scholarly journals A novel competition ELISA for the rapid quantification of SARS‐CoV ‐2 neutralizing antibodies in convalescent plasma

Transfusion ◽  
2021 ◽  
Author(s):  
Elise Wouters ◽  
Caro Verbrugghe ◽  
Rosalie Devloo ◽  
Isabelle Debruyne ◽  
Dorien De Clippel ◽  
...  
Keyword(s):  
Neutralizing Antibodies ◽  
Competition Elisa ◽  
Rapid Quantification

Establishment and Clinical Validation of an In-Cell ELISA-Based Assay for the Rapid Quantification of Rabies Virus Neutralizing Antibodies

2021 ◽  
Author(s):  
Lara Schöler ◽  
Vu Thuy Khanh Le-Trilling ◽  
Ulf Dittmer ◽  
Melanie Fiedler ◽  
Mirko B. Trilling
Keyword(s):  
Rabies Virus ◽  
Neutralizing Antibodies ◽  
Clinical Validation ◽  
Cell Elisa ◽  
Rapid Quantification

Adhesion molecule expression indicates a therapeutical effect of natatizumab despite the presence of neutralizing antibodies

2009 ◽  
Vol 36 (S 02) ◽  
Author(s):  
G Pilz ◽  
P Wipfler ◽  
K Oppermann ◽  
C Sulzer ◽  
A Kunz ◽  
...  
Keyword(s):  
Adhesion Molecule ◽  
Neutralizing Antibodies ◽  
Adhesion Molecule Expression

Endothelial Cell Protein S Synthesis Is Upregulated by the Complex of IL-6 and Soluble IL-6 Receptor

1997 ◽  
Vol 77 (05) ◽  
pp. 1014-1019 ◽  
Author(s):  
W Craig Hooper ◽  
Donald J Phillips ◽  
Bruce L Evatt
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Cell Line ◽  
Neutralizing Antibodies ◽  
Hepatoma Cell ◽  
Protein S ◽  
Oncostatin M ◽  
Cell Protein ◽  
Microvascular Endothelial Cell ◽  
Hepatoma Cell Line

SummaryWe have recently demonstrated that the proinflammatory cytokine, interleukin-6 (IL-6), could upregulate the production of protein S in the human hepatoma cell line, HepG-2, but not in endothelial cells. In this study, we have demonstrated that the combination of exogenous IL-6 and soluble IL-6 receptor (sIL-6R) could significantly upregulate protein S production in both primary human umbilical vein endothelial cells (HUVEC) and in the immortalized human microvascular endothelial cell line, HMEC-1. The IL-6/sIL-6R complex was also able to rapidly induce tyrosine phosphorylation of the IL-6 transducer, gpl30. Neutralizing antibodies directed against either IL-6 or gpl30 blocked protein S upregulation by the IL-6/sIL-6R complex. It was also observed that exogenous sIL-6R could also upregulate protein S by forming a complex with IL-6 constitutively produced by the endothelial cell. Two other cytokines which also utilize the gpl30 receptor, oncostatin M (OSM) and leukemia inhibitory factor (LIF), were also able to upregulate endothelial cell protein S. This study demonstrates a mechanism that allows endothelial cells to respond to IL-6 and also illustrates the potential importance of circulating soluble receptors in the regulation of the anticoagulation pathway.

Combining capture ELISA and in vivo MxA test to detect neutralizing antibodies to interferon-beta in a large cohort of multiple sclerosis patients

2007 ◽  
Vol 34 (S 2) ◽  
Author(s):  
K Bulat ◽  
S Cepok ◽  
G von Geldern ◽  
S Hochgesand ◽  
T Menge ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Neutralizing Antibodies ◽  
Interferon Beta ◽  
Large Cohort ◽  
Capture Elisa ◽  
Multiple Sclerosis Patients

Chapter 2b: The molecular antigenic structure of the TBEV

2020 ◽  
Keyword(s):  
Conformational Changes ◽  
Neutralizing Antibodies ◽  
Lipid Membrane ◽  
Cell Entry ◽  
Antigenic Structure ◽  
E Proteins ◽  
Amino Acid Sequence Level ◽  
Endosomal Membrane ◽  
E Protein ◽  
Golgi Network

TBEV-particles are assembled in an immature, noninfectious form in the endoplasmic reticulum by the envelopment of the viral core (containing the viral RNA) by a lipid membrane associated with two viral proteins, prM and E. Immature particles are transported through the cellular exocytic pathway and conformational changes induced by acidic pH in the trans-Golgi network allow the proteolytic cleavage of prM by furin, a cellular protease, resulting in the release of mature and infectious TBE-virions. The E protein controls cell entry by mediating attachment to as yet ill-defined receptors as well as by low-pH-triggered fusion of the viral and endosomal membrane after uptake by receptor-mediated endocytosis. Because of its key functions in cell entry, the E protein is the primary target of virus neutralizing antibodies, which inhibit these functions by different mechanisms. Although all flavivirus E proteins have a similar overall structure, divergence at the amino acid sequence level is up to 60 percent (e.g. between TBE and dengue viruses), and therefore cross-neutralization as well as (some degree of) cross-protection are limited to relatively closely related flaviviruses, such as those constituting the tick-borne encephalitis serocomplex.

Broadly Neutralizing Antibodies (BNAbs): templates for HIV-1 vaccine design

2017 ◽  
Vol 2 (4) ◽  
Author(s):  
Lixin Yan ◽  
◽  
Lihong Liu ◽  
Yilin Wang ◽  
Xi Huang ◽  
...  
Keyword(s):  
Neutralizing Antibodies ◽  
Vaccine Design ◽  
Broadly Neutralizing Antibodies ◽  
Hiv 1
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