MYCOPLASMAS

"Mycoplasmas are most unusual self-replicating bacteria, possessing very small genomes, lacking cell wall components, requiring cholesterol for membrane function and growth, using UGA codon for tryptophan, passing through "bacterial-retaining" filters, and displaying genetic economy that requires a strict dependence on the host for nutrients and refuge. In addition, many of the mycoplasmas pathogenic for humans and animals possess extraordinary specialized tip organelles that mediate their intimate interaction with eucaryotic cells. This host-adapted survival is achieved through surface parasitism of target cells, acquisition of essential biosynthetic precursors, and in some cases, subsequent entry and survival intracellularly. Misconceptions concerning the role of mycoplasmas in disease pathogenesis can be directly attributed to their biological subtleties and to fundamental deficits in understanding their virulence capabilities." (Baseman, 1997)

Members of the genus Mycoplasma [NCBI TAXONOMY] include over 100 documented human, animal and plant species and are the smallest organisms lacking cell walls that are capable of self-replication and cause various diseases in humans, animals, and plants. Seven different species of mycoplasma have been associated with various infections in humans to date. The earliest reports of mycoplasma infectious agents in humans appeared in the 1930s, 1940s and finally, in the early 1960s when the definite relationship between Mycoplasma pneumoniae as the primary cause of atypical pneumoniae was established.

Many strains of mycoplasma have been thought of in the past as benign bacteria commonly found in the gut and mucous and just a part of the "friendly" bacteria of the body which comprise the commensal microbial flora of healthy persons. However, recent advances in genome research and testing methodologies demonstrate that these mycoplasma may be implicated in the pathogenisis of many chronic diseases when they invade host cells and move out of the microbial flora and into other tissues, organs and the blood supply. A good example of this is that a common mycoplasma found in the urogenital tract, Mycoplasma genitalium, was recently found in the lung and upper repiratory tract of patients suffering from a range of upper respiratory diseases including chronic asthma. (Baseman, 1997) Conversely, Mycoplasma pneumoniae, normally only found in respiratory mucous, was isolated living in the human urogenital tract led researchers to suggest "that these mycoplasmas have evolved parasitic strategies that include overlapping tissue tropisms as determined by the genetic and chemical relatedness of their cytadherence genes and proteins."(Goulet 1995)

A review of the clinical documentation being performed around the world on mycoplasmas indicate that scientists are hypothesizing them to be cofactors or actual causes of many human diseases, including: chronic fatigue immune dysfunction syndrome, auto-immune disorders (lupus, multiple sclerosis and Lou Gehrig's Disease/ALS), arthritis, fibromyalgia, acquired immune deficiency syndrome, "idiopathic" cd4 positive t-lymphocytopenia (aka HIV-negative AIDS), psoriasis, scleroderma, Crohn's disease, cancers, lymphoma, leukemia, pelvic inflammatory disease, asthma, atypical pneumonia, Sjogren's syndrome, interstitial cytitis, and Alzheimer's disease.

To understand how mycoplasmas can cause chronic disease, we must first look at the species' unique properties and interactions with host cells. Unlike viruses and bacteria, mycoplasmas are the smallest free-living and self-duplicating microorganisms, as they don't require living cells to replicate their DNA and growth. More complex than viruses, mycoplasmas utilize RNA for replication, which in turn makes them susceptible only to the nucelophylic growth and/or protein synthesis inhibiting antibiotics. This antibiotic sensitivity was a clue used in the identification of the filtrable viral-like "Eaton Agent" as Mycoplasma pneumoniae, the cause of atypical pneumonia. This respiratory strain is now also suspected as a cause of arthritis, neurological and other localized disorders.

Mycoplasma's tiny viral-like size and pleomorphism (The variation in the appearance of the nuclei of the same cell type.) facilitates their cell penetration but limits their synthetic capacity, thus requiring preformed maco moleules from another host cell for growth and reproduction. These include basic peptides or protein fragments from enzyme digested tissues and constant cell replacement. Also required are nuecleotides, neucleic acid fragments, cholesterol and fatty acids in the form of nucleoproteins and lipoproteins. To survive and replicate, mycoplasmas can live intra and extracellularly as saprophytes utilizing the fragments from living, dead or dying cells. Their double layer lioprotein membrane controls the intracellular flow of nutrients and provides a highly unstable osmolar microbe, difficult to isolate and visualize. Interestingly, when scientists tried to culture strains of mycoplasmas, they were seen to actually mimic their culture media, leading reseearchers to conclude that their composition and properties would also mimic and vary among the in-vivo cultures of host tissues and fluids. For example, the cholesterol concentration in the host's mycoplasmas would depend on the host's cholesterol levels in blood and tissues. The wide variation in mycoplasma's composition of lipid, neucleic acid, and protein produced in a test tube culture may be even more variable in the hosts. Therefore, depending on which host cells the mycoplasma invade or attach to, it can actually morph into or mimic the host cells and begin competing for certain cellular nutrients like proteins, amino acids and lipids causing a deregulation of the cell without actually killing it.

Based on new advances in genome research pertaining to mycoplasmas and host cell interaction indicates the following:

"The genomes of most Mycoplasma species encode about 600 proteins. For example, The M. genitalium and M. pneumoniae genomes contain 470 and 677 protein-coding gene sequences, respectively, compared with 1,703 protein genes in Haemophilus influenzae and about 4,000 genes in E. Coli. The genomes of M. genitalium and M. pneumoniae have lost the genes involved in certain biosynthetic pathways, such as the genes for amino and fatty acid and vitamin synthesis. Since they are cell wall-deficient bacteria, there is a major reduction in genetic information needed for cell wall biosynthesis. Although Mycoplasma species carry a minimal set of genes involved in energy metabolism and biosynthesis, they still have the essential genes for DNA replication, transcription, translation, and the minimal number of rRNA and tRNA genes. The reduction in mycoplasmal genomes explains their need for host nutritional molecules. A significant number of mycoplasmal genes appear to be devoted to cell adhesion and attachment organelles as well as variable membrane surface antigens to maintain parasitism and evade host immune and nonimmune surveillance systems. Mycoplasma species variably express structurally heterogeneous cell surface antigens. Variations in the genes encoding cell surface adherence molecules reveal distinct patterns of mutations capable of generating changes in mycoplasma cell surface molecular size and antigenic diversity. Variable surface antigenic structures and rapid changes in their expression are thought to play important roles in the pathogenesis of mycoplasmal infections by providing altered structures for escape from immune responses and protein structures that enhance cell and tissue colonization and penetration of the mucosal barrier." (Nicolson, GL 1999)

Clearly, multiple pathways of interactions with host/target cells appears to be the modus operandi of the Mycoplasma species. This can result in a variety of diseases and chronic syndromes depending on which host cells are targeted and used. Documented interactions with host cells by mycoplasmas in the below referenced clinical documentation includes the following:

  • Certain Mycoplasma species can either activate or suppress host immune systems, and they may use these activities to evade host immune responses. For example, some mycoplasmas can inhibit or stimulate the proliferation of normal lymphocyte subsets, induce B-cell differentiation and trigger the secretion of cytokines, including interleukin-1 (IL-1), IL-2, IL-4, IL-6, tumor necrosis factor-a (TNFa), interferons, and granulocyte macrophage-colony stimulating factor (GM-CSF) from B-cells as well as other cell types. Moreover, it was also found that M. fermentans-derived lipids can interfere with the interferon (IFN)-g-dependent expression of MHC class II molecules on macrophages. This suppression results in impaired antigen presentation to helper T-cells in an experimental animal model. Also, mycoplasmas are able to secret soluble factors that can stimulate proliferation or inhibit the growth and differentiation of immune competent cells.
  • Mycoplasmas can target the host white blood cells (lymphocytes/WBC) for intracellular infection, and these cells have the unique ability to cross the blood-brain barrier over into the spinal fluid and d into the host central nervous system (CNS).
  • Once inside the host CNS, certain pathogenic mycoplasmas have been reported to activate the CNS hypothalamus/pituitary/adrenal axis and neuroendocrine system. The hypothalamus and pituitary glands form part of the human endocrine system which produces hormones that regulate nearly every bodily function. This involvement is hypothesized to contribute to diseases such as fibromyalgia, chronic fatigue, and some AIDS-related symptoms.[Yirmiya R, 1999]
  • Mycoplasma species are known to secrete immune-modulating substances. For example, immune cells are affected by spiralin, a well-characterized mycoplasmal lipoprotein that can stimulate the in vitro proliferation of human peripheral blood mononuclear cells. This stimulation of immune cells results in secretion of proinflammatory cytokines (TNFa, IL-1 or -6). Spiralin can also induce the maturation of murine B-cells.
  • Mycoplasmas can escape immune recognition by undergoing surface antigenic variations thus rapidly altering their cell surface structures. Such antigenic variability, the ability to suppress host immune responses, slow growth rates and intracellular locations may explain the chronic nature of mycoplasmal infections and the common inability of a host to suppress mycoplasmal infections with host immune and nonimmune responses.
  • Rapid adaptation to host microenvironments by mycoplasmas is usually accompanied by rapid changes in cell surface adhesion receptors for more successful cell binding and entry as well as rapid structural protein changes to mimic host antigenic structures (antigen mimicry). For example, during chronic, active arthritis the size and antigenic diversity of the surface lipoprotein Vaa antigen changes in structure and expression in vivo. Antigenic divergence of Vaa can affect the adherence properties of M. hominis and enhance evasion of host-mediated immunity. Variations in the Vaa genes reveal a distinct pattern of mutations that generate mycoplasma surface variations and thus avoid host immune responses.
  • Mycoplasmas can directly suppress host immune responses by initiating or enhancing apoptosis. For example, M. fermentans, a recently discovered mycoplasma found in the urine of HIV and AIDS positive patients, can initiate or enhance concanavalin A-induced apoptosis (programmed cell death) of T-cells. Relatively large amounts of nucleases are also expressed by Mycoplasma species, and these can be released intracellularly to cause degradation of host DNA. Mycoplasmal nucleases may also be involved in secondary necrosis seen in advanced mycoplasmal infections, as indicated by the occurrence of morphological characteristics of apoptosis (chromatin condensation) and necrosis (loss of membrane integrity and organelle swelling). Although mycoplasmas can release activated oxygen species that may be involved in initiating apoptosis, some Mycoplasma species, such as M. fermentans, express a novel cytolytic activity in a nonlipid protein fraction that has a cytocidal effect not mediated by the known mycoplasmal cytokines like TNFa.
  • In addition to apoptosis, mycoplasmas can also release growth inhibitory molecules into their surroundings, such as arginine deaminase. This enzyme can act as a growth-inhibitory substance that suppresses IL-2 production and receptor expression in T cells stimulated by non-specific mitogens, and it can induce the morphologic features of dying cells and DNA fragmentation indicative of apoptosis.
  • Hydrogen peroxide and superoxide radicals are generated by adhering mycoplasmas, which induces oxidative stress, including host cell membrane damage.
  • Competition for and depletion of nutrients or biosynthetic precursors by mycoplasmas, which disrupts host cell maintenance and function.
  • Existence of capsule-like material and electron-dense surface layers or structures, which provides increased integrity to the mycoplasma surface and confers immunoregulatory activities
  • High-frequency phase and antigenic variation, which results in surface diversity and possible avoidance of protective host immune defenses
  • Secretion or introduction of mycoplasmal enzymes, such as phospholipases, ATPases, hemolysins, proteases, and nucleases into the host cell milieu, which leads to localized tissue disruption and disorganization and chromosomal aberrations and tumor formation.
  • Intracellular residence, which sequesters mycoplasmas, establishes latent or chronic states, and circumvents mycoplasmicidal immune mechanisms and selective drug therapies




Referenced Mycoplasma Research and Documentation


Full Text Research Articles Available to Read Online

  • Baseman & Tully. Mycoplasmas: Sophisticated, Reemerging, and Burdened by Their Notoriety. Emerging Infectious Diseases 1997. [Full Text]
  • Nicolson, G., et.al., Diagnosis and integrative treatment of intracellular bacterial infections in Chronic Fatigue and Fibromyalgia Syndromes, Gulf War Illness, Rheumatoid Arthritis and other chronic illnesses. Clin. Pract. Alt. Medicine 2000; 1(2): 92-102 [Full Text]
  • Nasralla, M., et.al., Examination of mycoplasmas in blood of 565 Chronic Illness patients by polymerase chain reaction. Intern. J. Med. Biol. Environ. 2000; 28(1): 15-23. [Full Text]
  • Cassell, G.H., Infectious Causes of Chronic Inflammatory Diseases and Cancer. Emerging Infectious Diseases Vol 4:3 1998 [Full Text]
  • Razin, S., et.al., Molecular Biology and Pathogenicity of Mycoplasmas. Microbiol Mol Biol Rev 62: 1094-1156 [Full Text]
  • Nicolson, G. Mycoplasmal Infections in Chronic Illnesses: Fibromyalgia and Chronic Fatigue Syndromes, Gulf War Illness, HIV-AIDS and Rheumatoid Arthritis. Medical Sentinel, Volume 4, Number 5, September/October 1999, pp. 172-175, 191. [Full Text]
  • Brenner, C. MYCOPLASMAS AND HIV INFECTION: FROM EPIDEMIOLOGY TO THEIR INTERACTION WITH IMMUNE CELLS Frontiers in Bioscience 1, e42-54, August 1,1996 [Full Text]
  • Nicolson, G. The Pathogenesis and Treatment of Mycoplasmal Infections Antimicrob. Infect. Dis. Newsl. 1999; 17(11) : 81-88 [Full text]
  • Olivier Neyrolles, Phase Variations of the Mycoplasma penetrans Main Surface Lipoprotein Increase Antigenic Diversity. Infection and Immunity, April 1999, p. 1569-1578, Vol. 67, No. 4 [Full text]
  • Nicolson, G. Diagnosis and Treatment of Chronic Mycoplasmal Infections in Fibromyalgia and Chronic Fatigue Syndromes: Relationship to Gulf War Illness. Biomed. Therapy 1998; 16: 266-271 [Full text]
  • Nicolson, G. Identification And Treatment Of Chronic Infections In CFIDS, Fibromyalgia Syndrome And Rheumatoid Arthritis CFIDS Chronicle 1999; 12(3): 19-21 [Full text]
    Kaufmann, A., et.al., (1999). Induction of Cytokines and Chemokines in Human Monocytes by Mycoplasma fermentans-Derived Lipoprotein MALP-2. Infect. Immun. 67: 6303-6308 [Full text]
  • Nicolson, G., et.al., Role of Mycoplasmal Infections in Fatigue Illnesses: Chronic Fatigue and Fibromyalgia Syndromes, Gulf War Illness and Rheumatoid Arthritis J. Chronic Fatigue Syndr. 2000; 6(3/4):23-39 [Full Text]
  • Sharma, S., Detection and Confirmation of Mycoplasma pneumoniae in Urogenital Specimens by PCR. Journal of Clinical Microbiology, January 1998, p. 277-280, Vol. 36, No. 1 [Full Text]
  • Cartner, S.C., et.al., Roles of Innate and Adaptive Immunity in Respiratory Mycoplasmosis ( study on mice about contagiousness ) Infect Immun, August 1998, p. 3485-3491, Vol. 66, No. 8 [Full Text]
  • Nicolson, G., et.al., Diagnosis and Treatment of Chronic Infections in Chronic Fatigue Syndrome, Fibromyalgia Syndrome and Gulf War Illness International Journal of Occupational Medicine, Immunology and Toxicology 1996 ; 5 : 69-78 [Full text]
  • Mühlradt,P., et.al., Structure and Specific Activity of Macrophage-Stimulating Lipopeptides from Mycoplasma hyorhinis .Infection and Immunity, October 1998, p. 4804-4810, Vol. 66, No. 10 [Full Text]
  • Kenny, G. E., et.al., (1999). Ofloxacin Selects Gyrase Mutations in First-Step Mycoplasma hominis Mutants, whereas Sparfloxacin Selects Topoisomerase IV Mutations. Antimicrob. Agents Chemother. 43: 2493-2496 [Abstract] [Full Text]  
  • Bébéar, C. M.,et.al., (2000). Cloning and Nucleotide Sequence of the DNA Gyrase (gyrA) Gene from Mycoplasma hominis and Characterization of Quinolone-Resistant Mutants Selected In Vitro with Trovafloxacin. Antimicrob. Agents Chemother. 44: 2719-2722 [Abstract] [Full Text]  
  • Bébéar, C. M., et.al., 1998. Alterations in topoisomerase IV and DNA gyrase in quinolone-resistant mutants of Mycoplasma hominis obtained in vitro. Antimicrob. Agents Chemother. 42:2304-2311[Abstract/Full Text].
  • Bang, H.,et.al., (2000). Prolyl isomerases in a minimal cell: Catalysis of protein folding by trigger factor from Mycoplasma genitalium. Eur J Biochem 267: 3270-3280 [Abstract] [Full Text] 
  • Washburn, L. R., et.al., (1998). Molecular Characterization of Mycoplasma arthritidis Variable Surface Protein MAA2. Infect. Immun. 66: 2576-2586 [Abstract] [Full Text]  
  • Noormohammadi, A. H.,et.al., (1998). Multigene Families Encoding the Major Hemagglutinins in Phylogenetically Distinct Mycoplasmas. Infect. Immun. 66: 3470-3475 [Abstract] [Full Text]  
  • Neyrolles, O., Chambaud, I., Ferris, S., Prevost, M.-C., Sasaki, T., Montagnier, L., Blanchard, A. (1999). Phase Variations of the Mycoplasma penetrans Main Surface Lipoprotein Increase Antigenic Diversity. Infect. Immun. 67: 1569-1578 [Abstract] [Full Text]  
  • Seto, S., Miyata, M. (1998). Cell Reproduction and Morphological Changes in Mycoplasma capricolum. J. Bacteriol. 180: 256-264 [Abstract] [Full Text]  
  • Seto, S., Miyata, M. (1999). Partitioning, Movement, and Positioning of Nucleoids in Mycoplasma capricolum. J. Bacteriol. 181: 6073-6080 [Abstract] [Full Text]  
  • Duret, S., Danet, J.-L., Garnier, M., Renaudin, J. (1999). Gene Disruption through Homologous Recombination in Spiroplasma citri: an scm1-Disrupted Motility Mutant Is Pathogenic. J. Bacteriol. 181: 7449-7456 [Abstract] [Full Text]  
  • Calcutt, M. J., Lavrrar, J. L., Wise, K. S. (1999). IS1630 of Mycoplasma fermentans, a Novel IS30-Type Insertion Element That Targets and Duplicates Inverted Repeats of Variable Length and Sequence during Insertion. J. Bacteriol. 181: 7597-7607 [Abstract] [Full Text]  
  • Shen, X., Gumulak, J., Yu, H., French, C. T., Zou, N., Dybvig, K. (2000). Gene Rearrangements in the vsa Locus of Mycoplasma pulmonis. J. Bacteriol. 182: 2900-2908 [Abstract] [Full Text]  
  • Dybvig, K., French, C. T., Voelker, L. L. (2000). Construction and Use of Derivatives of Transposon Tn4001 That Function in Mycoplasma pulmonis and Mycoplasma arthritidis. J. Bacteriol. 182: 4343-4347 [Abstract] [Full Text]  
  • Kannan, T. R., Baseman, J. B. (2000). Expression of UGA-Containing Mycoplasma Genes in Bacillus subtilis. J. Bacteriol. 182: 2664-2667 [Abstract] [Full Text]  
  • Razin, S., Yogev, D., Naot, Y. (1998). Molecular Biology and Pathogenicity of Mycoplasmas. Microbiol Mol Biol Rev 62: 1094-1156 [Abstract] [Full Text]  
  • Dybvig, K., Sitaraman, R., French, C. T. (1998). A family of phase-variable restriction enzymes with differing specificities generated by high-frequency gene rearrangements. Proc. Natl. Acad. Sci. U. S. A. 95: 13923-13928 [Abstract] [Full Text]  
  • Dhandayuthapani, S., Rasmussen, W. G., Baseman, J. B. (1999). Disruption of gene mg218 of Mycoplasma genitalium through homologous recombination leads to an adherence-deficient phenotype. Proc. Natl. Acad. Sci. U. S. A. 96: 5227-5232 [Abstract] [Full Text]  


Chronic Fatigue Syndrome and Fibromyalgia

Buskila D. Fibromyalgia, chronic fatigue syndrome, and myofascial pain syndrome. Curr Opin Rheumatol. 2000 Mar;12(2):113-23. Review.
Nicolson, G. Chronic Infections in Fibromyalgia Syndrome: Sources of Morbidity and Illness Progression. Fibromyalgia Survivor 2000
Nasralla M, Multiple mycoplasmal infections detected in blood of patients with chronic fatigue syndrome and/or fibromyalgia syndrome. Eur J Clin Microbiol Infect Dis. 1999 Dec;18(12):859-65.
Nasralla, M. Mycoplasmal Infections in Blood from Patients with Chronic Fatigue Syndrome, Fibromyalgia Syndrome or Gulf War Illness International CFS Congress, Sydney, Australia, 1998
Vojdani A, Detection of Mycoplasma genus and Mycoplasma fermentans by PCR in patients with Chronic Fatigue Syndrome. FEMS Immunol Med Microbiol. 1998 Dec;22(4):355-65.
Nicolson, G.L., et.al., New Treatments for Chronic Infections,Found in Fibromyalgia, Syndrome, Chronic Fatigue Syndrome, Rheumatoid Arthritis and Gulf War Illness
Nicolson, G. Identification and Treatment of Chronic Infections in Fibromyalgia Syndrome FMS Newsletter 1999
Choppa PC, Multiplex PCR for the detection of Mycoplasma fermentans, M. hominis and M. penetrans in cell cultures and blood samples of patients with chronic fatigue syndrome. Mol Cell Probes. 1998 Oct;12(5):301-8.
Nicolson, G., et.al. Identification and Treatment of Chronic Infections in CFIDS, Fibromyalgia Sydrome and Rheumatoid Arthritis Patients that Cause Morbidity and Illness Progression Doctor's Educational Booklet, CFIDS Assoc. of America 1998
Yirmiya R, The role of brain cytokines in mediating the behavioral and neuroendocrine effects of intracerebral mycoplasma fermentans. Brain Res. 1999 May 22;829(1-2):28-38.


Arthritis and Rheumatoid Arthritis

Horowitz S, et.al., Mycoplasma fermentans in rheumatoid arthritis and other inflammatory arthritides. J Rheumatol. 2000 Dec;27(12):2747-53.
Cole, B. C., et.al., Triggering and exacerbation of autoimmune arthritis by the Mycoplasma arthritidis superantigen MAM. Arthritis Rheum. 36:994-1002
Marie, C., et.al., (1999). Involvement of Mitogen-Activated Protein Kinase Pathways in Interleukin-8 Production by Human Monocytes and Polymorphonuclear Cells Stimulated with Lipopolysaccharide or Mycoplasma fermentans Membrane Lipoproteins. Infect. Immun. 67: 688-693
Mercola, J.M., PROTOCOL FOR USING ANTIBIOTICS IN THE TREATMENT OF RHEUMATIC DISEASES As Presented at the 31st Annual Meeting of the American Academy of Environmental Medicine Boston, Massachusetts - October 1996
Clark, HW., Mycoplasmas Properties and their Role in Autoimmune Diseases. San Marcos University College of Veterinarian Medicine Lima, Peru Lectures 8/99
Schaeverbeke, T., et.al., 1996. Mycoplasma fermentans in joints of patients with rheumatic arthritis and other joint disorders. Lancet. 347: 1418
Piec, G., et.al. Effect of MALP-2, a Lipopeptide from Mycoplasma fermentans, on Bone Resorption In Vitro. Infection and Immunity, December 1999, p. 6281-6285, Vol. 67, No. 12
Quentmeier, H., et.al., 1990. Mycoplasma fermentans-derived high molecular weight material induces interleukin-6 release in cultures of murine macrophages and human monocytes. Infect. Immun. 58: 1273-1280
Schaeverbeke, T., et.al., Systematic detection of mycoplasmas by culture and polymerase chain reaction (PCR) procedures in 209 synovial fluid samples. Br. J. Rheumatol. 36:310-314
Mu, H.-H., et.al., Modulation of Cytokine Profiles by the Mycoplasma Superantigen Mycoplasma arthritidis Mitogen Parallels Susceptibility to Arthritis Induced by M. arthritidis. Infect. Immun. 68: 1142-1149
Clark, H. MYCOPLASMAS & RHEUMATIC DISEASE: The Physician's Page Vol. 3, No. 3 © A Publication of The Road Back Foundation
Cole, B. C., et.al, Stimulation of mouse lymphocytes by a mitogen derived from Mycoplasma arthritidis (MAM). VIII. Selective activation of T cells expressing distinct V beta T cell receptors from various strains of mice by the "superantigen" MAM. J. Immunol. 144:425-431
Cole, B. C., et.al., The Mycoplasma arthritidis T-cell mitogen, MAM: a model superantigen. Immunol. Today 12:271-276
Schaeverbeke, T., et.al., Mycoplasma fermentans, but not M. penetrans, detected by PCR assays in synovium from patients with rheumatoid arthritis and other rheumatic disorders. J. Clin. Pathol. 49:824-828
Cole, B. C., L. R. Washburn, and D. Taylor-Robinson. 1985. Mycoplasma-induced arthritis, p. 107-160. In S. Razin, and M. F. Barile (ed.), The mycoplasmas, vol. IV. Mycoplasma pathogenicity. Academic Press, Inc., Orlando, Fla.
Pubmed/Medline Abstracts Too many to list


Autoimmune Diseases

Baseman, J. B., et.al., Interplay between mycoplasma surface proteins, airway cells, and the protean manifestations of mycoplasma-mediated human infections. Am. J. Respir. Crit. Care Med. 154:S137-S144[Medline].
Greenlee JE, et.al., Controversies in neurological infectious diseases. Semin Neurol. 2000;20(3):375-86.
Feizi, T., et.al., Carbohydrate recognition by Mycoplasma pneumoniae and pathologic consequences. Am. J. Res. Crit. Care Med. 154:S133-S136
Hodtsev, A. S., et.al., 1998. Mycoplasma Superantigen Is a CDR3-dependent Ligand for the T Cell Antigen Receptor. J. Exp. Med. 187: 319-327
Nishimura, et.al., Post infections encephalitis with anti-galactocerebroside antibody subsequent to Mycoplasma pneumoniae infection. J. Neurol. Sci. 140:91-95
Ginsburg KS, Ureaplasma urealyticum and Mycoplasma hominis in women with systemic lupus erythematosus. Arthritis Rheum. 1992 Apr;35(4):429-33.
Razin, S., et.al., Molecular Biology and Pathogenicity of Mycoplasmas. [Section: INTERACTIONS WITH THE HOST IMMUNE SYSTEM] Microbiol Mol Biol Rev 62: 1094-1156
Cole, B. C., et.al., Genomic composition and allelic polymorphisms influence V beta usage by the Mycoplasma arthritidis superantigen. J. Immunol. 150:3291-3299
PubMed/Medine Abstracts Too many to list


Amyotrophic Lateral Sclerosis (ALS) / Lou Gehrig's Disease
Website with compiled research


Leukemia

Alexander FE. Is Mycoplasma Pneumonia associated with childhood acute lymphoblastic leukemia? Cancer Causes Control. 1997 Sep;8(5):803-11.
Reyes, L., et.al., (1999). Effects of Mycoplasma fermentans incognitus on Differentiation of THP-1 Cells [monocytoid leukemic cell line]. Infect. Immun. 67: 3188-3192
PubMed/Medline Abstracts Too many to list


Cancer

Razin, S., et.al., Molecular Biology and Pathogenicity of Mycoplasmas. [Section: Clastogenic and Oncogenic Effects] Microbiol Mol Biol Rev 62: 1094-1156
Pubmed/Medline Abstracts Too many to list


Asthma

Chu HW, et.al., Substance P and its receptor neurokinin 1 expression in asthmatic airways. J Allergy Clin Immunol. 2000 Oct;106(4):713-22.
Daian CM, et.al., The role of atypical organisms in asthma. Allergy Asthma Proc. 2000 Mar-Apr;21(2):107-11. Review.
Freymuth F, et.al., Detection of viral, Chlamydia pneumoniae and Mycoplasma pneumoniae infections in exacerbations of asthma in children. J Clin Virol. 1999 Aug;13(3):131-9.
Sabato AR, et.al., Mycoplasma pneumoniae: acute illness, antibiotics, and subsequent pulmonary function. Arch Dis Child 1984;59:1034-7.
Seggev JS, et al. Mycoplasma pneumoniae is a frequent cause of exacerbation of bronchial asthma in adults. Annals of Allergy 1986;57:263-5.
Yano T, et.al., Association of Mycoplasma pneumoniae antigen with initial onset of bronchial asthma. Am J Respir Crit Care Med 1994;149:1348-53.
Henderson FW, et al. The etiologic and epidemiologic spectrum of bronchiolitis in pediatric practice. J Pediatr 1979;95:183-90.
Atmar RL. Chlamydia Species and Mycoplasma pneumoniae. Curr Infect Dis Rep. 1999 Apr;1(1):73-79.
Cassell, G.H., Infectious Causes of Chronic Inflammatory Diseases and Cancer. Emerging Infectious Diseases Vol 4:3 1998
Kraft M, et al. Detection of Mycoplasma pneumoniae in the airways of adults with chronic asthma. Am J Resp Crit Care Med. In press 1998.
Cassell GH, Clyde WA, Davis JK. Mycoplasmal res-piratory infections. In: Razin S, Tully JG, editors. The Mycoplasmas. New York: Academic Press; 1985. p. 66-106.
Shimuzu T, et.al., Immunoglobulin levels, number of eosinophils in the peripheral blood and bronchial hypersensitivity in children with Mycoplasma pneumoniae pneumonia. Japanese Journal of Allergology 1991;40:21-7.
Other Medline/PubMed Abstracts - Too many to list

HIV/AIDS

Hussain, A., et.al., Mycoplasma penetrans and Other Mycoplasmas in Urine of Human Immunodeficiency Virus-Positive Children J. Clin. Microbiol. 37: 1518-1523.
Shang, H.,et.al., 1995. Suppression of HIV-1 reverse transcriptase activity by culture supernatants of mycoplasmas. Microbiol. Immunol. 39:987-993
Lo, S.-C., et.al., 1989. Identification of Mycoplasma incognitus infection in patients with AIDS: an immunohistochemical, in situ hybridization and ultrastructural study. Am. J. Trop. Med. Hyg. 41: 601-616
Blanchard, A., and L. Montagnier. 1994. Aids-associated mycoplasmas. Annu. Rev. Microbiol. 48:687-712[Abstract].
Shibata, K., et.al., 1995. AIDS-associated mycoplasmas possess phospholipase C in the membrane. Infect. Immun. 63:4174-4177
SA Poulin, et.al., Antibiotic susceptibilities of AIDS-associated mycoplasmas J. Clin. Microbiol. 32: 1101-1103.
Bendjennat, M., et.al., (1999). Role of Mycoplasma penetrans Endonuclease P40 as a Potential Pathogenic Determinant. Infect. Immun. 67: 4456-
Kikkawa, S., et.al., Complement Activation in Mycoplasma fermentans-Induced Mycoplasma Clearance from Infected Cells: Probing of the Organism with Monoclonal Antibodies against M161Ag. Infect. Immun. 68: 1672-1680
Lo, S.-C.,et.al., 1991. Newly discovered mycoplasma isolated from patients infected with HIV. Lancet. 338: 1415-1418
Grau, O., et.al., 1998. A longitudinal study of seroreactivity against Mycoplasma penetrans in HIV infected homosexual men: association with disease progression. AIDS Res. Hum. Retroviruses 14:664-667.
Spergser J. Host-pathogen interactions in mycoplasma pathogenesis: virulence and survival strategies of minimalist prokaryotes. Int J Med Microbiol. 2000 Mar;290(1):15-25.
Pubmed/Medline Abstracts Too many too list


Gulf War Syndrome

Nicolson, G. Diagnosis and Treatment of Chronic Mycoplasmal Infections in Fibromyalgia and Chronic Fatigue Syndromes: Relationship to Gulf War Illness. Biomed. Therapy 1998; 16: 266-271 [Full text]
Nicolson G, et.al., Gulf War illnesses. Medicine, Conflict, and Survival 1998;14:156-65.
Knoke JD, Gray GC. Hospitalizations for unexplained illnesses among U.S. veterans of the Persian Gulf War. Emerg Infect Dis 1998;4:211-19.
Fukada K, et al. Chronic multisystem illnesses affecting Air Force veterans of the Gulf War. JAMA 1998;280:981-8.
WRITTEN TESTIMONY OF Dr. Garth L. Nicolson, Special Oversight Board for Department of Defense Investigations of Gulf War Chemical and Biological Incidents November 19, 1998




Other Online Resources:

HSI Article on mycoplasmas and autoimmune disorders

Textbook Descriptions of Mycoplasmas From Medical Microbiology by Dr. Samuel Baron, MD
The International Organization of Mycoplasmology
MYCOPLASMAS By Errol Prasad & Richard Lim-Fong, Microbiology & Public Health of Northern Alberta (Cananda)
The Institute for Molecular Medicine offers laboratory testing for mycoplasmal infections and a good amount of information and research on their website.
Medical Diagnostic Labs offers laboratory testing.
SEARCH the Center for Disease Control and Prevention website for documents on mycoplasmas.


The above text has been authored by Leslie Taylor, Milam County, Texas 77857 and copyrighted © 2001. All rights reserved. Please refer to the Copyright Statement on permitted uses of this document.

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Last updated 12-21-2012