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  1. Article ; Online: Lipoarabinomannan mediates localized cell wall integrity during division in mycobacteria.

    Sparks, Ian L / Kado, Takehiro / Prithviraj, Malavika / Nijjer, Japinder / Yan, Jing / Morita, Yasu S

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 2191

    Abstract: The growth and division of mycobacteria, which include clinically relevant pathogens, deviate from that of canonical bacterial models. Despite their Gram-positive ancestry, mycobacteria synthesize and elongate a diderm envelope asymmetrically from the ... ...

    Abstract The growth and division of mycobacteria, which include clinically relevant pathogens, deviate from that of canonical bacterial models. Despite their Gram-positive ancestry, mycobacteria synthesize and elongate a diderm envelope asymmetrically from the poles, with the old pole elongating more robustly than the new pole. The phosphatidylinositol-anchored lipoglycans lipomannan (LM) and lipoarabinomannan (LAM) are cell envelope components critical for host-pathogen interactions, but their physiological functions in mycobacteria remained elusive. In this work, using biosynthetic mutants of these lipoglycans, we examine their roles in maintaining cell envelope integrity in Mycobacterium smegmatis and Mycobacterium tuberculosis. We find that mutants defective in producing mature LAM fail to maintain rod cell shape specifically at the new pole and para-septal regions whereas a mutant that produces a larger LAM becomes multi-septated. Therefore, LAM plays critical and distinct roles at subcellular locations associated with division in mycobacteria, including maintenance of local cell wall integrity and septal placement.
    MeSH term(s) Lipopolysaccharides ; Mycobacterium smegmatis/genetics ; Cell Wall ; Mycobacterium tuberculosis/genetics
    Chemical Substances lipoarabinomannan ; Lipopolysaccharides
    Language English
    Publishing date 2024-03-11
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-46565-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Lipoarabinomannan regulates septation in

    Sparks, Ian L / Nijjer, Japinder / Yan, Jing / Morita, Yasu S

    bioRxiv : the preprint server for biology

    2023  

    Abstract: The growth and division of mycobacteria, which include several clinically relevant pathogens, deviate significantly from that of canonical bacterial models. Despite their Gram-positive ancestry, mycobacteria synthesize and elongate a diderm envelope ... ...

    Abstract The growth and division of mycobacteria, which include several clinically relevant pathogens, deviate significantly from that of canonical bacterial models. Despite their Gram-positive ancestry, mycobacteria synthesize and elongate a diderm envelope asymmetrically from the poles, with the old pole elongating more robustly than the new pole. In addition to being structurally distinct, the molecular components of the mycobacterial envelope are also evolutionarily unique, including the phosphatidylinositol-anchored lipoglycans lipomannan (LM) and lipoarabinomannan (LAM). LM and LAM modulate host immunity during infection, but their role outside of intracellular survival remains poorly understood, despite their widespread conservation among non-pathogenic and opportunistically pathogenic mycobacteria. Previously,
    Language English
    Publishing date 2023-03-26
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.03.26.534150
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mycobacterium smegmatis: The Vanguard of Mycobacterial Research.

    Sparks, Ian L / Derbyshire, Keith M / Jacobs, William R / Morita, Yasu S

    Journal of bacteriology

    2023  Volume 205, Issue 1, Page(s) e0033722

    Abstract: The genus Mycobacterium contains several slow-growing human pathogens, including Mycobacterium tuberculosis, Mycobacterium leprae, and Mycobacterium avium. Mycobacterium smegmatis is a nonpathogenic and fast growing species within this genus. In 1990, a ... ...

    Abstract The genus Mycobacterium contains several slow-growing human pathogens, including Mycobacterium tuberculosis, Mycobacterium leprae, and Mycobacterium avium. Mycobacterium smegmatis is a nonpathogenic and fast growing species within this genus. In 1990, a mutant of M. smegmatis, designated mc
    MeSH term(s) Humans ; Mycobacterium smegmatis/genetics ; Escherichia coli/genetics ; Mycobacterium tuberculosis/genetics ; Tuberculosis ; Isoniazid
    Chemical Substances Isoniazid (V83O1VOZ8L)
    Language English
    Publishing date 2023-01-04
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/jb.00337-22
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  4. Article ; Online: Detergent-induced quantitatively limited formation of diacyl phosphatidylinositol dimannoside in Mycobacterium smegmatis.

    Kitzmiller, Claire E / Cheng, Tan-Yun / Prandi, Jacques / Sparks, Ian L / Moody, D Branch / Morita, Yasu S

    Journal of lipid research

    2024  , Page(s) 100533

    Abstract: Mycobacterial plasma membrane, together with the peptidoglycan-arabinogalactan cell wall and waxy outer membrane, creates a robust permeability barrier against xenobiotics. The fact that several anti-tuberculosis drugs target plasma membrane-embedded ... ...

    Abstract Mycobacterial plasma membrane, together with the peptidoglycan-arabinogalactan cell wall and waxy outer membrane, creates a robust permeability barrier against xenobiotics. The fact that several anti-tuberculosis drugs target plasma membrane-embedded enzymes underscores the importance of the plasma membrane in bacterial physiology and pathogenesis. Nevertheless, its accurate phospholipid composition remains undefined, with conflicting reports on the abundance of phosphatidylinositol mannosides (PIMs), physiologically important glycolipids evolutionarily conserved among mycobacteria and related bacteria. Some studies indicate cardiolipin, phosphatidylethanolamine, and phosphatidylinositol as dominant structural phospholipids. Conversely, some suggest PIMs dominate the plasma membrane. A striking example of the latter is the use of reverse micelle extraction, showing diacyl phosphatidylinositol dimannoside (Ac
    Language English
    Publishing date 2024-03-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80154-9
    ISSN 1539-7262 ; 0022-2275
    ISSN (online) 1539-7262
    ISSN 0022-2275
    DOI 10.1016/j.jlr.2024.100533
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Cell Walls and Membranes of Actinobacteria.

    Rahlwes, Kathryn C / Sparks, Ian L / Morita, Yasu S

    Sub-cellular biochemistry

    2019  Volume 92, Page(s) 417–469

    Abstract: Actinobacteria is a group of diverse bacteria. Most species in this class of bacteria are filamentous aerobes found in soil, including the genus Streptomyces perhaps best known for their fascinating capabilities of producing antibiotics. These bacteria ... ...

    Abstract Actinobacteria is a group of diverse bacteria. Most species in this class of bacteria are filamentous aerobes found in soil, including the genus Streptomyces perhaps best known for their fascinating capabilities of producing antibiotics. These bacteria typically have a Gram-positive cell envelope, comprised of a plasma membrane and a thick peptidoglycan layer. However, there is a notable exception of the Corynebacteriales order, which has evolved a unique type of outer membrane likely as a consequence of convergent evolution. In this chapter, we will focus on the unique cell envelope of this order. This cell envelope features the peptidoglycan layer that is covalently modified by an additional layer of arabinogalactan . Furthermore, the arabinogalactan layer provides the platform for the covalent attachment of mycolic acids , some of the longest natural fatty acids that can contain ~100 carbon atoms per molecule. Mycolic acids are thought to be the main component of the outer membrane, which is composed of many additional lipids including trehalose dimycolate, also known as the cord factor. Importantly, a subset of bacteria in the Corynebacteriales order are pathogens of human and domestic animals, including Mycobacterium tuberculosis. The surface coat of these pathogens are the first point of contact with the host immune system, and we now know a number of host receptors specific to molecular patterns exposed on the pathogen's surface, highlighting the importance of understanding how the cell envelope of Actinobacteria is structured and constructed. This chapter describes the main structural and biosynthetic features of major components found in the actinobacterial cell envelopes and highlights the key differences between them.
    MeSH term(s) Actinobacteria/cytology ; Animals ; Cell Membrane/chemistry ; Cell Membrane/metabolism ; Cell Wall/chemistry ; Cell Wall/metabolism ; Humans ; Mycobacterium tuberculosis/pathogenicity ; Mycolic Acids/metabolism ; Peptidoglycan/metabolism
    Chemical Substances Mycolic Acids ; Peptidoglycan
    Language English
    Publishing date 2019-06-18
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 0306-0225 ; 0096-8757
    ISSN 0306-0225 ; 0096-8757
    DOI 10.1007/978-3-030-18768-2_13
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: A cell wall synthase accelerates plasma membrane partitioning in mycobacteria.

    Kado, Takehiro / Akbary, Zarina / Motooka, Daisuke / Sparks, Ian L / Melzer, Emily S / Nakamura, Shota / Rojas, Enrique R / Morita, Yasu S / Siegrist, M Sloan

    eLife

    2023  Volume 12

    Abstract: Lateral partitioning of proteins and lipids shapes membrane function. In model membranes, partitioning can be influenced both by bilayer-intrinsic factors like molecular composition and by bilayer-extrinsic factors such as interactions with other ... ...

    Abstract Lateral partitioning of proteins and lipids shapes membrane function. In model membranes, partitioning can be influenced both by bilayer-intrinsic factors like molecular composition and by bilayer-extrinsic factors such as interactions with other membranes and solid supports. While cellular membranes can departition in response to bilayer-intrinsic or -extrinsic disruptions, the mechanisms by which they partition de novo are largely unknown. The plasma membrane of
    MeSH term(s) Cell Membrane ; Benzyl Alcohol ; Cell Wall ; Mycobacterium smegmatis
    Chemical Substances Benzyl Alcohol (LKG8494WBH)
    Language English
    Publishing date 2023-09-04
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.81924
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  7. Article ; Online: Fluorescence Imaging-Based Discovery of Membrane Domain-Associated Proteins in

    Rokicki, Corelle A Z / Brenner, James R / Dills, Alexander H / Judd, Julius J / Kester, Jemila C / Puffal, Julia / Sparks, Ian L / Prithviraj, Malavika / Anderson, Brittany R / Wade, Joseph T / Gray, Todd A / Derbyshire, Keith M / Fortune, Sarah M / Morita, Yasu S

    Journal of bacteriology

    2021  Volume 203, Issue 22, Page(s) e0041921

    Abstract: Mycobacteria spatially organize their plasma membrane, and many enzymes involved in envelope biosynthesis associate with a membrane compartment termed the intracellular membrane domain (IMD). The IMD is concentrated in the polar regions of growing cells ... ...

    Abstract Mycobacteria spatially organize their plasma membrane, and many enzymes involved in envelope biosynthesis associate with a membrane compartment termed the intracellular membrane domain (IMD). The IMD is concentrated in the polar regions of growing cells and becomes less polarized under nongrowing conditions. Because mycobacteria elongate from the poles, the observed polar localization of the IMD during growth likely supports the localized biosynthesis of envelope components. While we have identified more than 300 IMD-associated proteins by proteomic analyses, only a few of these have been verified by independent experimental methods. Furthermore, some IMD-associated proteins may have escaped proteomic identification and remain to be identified. Here, we visually screened an arrayed library of 523 Mycobacterium smegmatis strains, each producing a Dendra2-FLAG-tagged recombinant protein. We identified 29 fusion proteins that showed polar fluorescence patterns characteristic of IMD proteins. Twenty of these had previously been suggested to localize to the IMD based on proteomic data. Of the nine remaining IMD candidate proteins, three were confirmed by biochemical methods to be associated with the IMD. Taken together, this new colocalization strategy is effective in verifying the IMD association of proteins found by proteomic analyses while facilitating the discovery of additional IMD-associated proteins.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cell Membrane ; Gene Expression Regulation, Bacterial/physiology ; Mycobacterium smegmatis/genetics ; Mycobacterium smegmatis/metabolism ; Optical Imaging/methods ; Protein Domains
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 2021-09-13
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.00419-21
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  8. Article ; Online: Small Molecule Chelators Reveal That Iron Starvation Inhibits Late Stages of Bacterial Cytokinesis.

    Santos, Thiago M A / Lammers, Matthew G / Zhou, Maoquan / Sparks, Ian L / Rajendran, Madhusudan / Fang, Dong / De Jesus, Crystal L Y / Carneiro, Gabriel F R / Cui, Qiang / Weibel, Douglas B

    ACS chemical biology

    2017  Volume 13, Issue 1, Page(s) 235–246

    Abstract: Bacterial cell division requires identification of the division site, assembly of the division machinery, and constriction of the cell envelope. These processes are regulated in response to several cellular and environmental signals. Here, we use small ... ...

    Abstract Bacterial cell division requires identification of the division site, assembly of the division machinery, and constriction of the cell envelope. These processes are regulated in response to several cellular and environmental signals. Here, we use small molecule iron chelators to characterize the surprising connections between bacterial iron homeostasis and cell division. We demonstrate that iron starvation downregulates the transcription of genes encoding proteins involved in cell division, reduces protein biosynthesis, and prevents correct positioning of the division machinery at the division site. These combined events arrest the constriction of the cell during late stages of cytokinesis in a manner distinct from known mechanisms of inhibiting cell division. Overexpression of genes encoding cell division proteins or iron transporters partially suppresses the biological activity of iron chelators and restores growth and division. We propose a model demonstrating the effect of iron availability on the regulatory mechanisms coordinating division in response to the nutritional state of the cell.
    MeSH term(s) Bacteria/cytology ; Bacteria/drug effects ; Bacteria/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Benzimidazoles/metabolism ; Benzimidazoles/pharmacology ; Caulobacter crescentus/cytology ; Caulobacter crescentus/drug effects ; Caulobacter crescentus/metabolism ; Cobalt/pharmacology ; Copper/pharmacology ; Cytokinesis/drug effects ; Escherichia coli/cytology ; Escherichia coli/drug effects ; Escherichia coli/metabolism ; Gene Expression Regulation, Bacterial/drug effects ; Hydrazines/metabolism ; Hydrazines/pharmacology ; Iron/metabolism ; Iron/pharmacology ; Iron Chelating Agents/metabolism ; Iron Chelating Agents/pharmacology ; Naphthalenes/metabolism ; Naphthalenes/pharmacology ; Peptidoglycan/metabolism
    Chemical Substances Bacterial Proteins ; Benzimidazoles ; Hydrazines ; Iron Chelating Agents ; N'-((E)-(2-hydroxynaphthalen-1-yl)methylidene)-3-(2-methyl-1H-benzimidazol-1-yl)propanehydrazide ; Naphthalenes ; Peptidoglycan ; Cobalt (3G0H8C9362) ; Copper (789U1901C5) ; Iron (E1UOL152H7)
    Language English
    Publishing date 2017-12-20
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ISSN 1554-8937
    ISSN (online) 1554-8937
    DOI 10.1021/acschembio.7b00560
    Database MEDical Literature Analysis and Retrieval System OnLINE

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