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SARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin—Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases

The immune response to SARS-CoV-2 infection requires antibody recognition of the spike protein. In a study designed to examine the molecular features of anti-spike and anti-nucleocapsid antibodies, patient plasma proteins binding to pre-fusion stabilised complete spike and nucleocapsid proteins were...

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Autores principales: Iles, Jason, Zmuidinaite, Raminta, Sadee, Christoph, Gardiner, Anna, Lacey, Jonathan, Harding, Stephen, Ule, Jernej, Roblett, Debra, Heeney, Jonathan, Baxendale, Helen, Iles, Ray K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9030890/
https://www.ncbi.nlm.nih.gov/pubmed/35456942
http://dx.doi.org/10.3390/ijms23084126
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author Iles, Jason
Zmuidinaite, Raminta
Sadee, Christoph
Gardiner, Anna
Lacey, Jonathan
Harding, Stephen
Ule, Jernej
Roblett, Debra
Heeney, Jonathan
Baxendale, Helen
Iles, Ray K.
author_facet Iles, Jason
Zmuidinaite, Raminta
Sadee, Christoph
Gardiner, Anna
Lacey, Jonathan
Harding, Stephen
Ule, Jernej
Roblett, Debra
Heeney, Jonathan
Baxendale, Helen
Iles, Ray K.
author_sort Iles, Jason
collection PubMed
description The immune response to SARS-CoV-2 infection requires antibody recognition of the spike protein. In a study designed to examine the molecular features of anti-spike and anti-nucleocapsid antibodies, patient plasma proteins binding to pre-fusion stabilised complete spike and nucleocapsid proteins were isolated and analysed by matrix-assisted laser desorption ionisation–time of flight (MALDI-ToF) mass spectrometry. Amongst the immunoglobulins, a high affinity for human serum albumin was evident in the anti-spike preparations. Careful mass comparison revealed the preferential capture of advanced glycation end product (AGE) forms of glycated human serum albumin by the pre-fusion spike protein. The ability of bacteria and viruses to surround themselves with serum proteins is a recognised immune evasion and pathogenic process. The preference of SARS-CoV-2 for AGE forms of glycated serum albumin may in part explain the severity and pathology of acute respiratory distress and the bias towards the elderly and those with (pre)diabetic and atherosclerotic/metabolic disease.
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spelling pubmed-90308902022-04-23 SARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin—Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases Iles, Jason Zmuidinaite, Raminta Sadee, Christoph Gardiner, Anna Lacey, Jonathan Harding, Stephen Ule, Jernej Roblett, Debra Heeney, Jonathan Baxendale, Helen Iles, Ray K. Int J Mol Sci Article The immune response to SARS-CoV-2 infection requires antibody recognition of the spike protein. In a study designed to examine the molecular features of anti-spike and anti-nucleocapsid antibodies, patient plasma proteins binding to pre-fusion stabilised complete spike and nucleocapsid proteins were isolated and analysed by matrix-assisted laser desorption ionisation–time of flight (MALDI-ToF) mass spectrometry. Amongst the immunoglobulins, a high affinity for human serum albumin was evident in the anti-spike preparations. Careful mass comparison revealed the preferential capture of advanced glycation end product (AGE) forms of glycated human serum albumin by the pre-fusion spike protein. The ability of bacteria and viruses to surround themselves with serum proteins is a recognised immune evasion and pathogenic process. The preference of SARS-CoV-2 for AGE forms of glycated serum albumin may in part explain the severity and pathology of acute respiratory distress and the bias towards the elderly and those with (pre)diabetic and atherosclerotic/metabolic disease. MDPI 2022-04-08 /pmc/articles/PMC9030890/ /pubmed/35456942 http://dx.doi.org/10.3390/ijms23084126 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Iles, Jason
Zmuidinaite, Raminta
Sadee, Christoph
Gardiner, Anna
Lacey, Jonathan
Harding, Stephen
Ule, Jernej
Roblett, Debra
Heeney, Jonathan
Baxendale, Helen
Iles, Ray K.
SARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin—Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases
title SARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin—Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases
title_full SARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin—Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases
title_fullStr SARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin—Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases
title_full_unstemmed SARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin—Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases
title_short SARS-CoV-2 Spike Protein Binding of Glycated Serum Albumin—Its Potential Role in the Pathogenesis of the COVID-19 Clinical Syndromes and Bias towards Individuals with Pre-Diabetes/Type 2 Diabetes and Metabolic Diseases
title_sort sars-cov-2 spike protein binding of glycated serum albumin—its potential role in the pathogenesis of the covid-19 clinical syndromes and bias towards individuals with pre-diabetes/type 2 diabetes and metabolic diseases
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9030890/
https://www.ncbi.nlm.nih.gov/pubmed/35456942
http://dx.doi.org/10.3390/ijms23084126
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