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      Arming the troops: Post-translational modification of extracellular bacterial proteins

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          Abstract

          Protein secretion is almost universally employed by bacteria. Some proteins are retained on the cell surface, whereas others are released into the extracellular milieu, often playing a key role in virulence. In this review, we discuss the diverse types and potential functions of post-translational modifications (PTMs) occurring to extracellular bacterial proteins.

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          Histone methylation: a dynamic mark in health, disease and inheritance.

          Eric Greer, Yang Shi (2012)
          Organisms require an appropriate balance of stability and reversibility in gene expression programmes to maintain cell identity or to enable responses to stimuli; epigenetic regulation is integral to this dynamic control. Post-translational modification of histones by methylation is an important and widespread type of chromatin modification that is known to influence biological processes in the context of development and cellular responses. To evaluate how histone methylation contributes to stable or reversible control, we provide a broad overview of how histone methylation is regulated and leads to biological outcomes. The importance of appropriately maintaining or reprogramming histone methylation is illustrated by its links to disease and ageing and possibly to transmission of traits across generations.
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            Recognition of lipopeptide patterns by Toll-like receptor 2-Toll-like receptor 6 heterodimer.

            Jin Young Kang, Xuehua Nan, Mi Jin … (2009)
            Toll-like receptor 2 (TLR2) initiates potent immune responses by recognizing diacylated and triacylated lipopeptides. Its ligand specificity is controlled by whether it heterodimerizes with TLR1 or TLR6. We have determined the crystal structures of TLR2-TLR6-diacylated lipopeptide, TLR2-lipoteichoic acid, and TLR2-PE-DTPA complexes. PE-DTPA, 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid, is a synthetic phospholipid derivative. Two major factors contribute to the ligand specificity of TLR2-TLR1 or TLR2-TLR6 heterodimers. First, the lipid channel of TLR6 is blocked by two phenylalanines. Simultaneous mutation of these phenylalanines made TLR2-TLR6 fully responsive not only to diacylated but also to triacylated lipopeptides. Second, the hydrophobic dimerization interface of TLR2-TLR6 is increased by 80%, which compensates for the lack of amide lipid interaction between the lipopeptide and TLR2-TLR6. The structures of the TLR2-lipoteichoic acid and the TLR2-PE-DTPA complexes demonstrate that a precise interaction pattern of the head group is essential for a robust immune response by TLR2 heterodimers. Copyright 2009 Elsevier Inc. All rights reserved.
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              Bacterial Secretion Systems: An Overview.

              Erin R. Green, Joan Mecsas (2016)
              Bacterial pathogens utilize a multitude of methods to invade mammalian hosts, damage tissue sites, and thwart the immune system from responding. One essential component of these strategies for many bacterial pathogens is the secretion of proteins across phospholipid membranes. Secreted proteins can play many roles in promoting bacterial virulence, from enhancing attachment to eukaryotic cells, to scavenging resources in an environmental niche, to directly intoxicating target cells and disrupting their functions. Many pathogens use dedicated protein secretion systems to secrete virulence factors from the cytosol of the bacteria into host cells or the host environment. In general, bacterial protein secretion apparatuses can be divided into classes, based on their structures, functions, and specificity. Some systems are conserved in all classes of bacteria and secrete a broad array of substrates, while others are only found in a small number of bacterial species and/or are specific to only one or a few proteins. In this chapter, we review the canonical features of several common bacterial protein secretion systems, as well as their roles in promoting the virulence of bacterial pathogens. Additionally, we address recent findings that indicate that the innate immune system of the host can detect and respond to the presence of protein secretion systems during mammalian infection.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Sci Prog
                Journal ID (iso-abbrev): Sci Prog
                Journal ID (publisher-id): SCI
                Journal ID (hwp): spsci
                Title: Science Progress
                Publisher: SAGE Publications (Sage UK: London, England )
                ISSN (Print): 0036-8504
                ISSN (Electronic): 2047-7163
                Publication date (Electronic): 4 November 2020
                Publication date Collection: Oct-Dec 2020
                Volume: 103
                Issue: 4
                Electronic Location Identifier: 0036850420964317
                Affiliations
                [1-0036850420964317]Department of Biochemistry, University of Cambridge, Cambridge, UK
                Author notes
                [*]Martin Welch, Department of Biochemistry, University of Cambridge, Hopkins Building, Tennis Court Road, Cambridge, CB2 1QW, UK. Email: mw240@ 123456cam.ac.uk
                Author information
                https://orcid.org/0000-0003-3646-1733
                Article
                Publisher ID: 10.1177_0036850420964317
                DOI: 10.1177/0036850420964317
                PMC ID: 10450907
                PubMed ID: 33148128
                SO-VID: 63f9a13d-adcb-4f5d-b034-d822a232636c
                Copyright © © The Author(s) 2020
                License:

                This article is distributed under the terms of the Creative Commons Attribution 4.0 License ( https://creativecommons.org/licenses/by/4.0/) which permits any use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages ( https://us.sagepub.com/en-us/nam/open-access-at-sage).

                History
                Funding
                Funded by: The Evelyn Trust, ;
                Funded by: The Cystic Fibrosis Trust, ;
                Funded by: Biotechnology and Biological Sciences Research Council, FundRef https://doi.org/10.13039/501100000268;
                Award ID: Institutional DTP studentship to SF
                Funded by: British Lung Foundation, FundRef https://doi.org/10.13039/501100000351;
                Categories
                Subject: Review
                Custom metadata
                cover-date October-December 2020
                typesetter ts1

                Keywords: post-translational modification,protein secretion,bacterial pathogens,bacterial virulence factors,proteomics,methylation,acetylation,glycosylation,lipidation
                Data availability:
                Keywords: post-translational modification, protein secretion, bacterial pathogens, bacterial virulence factors, proteomics, methylation, acetylation, glycosylation, lipidation

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