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Some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients
The antibodies of schizophrenic patients that hydrolyze myelin basic protein (MBP) have been actively studied recently, but the mechanism of the catalytic properties of immunoglobulin molecules remains unknown. Determination of specific immunoglobulin sequences associated with the high activity of M...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
PeerJ Inc.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10329820/ https://www.ncbi.nlm.nih.gov/pubmed/37431466 http://dx.doi.org/10.7717/peerj.15584 |
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author | Zavialova, Maria Kamaeva, Daria Kazieva, Laura Skvortsov, Vladlen S. Smirnova, Liudmila |
author_facet | Zavialova, Maria Kamaeva, Daria Kazieva, Laura Skvortsov, Vladlen S. Smirnova, Liudmila |
author_sort | Zavialova, Maria |
collection | PubMed |
description | The antibodies of schizophrenic patients that hydrolyze myelin basic protein (MBP) have been actively studied recently, but the mechanism of the catalytic properties of immunoglobulin molecules remains unknown. Determination of specific immunoglobulin sequences associated with the high activity of MBP proteolysis will help to understand the mechanisms of abzyme catalysis. In the course of comparative mass spectrometric analysis of IgG peptides from the blood serum of patients with acute schizophrenia and healthy people, 12 sequences were identified, which were found only in antibodies that hydrolyze MBP. These sequences belong to IgG heavy chains and κ- and λ-type light chains, with eight of them belonging to variable domains. The content of peptides from the variable regions of the light chains does not correlate with the proteolytic activity of IgG to MBP in patients with schizophrenia, whereas for two sequences from the variable regions of the heavy chains (FQ(+0.98)GWVTMTR and *LYLQMN(+0.98)SLR), an increase in activity with increasing their concentration. The results suggest that these sequences may be involved in one way or another in MBP hydrolysis. |
format | Online Article Text |
id | pubmed-10329820 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | PeerJ Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-103298202023-07-10 Some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients Zavialova, Maria Kamaeva, Daria Kazieva, Laura Skvortsov, Vladlen S. Smirnova, Liudmila PeerJ Biochemistry The antibodies of schizophrenic patients that hydrolyze myelin basic protein (MBP) have been actively studied recently, but the mechanism of the catalytic properties of immunoglobulin molecules remains unknown. Determination of specific immunoglobulin sequences associated with the high activity of MBP proteolysis will help to understand the mechanisms of abzyme catalysis. In the course of comparative mass spectrometric analysis of IgG peptides from the blood serum of patients with acute schizophrenia and healthy people, 12 sequences were identified, which were found only in antibodies that hydrolyze MBP. These sequences belong to IgG heavy chains and κ- and λ-type light chains, with eight of them belonging to variable domains. The content of peptides from the variable regions of the light chains does not correlate with the proteolytic activity of IgG to MBP in patients with schizophrenia, whereas for two sequences from the variable regions of the heavy chains (FQ(+0.98)GWVTMTR and *LYLQMN(+0.98)SLR), an increase in activity with increasing their concentration. The results suggest that these sequences may be involved in one way or another in MBP hydrolysis. PeerJ Inc. 2023-07-06 /pmc/articles/PMC10329820/ /pubmed/37431466 http://dx.doi.org/10.7717/peerj.15584 Text en ©2023 Zavialova et al. https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited. |
spellingShingle | Biochemistry Zavialova, Maria Kamaeva, Daria Kazieva, Laura Skvortsov, Vladlen S. Smirnova, Liudmila Some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients |
title | Some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients |
title_full | Some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients |
title_fullStr | Some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients |
title_full_unstemmed | Some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients |
title_short | Some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients |
title_sort | some structural features of the peptide profile of myelin basic protein-hydrolyzing antibodies in schizophrenic patients |
topic | Biochemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10329820/ https://www.ncbi.nlm.nih.gov/pubmed/37431466 http://dx.doi.org/10.7717/peerj.15584 |
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