scholarly journals Human Secretory IgM Antibodies Activate Human Complement and Offer Protection at Mucosal Surface

2017 ◽  
Vol 85 (1) ◽  
pp. 43-50 ◽  
Author(s):  
T. E. Michaelsen ◽  
S. Emilsen ◽  
R. H. Sandin ◽  
B. K. Granerud ◽  
D. Bratlie ◽  
...  
Keyword(s):  
Mucosal Surface ◽  
Human Complement ◽  
Igm Antibodies ◽  
Secretory Igm

scholarly journals Immunoglobulin-like Domain of HsFcμR as a Capture Molecule for Detection of Crimean-Congo Hemorrhagic Fever Virus- and Zika Virus-Specific IgM Antibodies

2019 ◽  
Vol 65 (3) ◽  
pp. 451-461 ◽  
Author(s):  
Anne Rackow ◽  
Christa Ehmen ◽  
Ronald von Possel ◽  
Raquel Medialdea-Carrera ◽  
David Brown ◽  
...  
Keyword(s):  
Zika Virus ◽  
Specific Binding ◽  
Hemorrhagic Fever ◽  
Fever Virus ◽  
Size Exclusion ◽  
Animal Origin ◽  
Serum Samples ◽  
Crimean Congo Hemorrhagic Fever ◽  
Hemorrhagic Fever Virus ◽  
Igm Antibodies

Abstract BACKGROUND The cellular surface molecule HsTOSO/FAIM3/HsFcμR has been identified as an IgM-specific Fc receptor expressed on lymphocytes. Here, we show that its extracellular immunoglobulin-like domain (HsFcμR-Igl) specifically binds to IgM/antigen immune complexes (ICs) and exploit this property for the development of novel detection systems for IgM antibodies directed against Crimean-Congo hemorrhagic fever virus (CCHFV) and Zika virus (ZIKV). METHODS His-tagged HsFcμR-Igl was expressed in Escherichia coli and purified by affinity chromatography, oxidative refolding, and size-exclusion chromatography. Specific binding of HsFcμR-Igl to IgM/antigen ICs was confirmed, and 2 prototypic ELISAs for the detection of anti-CCHFV and anti-ZIKV IgM antibodies were developed. Thereby, patient sera and virus-specific recombinant antigens directly labeled with horseradish peroxidase (HRP) were coincubated on HsFcμR-Igl-coated ELISA plates. Bound ICs were quantified by measuring turnover of a chromogenic HRP substrate. RESULTS Assay validation was performed using paired serum samples from 15 Kosovar patients with a PCR-confirmed CCHFV infection and 28 Brazilian patients with a PCR-confirmed ZIKV infection, along with a panel of a priori CCHFV/ZIKV-IgM-negative serum samples. Both ELISAs were highly reproducible. Sensitivity and specificity were comparable with or even exceeded in-house gold standard testing and commercial kits. Furthermore, latex beads coated with HsFcμR-Igl aggregated upon coincubation with an IgM-positive serum and HRP-labeled antigen but not with either component alone, revealing a potential for use of HsFcμR-Igl as a capture molecule in aggregation-based rapid tests. CONCLUSIONS Recombinant HsFcμR-Igl is a versatile capture molecule for IgM/antigen ICs of human and animal origin and can be applied for the development of both plate- and bead-based serological tests.

scholarly journals The Crystal Structure of C2a, the Catalytic Fragment of Classical Pathway C3 and C5 Convertase of Human Complement

2007 ◽  
Vol 367 (1) ◽  
pp. 224-233 ◽  
Author(s):  
Vengadesan Krishnan ◽  
Yuanyuan Xu ◽  
Kevin Macon ◽  
John E. Volanakis ◽  
Sthanam V.L. Narayana
Keyword(s):  
Crystal Structure ◽  
Classical Pathway ◽  
Human Complement ◽  
Catalytic Fragment

Chemical Analysis of the C'l Fraction of Human Complement.

1946 ◽  
Vol 63 (2) ◽  
pp. 221-223 ◽  
Author(s):  
E. E. Ecker ◽  
B. Lustig ◽  
A. A. Kondritzer ◽  
S. Seifter
Keyword(s):  
Chemical Analysis ◽  
Human Complement
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