Immunoglobulin-fold containing bacterial adhesins: molecular and structural perspectives in host tissue colonization and infection
ABSTRACT Immunoglobulin (Ig) domains are one of the most widespread protein domains encoded by the human genome and are present in a large array of proteins with diverse biological functions. These Ig domains possess a central structure, the immunoglobulin-fold, which is a sandwich of two β sheets,...
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| Published in: | FEMS microbiology letters Vol. 368; no. 2; pp. 1 - 14 |
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| Language: | English |
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Oxford University Press
04-02-2021
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| Abstract | ABSTRACT
Immunoglobulin (Ig) domains are one of the most widespread protein domains encoded by the human genome and are present in a large array of proteins with diverse biological functions. These Ig domains possess a central structure, the immunoglobulin-fold, which is a sandwich of two β sheets, each made up of anti-parallel β strands, surrounding a central hydrophobic core. Apart from humans, proteins containing Ig-like domains are also distributed in a vast selection of organisms including vertebrates, invertebrates, plants, viruses and bacteria where they execute a wide array of discrete cellular functions. In this review, we have described the key structural deviations of bacterial Ig-folds when compared to the classical eukaryotic Ig-fold. Further, we have comprehensively grouped all the Ig-domain containing adhesins present in both Gram-negative and Gram-positive bacteria. Additionally, we describe the role of these particular adhesins in host tissue attachment, colonization and subsequent infection by both pathogenic and non-pathogenic Escherichia coli as well as other bacterial species. The structural properties of these Ig-domain containing adhesins, along with their interactions with specific Ig-like and non Ig-like binding partners present on the host cell surface have been discussed in detail.
Structural and molecular basis of bacterial adhesins; a gripping tale of host tissue colonization and infection by pathogenic bacteria. |
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| AbstractList | Immunoglobulin (Ig) domains are one of the most widespread protein domains encoded by the human genome and are present in a large array of proteins with diverse biological functions. These Ig domains possess a central structure, the immunoglobulin-fold, which is a sandwich of two [beta] sheets, each made up of anti-parallel [beta] strands, surrounding a central hydrophobic core. Apart from humans, proteins containing Ig-like domains are also distributed in a vast selection of organisms including vertebrates, invertebrates, plants, viruses and bacteria where they execute a wide array of discrete cellular functions. In this review, we have described the key structural deviations of bacterial Ig-folds when compared to the classical eukaryotic Ig-fold. Further, we have comprehensively grouped all the Ig-domain containing adhesins present in both Gram-negative and Gram-positive bacteria. Additionally, we describe the role of these particular adhesins in host tissue attachment, colonization and subsequent infection by both pathogenic and non-pathogenic Escherichia coli as well as other bacterial species. The structural properties of these Ig-domain containing adhesins, along with their interactions with specific Ig-like and non Ig-like binding partners present on the host cell surface have been discussed in detail. ABSTRACT Immunoglobulin (Ig) domains are one of the most widespread protein domains encoded by the human genome and are present in a large array of proteins with diverse biological functions. These Ig domains possess a central structure, the immunoglobulin-fold, which is a sandwich of two β sheets, each made up of anti-parallel β strands, surrounding a central hydrophobic core. Apart from humans, proteins containing Ig-like domains are also distributed in a vast selection of organisms including vertebrates, invertebrates, plants, viruses and bacteria where they execute a wide array of discrete cellular functions. In this review, we have described the key structural deviations of bacterial Ig-folds when compared to the classical eukaryotic Ig-fold. Further, we have comprehensively grouped all the Ig-domain containing adhesins present in both Gram-negative and Gram-positive bacteria. Additionally, we describe the role of these particular adhesins in host tissue attachment, colonization and subsequent infection by both pathogenic and non-pathogenic Escherichia coli as well as other bacterial species. The structural properties of these Ig-domain containing adhesins, along with their interactions with specific Ig-like and non Ig-like binding partners present on the host cell surface have been discussed in detail. Structural and molecular basis of bacterial adhesins; a gripping tale of host tissue colonization and infection by pathogenic bacteria. Immunoglobulin (Ig) domains are one of the most widespread protein domains encoded by the human genome and are present in a large array of proteins with diverse biological functions. These Ig domains possess a central structure, the immunoglobulin-fold, which is a sandwich of two β sheets, each made up of anti-parallel β strands, surrounding a central hydrophobic core. Apart from humans, proteins containing Ig-like domains are also distributed in a vast selection of organisms including vertebrates, invertebrates, plants, viruses and bacteria where they execute a wide array of discrete cellular functions. In this review, we have described the key structural deviations of bacterial Ig-folds when compared to the classical eukaryotic Ig-fold. Further, we have comprehensively grouped all the Ig-domain containing adhesins present in both Gram-negative and Gram-positive bacteria. Additionally, we describe the role of these particular adhesins in host tissue attachment, colonization and subsequent infection by both pathogenic and non-pathogenic Escherichia coli as well as other bacterial species. The structural properties of these Ig-domain containing adhesins, along with their interactions with specific Ig-like and non Ig-like binding partners present on the host cell surface have been discussed in detail. Immunoglobulin (Ig) domains are one of the most widespread protein domains encoded by the human genome and are present in a large array of proteins with diverse biological functions. These Ig domains possess a central structure, the immunoglobulin-fold, which is a sandwich of two [beta] sheets, each made up of anti-parallel [beta] strands, surrounding a central hydrophobic core. Apart from humans, proteins containing Ig-like domains are also distributed in a vast selection of organisms including vertebrates, invertebrates, plants, viruses and bacteria where they execute a wide array of discrete cellular functions. In this review, we have described the key structural deviations of bacterial Ig-folds when compared to the classical eukaryotic Ig-fold. Further, we have comprehensively grouped all the Ig-domain containing adhesins present in both Gram-negative and Gram-positive bacteria. Additionally, we describe the role of these particular adhesins in host tissue attachment, colonization and subsequent infection by both pathogenic and non-pathogenic Escherichia coli as well as other bacterial species. The structural properties of these Ig-domain containing adhesins, along with their interactions with specific Ig-like and non Ig-like binding partners present on the host cell surface have been discussed in detail. Keywords: immunoglobulin domain; Ig-fold; host entry receptors; fmbrial proteins; pilin domain; internalin |
| Audience | Academic |
| Author | Samanta, Dibyendu Duraivelan, Kheerthana Chatterjee, Shruti Nair, Asha V Basak, Aditya J |
| Author_xml | – sequence: 1 givenname: Shruti surname: Chatterjee fullname: Chatterjee, Shruti – sequence: 2 givenname: Aditya J surname: Basak fullname: Basak, Aditya J – sequence: 3 givenname: Asha V orcidid: 0000-0002-2037-1138 surname: Nair fullname: Nair, Asha V – sequence: 4 givenname: Kheerthana surname: Duraivelan fullname: Duraivelan, Kheerthana – sequence: 5 givenname: Dibyendu orcidid: 0000-0002-5733-6694 surname: Samanta fullname: Samanta, Dibyendu email: dibyendu.samanta@iitkgp.ac.in |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33355339$$D View this record in MEDLINE/PubMed |
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| Copyright | The Author(s) 2020. Published by Oxford University Press on behalf of FEMS. 2020 The Author(s) 2020. Published by Oxford University Press on behalf of FEMS. COPYRIGHT 2021 Oxford University Press |
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| Keywords | immunoglobulin domain pilin domain internalin Ig-fold fimbrial proteins host entry receptors |
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| Publisher | Oxford University Press |
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Immunoglobulin (Ig) domains are one of the most widespread protein domains encoded by the human genome and are present in a large array of proteins... Immunoglobulin (Ig) domains are one of the most widespread protein domains encoded by the human genome and are present in a large array of proteins with... |
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| SubjectTerms | Adhesins Analysis Arrays Bacteria Bacterial proteins Cell surface Cellular structure Colonization E coli Genomes Genomics Gram-negative bacteria Gram-positive bacteria Hydrophobicity Identification and classification Immunoglobulins Invertebrates Microbiology Properties Proteins Structure Vertebrates |
| Title | Immunoglobulin-fold containing bacterial adhesins: molecular and structural perspectives in host tissue colonization and infection |
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