao-Lormeau, Van-Mai et al. (23 June 2016). “Dengue virus sero-cross-reactivity drives antibody-dependent enhancement of infection with zika virus”. Nature Immunology 17 (9): 1102–1108. two:10.1038 / ni.3515. PMC 4994874. PMID 27339099. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4994874/. 
  12. ^ Jung, David; Alt, Frederick W (January 2004). “Unraveling V (D) J Recombination”. Cell 116 (2): 299–311. two:10.1016 / S0092-8674 (04) 00039-X. PMID 14744439. 
  13. ^ a b Janeway's immunobiology (8th ed.). Garland Science. (2012). Pp. 389–404. ISBN 978-0-8153-4243-4 
  14. ^ a b VanBlargan, Laura A .; Goo, Leslie; Pierson, Theodore C. (2016). “Deconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and Immunity” (English). Microbiology and Molecular Biology Reviews 80 (4): 989–1010. two:10.1128 / MMBR.00024-15. ISSN 1092-2172 . PMC 5116878. PMID 27784796. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5116878/. 
  15. ^ Crispin, Max; Ward, Andrew B .; Wilson, Ian A. (2018-05-20). “Structure and Immune Recognition of the HIV Glycan Shield” (English). Annual Review of Biophysics 47 (1): 499–523. two:10.1146 / annulev-biophys-060414-034156. ISSN 1936-122X. PMC 6163090. PMID 29595997. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6163090/. 
  16. ^ Guha, Debjani; Ayyavoo, Velpandi (2013). “Innate Immune Evasion Strategies by Human Immunodeficiency Virus Type 1” (English). ISRN AIDS 2013: 954806. two:10.1155/2013/954806. ISSN 2090-939X. PMC 3767209. PMID 24052891. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3767209/. 
  17. ^ a b Salazar, Georgina; Zhang, Ningyan; Fu, Tong-Ming; An, Zhiqiang (10 July 2017). “Antibody therapies for the prevention and treatment of viral infections”. NPJ Vaccines 2 (1): 19. two:10.1038 / s41541-017-0019-3. PMC 5627241. PMID 29263875. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5627241/. 
  18. ^ a b Casadevall, A; Dadachova, E; Pirofski, LA (September 2004). “Passive antibody therapy for infectious diseases.”. Nature Reviews. Microbiology 2 (9): 695–703. two:10.1038 / nrmicro974. PMID 15372080. 
  19. ^ Kreil, Thomas R. (March 2015). “Treatment of Ebola Virus Infection with Antibodies from Reconvalescent Donors”. Emerging Infectious Diseases 21 (3): 521–523. two:10.3201 / eid2103.141838. PMID 25695274. 
  20. ^ Schmidt, Rebecca; Beltzig, Lea C .; Sawatsky, Bevan; Dolnik, Olga; Dietzel, Erik; Krähling, Verena; Volz, Asisa; Sutter, Gerd et al. (5 October 2018). “Generation of therapeutic antisera for emerging viral infections ”. NPJ Vaccines 3 (1). two:10.1038 / s41541-018-0082-4. PMID 30323953. 
  21. ^ Hung, IF; To, KK; Lee, C.-K .; Lee, K.-L .; Chan, K .; Yan, W.-W .; Liu, R .; Watt, C.-L. Et al. (19 January 2011). “Convalescent Plasma Treatment Reduced Mortality in Patients With Severe Pandemic Influenza A (H1N1) 2009 Virus Infection”. Clinical Infectious Diseases 52 (4): 447–456. two:10.1093 / cid / ciq106. PMID 21248066. 
  22. ^ World Health Organization. “WHO | Use of convalescent whole blood or plasma collected from patients recovered from Ebola virus disease". WHO. 2020/4/5Browse.
  23. ^ Shen, Chenguang; Wang, Zhaoqin; Zhao, Fang; Yang, Yang; Li, Jinxiu; Yuan, Jing; Wang, Fuxiang; Li, Delin et al. (27 March 2020). “Treatment of 5 Critically Ill Patients With COVID-19 With Convalescent Plasma”. JAMA 323 (16): 1582. two:10.1001 / jama.2020.4783. PMC 7101507. PMID 32219428. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7101507/. 
  24. ^ Casadevall, Arturo; Pirofski, Liise-anne (13 March 2020). “The convalescent sera option for containing COVID-19”. Journal of Clinical Investigation 130 (4): 1545–1548. two:10.1172 / JCI138003. PMID 32167489. 
  25. ^ Bregenholt, S; Jensen, A; Lantto, J; Hyldig, S; Haurum, JS (2006). “Recombinant human polyclonal antibodies: A new class of therapeutic antibodies against viral infections.”. Current Pharmaceutical Design 12 (16): 2007–15. two:10.2174/138161206777442173. PMID 16787244. 
  26. ^ "Our Formulary". Infectious Diseases Laboratories. Centers for Disease Control and Prevention. As of December 2016, 12オ リ ジ ナ ルMore archives.2016/12/9Browse.
  27. ^ “A Randomized, Controlled Trial of ZMapp for Ebola Virus Infection”. New England Journal of Medicine 375 (15): 1448–1456. (13 October 2016). two:10.1056 / NEJMoa1604330. PMC 5086427. PMID 27732819. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5086427/. 
  28. ^ "Label --Palivizumab (Synagis), Medimmune, Incorporated". 2020/2/4Browse.
  29. ^ VanBlargan, Laura A .; Goo, Leslie; Pierson, Theodore C. (26 October 2016). “Deconstructing the Antiviral Neutralizing-Antibody Response: Implications for Vaccine Development and Immunity”. Microbiology and Molecular Biology Reviews 80 (4): 989–1010. two:10.1128 / MMBR.00024-15. PMID 27784796. 
  30. ^ Kwong, PD; Mascola, JR; Nabel, GJ (1 September 2011). “Rational Design of Vaccines to Elicit Broadly Neutralizing Antibodies to HIV-1”. Cold Spring Harbor Perspectives in Medicine 1 (1): a007278. two:10.1101 / cshperspect.a007278. PMID 22229123. 
  31. ^ Burton, Dennis R. (2002). “Antibodies, viruses and vaccines”. Nature Reviews Immunology 2 (9): 706–713. two:10.1038 / nri891. ISSN 1474-1733 . PMID 12209139. 
  32. ^ Kaslow, RA, ed (2014). Viral Infections of Humans: Epidemiology and Control (5th ed.). Springer. P. 56. ISBN 9781489974488. https://books.google.com/books?id=sxakBAAAQBAJ&pg=PA56 2020/4/4Browse. 
  33. ^ Santoro, MM; Perno, CF (2013). “HIV-1 Genetic Variability and Clinical Implications.”. ISRN Microbiology 2013: 481314. two:10.1155/2013/481314. PMC 3703378. PMID 23844315. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3703378/. 
  34. ^ a b Kumar, R; Qureshi, H; Deshpande, S; Bhattacharya, J (August 2018). “Broadly neutralizing antibodies in HIV-1 treatment and prevention.”. Therapeutic Advances in Vaccines and Immunotherapy 6 (4): 61–68. two:10.1177/2515135518800689. PMC 6187420. PMID 30345419. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6187420/. 
  35. ^ Cohen, J. (2013). “Bound for Glory”. Science 341 (6151): 1168–1171. bibcode2013Sci ... 341.1168C. two:10.1126 / science.341.6151.1168. PMID 24030996. 
  36. ^ Simek, MD; Rida, W; Priddy, FH; Pung, P; Carrow, E; Laufer, DS; Lehrman, JK; Boaz, M et al. (July 2009). “Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm.”. Journal of Virology 83 (14): 7337–48. two:10.1128 / JVI.00110-09. PMC 2704778. PMID 19439467. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2704778/. 
  37. ^ Haynes, Barton F .; Burton, Dennis R .; Mascola, John R. (30 October 2019). “Multiple roles for HIV broadly neutralizing antibodies”. Science Translational Medicine 11 (516): eaaz2686. two:10.1126 / scitranslmed.aaz2686. PMC 7171597. PMID 31666399. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7171597/. 
  38. ^ "HIV Databases”. Los Alamos National Laboratory. 2021/1/12Browse.
  39. ^ Corti, D; Cameroni, E; Guarino, B; Kallewaard, NL; Zhu, Q; Lanzavecchia, A (June 2017). “Tackling influenza with broadly neutralizing antibodies.”. Current Opinion in Virology 24: 60–69. two:10.1016 / j.coviro.2017.03.002. PMC 7102826. PMID 28527859. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7102826/. 
  40. ^ Colbert, MD; Flyak, AI; Ogega, CO; Kinchen, VJ; Massaccesi, G; Hernandez, M; Davidson, E; Doranz, BJ et al. (15 July 2019). “Broadly Neutralizing Antibodies Targeting New Sites of Vulnerability in Hepatitis C Virus E1E2.”. Journal of Virology 93 (14). two:10.1128 / JVI.02070-18. PMC 6600205. PMID 31068427. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6600205/. 
  41. ^ Durham, ND; Agrawal, A; Waltari, E; Croote, D; Zanini, F; Fouch, M; Davidson, E; Smith, O et al. (10 December 2019). “Broadly neutralizing human antibodies against dengue virus identified by single B cell transcriptomics.”. eLife 8. two:10.7554 / eLife.52384. PMC 6927745. PMID 31820734. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927745/. 
  42. ^ Goo, L; Debbink, K; Kose, N; Sapparapu, G; Doyle, MP; Wessel, AW; Richner, JM; Burgomaster, KE et al. (January 2019). “A protective human monoclonal antibody targeting the West Nile virus E protein preferentially recognizes mature virions.”. Nature Microbiology 4 (1): 71–77. two:10.1038 / s41564-018-0283-7. PMC 6435290. PMID 30455471. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6435290/. 
  43. ^ Bhiman, Jinal N .; Lynch, Rebecca M. (2017-03-27). “Broadly neutralizing antibodies as treatment: effects on virus and immune system”. Current HIV / AIDS Reports 14 (2): 54–62. two:10.1007 / s11904-017-0352-1. ISSN 1548-3568 . PMC 5401706. PMID 28349376. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5401706/. 

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