Grasping the nettle: A bacterial invasin that targets immunoglobulin variable domains

Barlow, Paul N.

doi:10.1074/jbc.h118.002949

Cited by 3 publications

(1 citation statement)

References 6 publications

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“…This domain is part of adhesion molecules of the intimin/invasin family. Furthermore, it has been shown that Big-domain-containing protein InvD from Yersinia pseudotuberculosis acts by binding the Fab region of IgG or IgA and might therefore avoid the clearance from the intestine by secretory IgA, making these proteins interesting targets to study bacteria-host interactions [ 82 ]. Although the SIHUMIx species are not enteropathogenic, these three novel sProteins are interesting candidates for the study of host microbiome interactions.…”

Section: Discussionmentioning

confidence: 99%

Discovery of novel community-relevant small proteins in a simplified human intestinal microbiome

et al. 2021

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Background The intestinal microbiota plays a crucial role in protecting the host from pathogenic microbes, modulating immunity and regulating metabolic processes. We studied the simplified human intestinal microbiota (SIHUMIx) consisting of eight bacterial species with a particular focus on the discovery of novel small proteins with less than 100 amino acids (= sProteins), some of which may contribute to shape the simplified human intestinal microbiota. Although sProteins carry out a wide range of important functions, they are still often missed in genome annotations, and little is known about their structure and function in individual microbes and especially in microbial communities. Results We created a multi-species integrated proteogenomics search database (iPtgxDB) to enable a comprehensive identification of novel sProteins. Six of the eight SIHUMIx species, for which no complete genomes were available, were sequenced and de novo assembled. Several proteomics approaches including two earlier optimized sProtein enrichment strategies were applied to specifically increase the chances for novel sProtein discovery. The search of tandem mass spectrometry (MS/MS) data against the multi-species iPtgxDB enabled the identification of 31 novel sProteins, of which the expression of 30 was supported by metatranscriptomics data. Using synthetic peptides, we were able to validate the expression of 25 novel sProteins. The comparison of sProtein expression in each single strain versus a multi-species community cultivation showed that six of these sProteins were only identified in the SIHUMIx community indicating a potentially important role of sProteins in the organization of microbial communities. Two of these novel sProteins have a potential antimicrobial function. Metabolic modelling revealed that a third sProtein is located in a genomic region encoding several enzymes relevant for the community metabolism within SIHUMIx. Conclusions We outline an integrated experimental and bioinformatics workflow for the discovery of novel sProteins in a simplified intestinal model system that can be generically applied to other microbial communities. The further analysis of novel sProteins uniquely expressed in the SIHUMIx multi-species community is expected to enable new insights into the role of sProteins on the functionality of bacterial communities such as those of the human intestinal tract.

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Section: Discussionmentioning

confidence: 99%

Discovery of novel community-relevant small proteins in a simplified human intestinal microbiome

et al. 2021

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Biological chemistry without borders

Guengerich¹

2018

Journal of Biological Chemistry

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Immunoglobulin-fold containing bacterial adhesins: molecular and structural perspectives in host tissue colonization and infection

Chatterjee

Basak

Nair

et al. 2020

FEMS Microbiology Letters

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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 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.

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Grasping the nettle: A bacterial invasin that targets immunoglobulin variable domains

Cited by 3 publications

References 6 publications

Discovery of novel community-relevant small proteins in a simplified human intestinal microbiome

Discovery of novel community-relevant small proteins in a simplified human intestinal microbiome

Biological chemistry without borders

Immunoglobulin-fold containing bacterial adhesins: molecular and structural perspectives in host tissue colonization and infection

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