ArticleScientific reports2014
Molecular interaction between natural IgG and ficolin--mechanistic insights on adaptive-innate immune crosstalk.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed.
- Collectins and Ficolins.Advances in experimental medicine and biology · 2025Review
- The Complement System.Advances in experimental medicine and biology · 2025Review
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Current insights into the expression and functions of tumor-derived immunoglobulins.Cell death discovery · 2021Review
- Natural Antibodies: from First-Line Defense Against Pathogens to Perpetual Immune Homeostasis.Clinical reviews in allergy & immunology · 2020Review
- Natural antibodies - facts known and unknown.Central-European journal of immunology · 2018Review
- Molecular mechanisms of macrophage Toll-like receptor-Fc receptor synergy.F1000Research · 2018Review
- Article
- Human lectins and their roles in viral infections.Molecules (Basel, Switzerland) · 2015Review
- A novel IgM-H-ficolin complement pathway to attack allogenic cancer cells in vitro.Scientific reports · 2015Article
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
- The unexplored roles of human serum IgA.DNA and cell biology · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, we found that natural IgG (nIgG; a non-specific immunoglobulin of adaptive immunity) is not quiescent, but plays a crucial role in immediate immune defense by collaborating with ficolin (an innate immune protein). However, how the nIgG and ficolin interplay and what factors control the complex formation during infection is unknown. Here, we found that mild acidosis and hypocalcaemia induced by infection- inflammation condition increased the nIgG:ficolin complex formation. Hydrogen-deuterium exchange mass spectrometry delineated the binding interfaces to the CH2-CH3 region of nIgG Fc and P-subdomain of ficolin FBG domain. Infection condition exposes novel binding sites. Site-directed mutagenesis and surface plasmon resonance analyses of peptides, derived from nIgG and ficolin, defined the interacting residues between the proteins. These results provide mechanistic insights on the interaction between two molecules representing the adaptive and innate immune pathways, prompting potential development of immunomodulatory/prophylactic peptides tunable to prevailing infection conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.