• Disease
  • Mycoplasma
  • Mycoplasma Pneumoniae
  • Mitchell F Balish

    Prominent publications by Mitchell F Balish

    KOL Index score: 13103

    The consensus of the members of the International Committee on Systematics of Prokaryotes' Subcommittee on the taxonomy of Mollicutes is that recently proposed sweeping changes to nomenclature of members of the Mycoplasmatales, specifically involving introduction of the names Malacoplasma gen. nov., Mesomycoplasma gen. nov., Metamycoplasma gen. nov., Metamycoplasmataceaefam. nov., Mycoplasmoidaceaefam. nov., Mycoplasmoidalesord. nov., Mycoplasmoides gen. nov., Mycoplasmopsis gen. nov., ...

    Also Ranks for: Mycoplasmoides Gen |  mycoplasmoidaceae fam |  proposed species |  recommended rejection |  names malacoplasma
    KOL Index score: 10231

    Within the genus Mycoplasma are species whose cells have terminal organelles, polarized structures associated with cytadherence and gliding motility. Mycoplasma penetrans, found mostly in HIV-infected patients, and Mycoplasma iowae, an economically significant poultry pathogen, are members of the Mycoplasma muris phylogenetic cluster. Both species have terminal organelles that interact with host cells, yet the structures in these species, or any in the M. muris cluster, remain ...

    Also Ranks for: Mycoplasma Penetrans |  gliding motility |  host cells |  scanning electron |  time lapse
    KOL Index score: 9419

    The terminal organelle of the cell wall-less pathogenic bacterium Mycoplasma pneumoniae is a complex structure involved in adherence, gliding motility and cell division. This membrane-bound extension of the mycoplasma cell possesses a characteristic electron-dense core. A number of proteins having direct or indirect roles in M. pneumoniae cytadherence have been previously localized to the terminal organelle. However, the cytadherence-accessory protein HMW2, which is required for the ...

    Also Ranks for: Mycoplasma Pneumoniae |  terminal organelle |  protein hmw2 |  green fluorescent |  cell division
    KOL Index score: 8199

    The surface protein P65 is a constituent of the Mycoplasma pneumoniae cytoskeleton and is present at reduced levels in mutants lacking the cytadherence accessory protein HMW2. Pulse-chase studies demonstrated that P65 is subject to accelerated turnover in the absence of HMW2. P65 was also less abundant in noncytadhering mutants lacking HMW1 or P30 but was present at wild-type levels in mutants lacking proteins A, B, C, and P1. P65 exhibited a polar localization like that in wild-type M. ...

    Also Ranks for: Mycoplasma Pneumoniae |  subcellular localization |  proteins p65 |  hmw1 hmw2 |  publication adhesins
    KOL Index score: 7767

    Several mycoplasma species have been shown to form biofilms that confer resistance to antimicrobials and which may affect the host immune system, thus making treatment and eradication of the pathogens difficult. The present study shows that the biofilms formed by two strains of the human pathogen Mycoplasma pneumoniae differ quantitatively and qualitatively. Compared with strain UAB PO1, strain M129 grows well but forms biofilms that are less robust, with towers that are less smooth at ...

    Also Ranks for: Mycoplasma Pneumoniae |  2 strains |  type 1 |  biofilm formation |  host immune
    KOL Index score: 7762

    Mycoplasma pneumoniae attachment to host cells requires biogenesis of a functional attachment organelle, including proper localization of the adhesion protein P1 to this structure. Mutations in the hmw2 gene result in the inability to cytadhere, failure to localize P1 to the attachment organelle, altered cell morphology and accelerated turnover of the cytadherence-associated proteins HMW1, HMW3 and P65. The hmw2 gene encodes HMW2 (190 kDa) and P28 (28 kDa), the latter apparently the ...

    Also Ranks for: Mycoplasma Pneumoniae |  protein hmw2 |  attachment organelle |  host cells |  gene deletion
    KOL Index score: 7674

    Mycoplasma pneumoniae adsorbs to host respiratory epithelium primarily by its attachment organelle, the proper function of which depends upon mycoplasma adhesin and cytoskeletal proteins. Among the latter are the cytadherence-associated proteins HMW1 and HMW2, whose specific roles in this process are unknown. In the M. pneumoniae cytadherence mutant I-2, loss of HMW2 results in accelerated turnover of HMW1 and other cytadherence-accessory proteins, probably by proteolysis. However, both ...

    Also Ranks for: Mycoplasma Pneumoniae |  triton shell |  cytoskeletal proteins |  cell surface |  sequence bacterial
    KOL Index score: 7530

    The cytoskeletal proteins HMW1 and HMW2 are components of the terminal organelle of the cell wall-less bacterium Mycoplasma pneumoniae. HMW1 is required for a tapered, filamentous morphology but exhibits accelerated turnover in the absence of HMW2. Here, we report that a reciprocal dependency exists between HMW1 and HMW2, with HMW2 subject to accelerated turnover with the loss of HMW1. Furthermore, the instability of HMW2 correlated with its failure to localize to the attachment ...

    Also Ranks for: Mycoplasma Pneumoniae |  terminal organelle |  bacterial proteins |  stability function |  publication adhesins
    KOL Index score: 7243

    The Mycoplasma pneumoniae cluster is a clade of eight described species which all exhibit cellular polarity. Their polar attachment organelle is a hub of cellular activities including cytadherence and gliding motility, and its duplication in the species M. pneumoniae is coordinated with cell division and DNA replication. The attachment organelle houses a detergent-insoluble, electron-dense core whose presence is required for structural integrity. Although mutant analysis has led to the ...

    Also Ranks for: Mycoplasma Pneumoniae |  attachment organelle |  gliding motility |  cell division |  dna replication
    KOL Index score: 7069

    Since its initial description in the 1940s and eventual elucidation as a highly evolved pathogenic bacterium, Mycoplasma pneumoniae has come to be recognized as a worldwide cause of primary atypical pneumonia. Beyond its ability to cause severe lower respiratory illness and milder upper respiratory symptoms it has become apparent that a wide array of extrapulmonary infectious and postinfectious events may accompany the infections in humans caused by this organism. Autoimmune disorders ...

    Also Ranks for: Mycoplasma Pneumoniae |  clinical manifestations |  laboratory detection |  chronic diseases |  minimal genome
    KOL Index score: 6872

    Despite their small size and reduced genomes, many mycoplasma cells have complex structures involved in virulence. Mycoplasma pneumoniae has served as a model for the study of virulence factors of a variety of mycoplasma species that cause disease in humans and animals. These cells feature an attachment organelle, which mediates cytadherence and gliding motility and is required for virulence. An essential component of the architecture of the attachment organelle is an internal ...

    Also Ranks for: Mycoplasma Amphoriforme |  gliding motility |  attachment organelle |  timelapse microcinematography |  respiratory pathogen
    KOL Index score: 6370

    Mycoplasma pneumoniae is a bacterial pathogen of humans that is a major causative agent of chronic respiratory disease. M. pneumoniae infections often recur even after successful treatment of symptoms with antibiotics, and resistance to antibiotics is increasing worldwide, with nearly complete resistance in some places. Although biofilms often contribute to chronicity and resistance, M. pneumoniae biofilms remain poorly characterized. Scanning electron microscopy revealed that cells of ...

    Also Ranks for: Mycoplasma Pneumoniae |  biofilm towers |  limited role |  scanning electron |  bacterial pathogen
    KOL Index score: 6227

    Mycoplasma pneumoniae is a minimal microbe with respect to cell envelope composition, biosynthetic and regulatory capabilities and genome size, yet it possesses a remarkably complex, multifunctional terminal organelle. This membrane-bound extension of the mycoplasma cell is defined by the presence of an electron-dense core that appears as paired, parallel bars oriented longitudinally and enlarging at the distal end to form a terminal button. Most non-cytadhering mutants of M. pneumoniae ...

    Also Ranks for: Terminal Organelle |  mycoplasma pneumoniae |  electrondense core |  cell division |  genome size
    KOL Index score: 6051

    Mycoplasmas are cell wall-less bacteria at the low extreme in genome size in the known prokaryote world, and the minimal nature of their genomes is clearly reflected in their metabolic and regulatory austerity. Despite this apparent simplicity, certain species such as Mycoplasma pneumoniae possess a complex terminal organelle that functions in cytadherence, gliding motility, and cell division. The attachment organelle is a membrane-bound extension of the cell and is characterized by an ...

    Also Ranks for: Terminal Organelle |  mycoplasma cytoskeleton |  cell division |  genome size |  sequence bacterial
    KOL Index score: 5600

    Mycoplasma pneumoniae is a common cause of upper and lower respiratory tract infections in persons of all ages and may be responsible for up to 40% of community-acquired pneumonias. A wide array of extrapulmonary events may accompany the infections caused by this organism, related to autoimmunity or direct spread. This review includes a discussion of the latest knowledge concerning the molecular pathological basis of mycoplasmal respiratory disease, how the organism interacts with the ...

    Also Ranks for: Mycoplasma Pneumoniae |  macrolide resistance |  host immune |  infections organism |  bacterial humans


    Mitchell F Balish: Influence Statistics

    Sample of concepts for which Mitchell F Balish is among the top experts in the world.
    Concept World rank
    motility mycoplasma penetrans #1
    nov mycoplasmoides gen #1
    terminal organelles #1
    nov mesomycoplasma gen #1
    mycoplasma insons mycoplasmas #1
    130 110kda myosin #1
    model protective towers #1
    iowae serovar strain #1
    towers individual #1
    canis dh82 cells #1
    myosin purified mitochondria #1
    motility mycoplasma pneumoniae #1
    iowae oxidative #1
    structures mycoplasmas #1
    cells meningoencephalitis #1
    biofilms pneumoniae infections #1
    microscopy penetrans #1
    gliding motor activity #1
    strain ii3r #1
    mycoplasmas gliding motility #1
    penetrans fluorescence microscopy #1
    gallisepticum amphoriforme cells #1
    iowae presence #1
    insons 16s #1
    pneumoniae protective biofilms #1
    combat mycoplasma #1
    cellular organization mycoplasma #1
    cytoskeleton microscopy electron #1
    biofilm towers #1
    p32 cytadherence ability #1
    mycoplasma insons electron #1
    cards toxin levels #1
    catalase mycoplasma iowae #1
    energy sources motility #1
    penetrans gliding motility #1
    penetrans gliding #1
    cells terminal organelles #1
    microsomes myosin #1
    cells towers #1
    malacoplasma gen #1
    attachment organelles #1

    Key People For Mycoplasma Pneumoniae

    Top KOLs in the world
    Ken B Waites
    mycoplasma pneumoniae united states ureaplasma urealyticum
    Deborah F Talkington
    mycoplasma pneumoniae united states typhoid fever
    Wallace A Clyde
    mycoplasma pneumoniae attachment protein monoclonal antibodies
    Joel Barry Baseman
    mycoplasma pneumoniae cards toxin treponema pallidum
    Enno Jacobs
    mycoplasma pneumoniae legionella pneumophila bacterial antigens
    mycoplasma pneumoniae extrapulmonary manifestations cerebrospinal fluid

    Mitchell F Balish:Expert Impact

    Concepts for whichMitchell F Balishhas direct influence:Mycoplasma pneumoniae,  Mycoplasma penetrans,  Mycoplasma iowae,  Terminal organelle,  Gliding motility,  Attachment organelle,  Mycoplasma insons,  Host cells.

    Mitchell F Balish:KOL impact

    Concepts related to the work of other authors for whichfor which Mitchell F Balish has influence:Mycoplasma pneumoniae,  Macrolide resistance,  Gliding motility,  Terminal organelle,  Mp infection,  Cards toxin,  Respiratory tract.



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    Department of Microbiology, Miami University, Oxford, OH 45056, USA | Department of Microbiology, Miami University, 212 Pearson Hall, Oxford, OH 45056, USA | Department of Microbiology, Miami University, Oxford, OH, United States | Miami University,