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Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential
C1q domain-containing proteins (C1qDC proteins) unexpectedly turned out to be widespread molecules among a variety of invertebrates, despite their lack of an integral complement system. Despite the wide distribution in the genomes of various invertebrates, data on the structure and properties of the...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10672478/ https://www.ncbi.nlm.nih.gov/pubmed/37999394 http://dx.doi.org/10.3390/md21110570 |
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author | Grinchenko, Andrei Buriak, Ivan Kumeiko, Vadim |
author_facet | Grinchenko, Andrei Buriak, Ivan Kumeiko, Vadim |
author_sort | Grinchenko, Andrei |
collection | PubMed |
description | C1q domain-containing proteins (C1qDC proteins) unexpectedly turned out to be widespread molecules among a variety of invertebrates, despite their lack of an integral complement system. Despite the wide distribution in the genomes of various invertebrates, data on the structure and properties of the isolated and characterized C1qDC proteins, which belong to the C1q/TNF superfamily, are sporadic, although they hold great practical potential for the creation of new biotechnologies. This review not only summarizes the current data on the properties of already-isolated or bioengineered C1qDC proteins but also projects further strategies for their study and biomedical application. It has been shown that further broad study of the carbohydrate specificity of the proteins can provide great opportunities, since for many of them only interactions with pathogen-associated molecular patterns (PAMPs) was evaluated and their antimicrobial, antiviral, and fungicidal activities were studied. However, data on the properties of C1qDC proteins, which researchers originally discovered as lectins and therefore studied their fine carbohydrate specificity and antitumor activity, intriguingly show the great potential of this family of proteins for the creation of targeted drug delivery systems, vaccines, and clinical assays for the differential diagnosis of cancer. The ability of invertebrate C1qDC proteins to recognize patterns of aberrant glycosylation of human cell surfaces and interact with mammalian immunoglobulins indicates the great biomedical potential of these molecules. |
format | Online Article Text |
id | pubmed-10672478 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106724782023-10-30 Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential Grinchenko, Andrei Buriak, Ivan Kumeiko, Vadim Mar Drugs Review C1q domain-containing proteins (C1qDC proteins) unexpectedly turned out to be widespread molecules among a variety of invertebrates, despite their lack of an integral complement system. Despite the wide distribution in the genomes of various invertebrates, data on the structure and properties of the isolated and characterized C1qDC proteins, which belong to the C1q/TNF superfamily, are sporadic, although they hold great practical potential for the creation of new biotechnologies. This review not only summarizes the current data on the properties of already-isolated or bioengineered C1qDC proteins but also projects further strategies for their study and biomedical application. It has been shown that further broad study of the carbohydrate specificity of the proteins can provide great opportunities, since for many of them only interactions with pathogen-associated molecular patterns (PAMPs) was evaluated and their antimicrobial, antiviral, and fungicidal activities were studied. However, data on the properties of C1qDC proteins, which researchers originally discovered as lectins and therefore studied their fine carbohydrate specificity and antitumor activity, intriguingly show the great potential of this family of proteins for the creation of targeted drug delivery systems, vaccines, and clinical assays for the differential diagnosis of cancer. The ability of invertebrate C1qDC proteins to recognize patterns of aberrant glycosylation of human cell surfaces and interact with mammalian immunoglobulins indicates the great biomedical potential of these molecules. MDPI 2023-10-30 /pmc/articles/PMC10672478/ /pubmed/37999394 http://dx.doi.org/10.3390/md21110570 Text en © 2023 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 | Review Grinchenko, Andrei Buriak, Ivan Kumeiko, Vadim Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential |
title | Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential |
title_full | Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential |
title_fullStr | Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential |
title_full_unstemmed | Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential |
title_short | Invertebrate C1q Domain-Containing Proteins: Molecular Structure, Functional Properties and Biomedical Potential |
title_sort | invertebrate c1q domain-containing proteins: molecular structure, functional properties and biomedical potential |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10672478/ https://www.ncbi.nlm.nih.gov/pubmed/37999394 http://dx.doi.org/10.3390/md21110570 |
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