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10.1080/19420862.2021.1905978

http://scihub22266oqcxt.onion/10.1080/19420862.2021.1905978
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33843452!8043170!33843452
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suck abstract from ncbi


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pmid33843452      MAbs 2021 ; 13 (1): 1905978
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  • Rigid monoclonal antibodies improve detection of SARS-CoV-2 nucleocapsid protein #MMPMID33843452
  • Hodge CD; Rosenberg DJ; Grob P; Wilamowski M; Joachimiak A; Hura GL; Hammel M
  • MAbs 2021[Jan]; 13 (1): 1905978 PMID33843452show ga
  • Monoclonal antibodies (mAbs) are the basis of treatments and diagnostics for pathogens and other biological phenomena. We conducted a structural characterization of mAbs against the N-terminal domain of nucleocapsid protein (NP(NTD)) from SARS-CoV-2 using small-angle X-ray scattering and transmission electron microscopy. Our solution-based results distinguished the mAbs' flexibility and how this flexibility affects the assembly of multiple mAbs on an antigen. By pairing two mAbs that bind different epitopes on the NP(NTD), we show that flexible mAbs form a closed sandwich-like complex. With rigid mAbs, a juxtaposition of the antigen-binding fragments is prevented, enforcing a linear arrangement of the mAb pair, which facilitates further mAb polymerization. In a modified sandwich enzyme-linked immunosorbent assay, we show that rigid mAb-pairings with linear polymerization led to increased NP(NTD) detection sensitivity. These enhancements can expedite the development of more sensitive and selective antigen-detecting point-of-care lateral flow devices, which are critical for early diagnosis and epidemiological studies of SARS-CoV-2 and other pathogens.
  • |Animals[MESH]
  • |Antibodies, Monoclonal/*immunology[MESH]
  • |Antibodies, Viral/*immunology[MESH]
  • |COVID-19/*immunology[MESH]
  • |Epitopes/*immunology[MESH]
  • |Humans[MESH]
  • |Nucleocapsid Proteins/*immunology[MESH]


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