A Comparative Study on the Virulence of Mycoplasma arthritidis And "Mycoplasma hominis, Type 2" Strains in Rats.

Cole, Barry C.; Miller, Matt; Ward, John

doi:10.3181/00379727-124-31676

Cited by 26 publications

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“…The 20 strains used in the present study contained four sets that were originally designated as or derived from the same strains but that had been maintained in different laboratories, sometimes for decades. Included among these were two PG6 strains (PG6 and 19611), two H606 strains (H606 and 13988), a set of four strains originally derived from Campo or PG27 (158, 23192, 14152, ATCC 14152) (4,13,14,33), and a set of three strains originally derived from Jasmin (Jasmin, 14124, ATCC 14124) (4,22). No changes in antigenic composition or restriction patterns were seen between PG6 and 19611 or between H606 and 13988 ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…This disease rarely occurs under natural conditions but is readily induced by the intravenous or intraperitoneal injection of M. arthritidis (6). Examination of reports from different laboratories that used different M. arthritidis strains indicates no dramatic differences in the nature of the diseases induced by the known virulent strains (4,8,16,17,19,24,43,47), although differences in the relative degree of arthritogenicity are prominent (16,17,19,22,53). In recent years several research groups, including our own, have begun to look more closely at those M. arthritidis cell components actually involved in host-parasite interaction.…”

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confidence: 99%

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Comparison of Mycoplasma arthritidis strains by enzyme-linked immunosorbent assay, immunoblotting, and DNA restriction analysis

et al. 1995

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Twenty Mycoplasma arthritidis strains or isolates were compared by a combination of enzyme-linked immunosorbent assay by an antiserum adsorption technique, Western immunoblotting, and restriction analysis of chromosomal DNA. Antigenic markers that defined strains related to strains 158p10p9, PG6, and H606 were identified. In addition, restriction analysis allowed all 20 strains to be divided into six groups. Results of restriction analysis corresponded generally with antigenic similarities, although the former did not allow grouping with as fine a precision as the latter. However, intrastrain antigenic variability, which is common among many Mycoplasma species, including M. arthritidis, introduced a complicating factor into our attempts at antigenic analysis. While serologic and antigenic analyses remain useful, we recommend that they be used with caution and in combination with other techniques for identifying and characterizing new isolates and newly acquired strains. Combinations of these techniques have proven to be useful in our laboratory for quality control and for uncovering interesting relationships among strains subjected to animal passage and their less virulent antecedents and among strains originally classified as the same but obtained from different sources and maintained, sometimes for decades, in different laboratories.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Comparison of Mycoplasma arthritidis strains by enzyme-linked immunosorbent assay, immunoblotting, and DNA restriction analysis

et al. 1995

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“…Strains used. The sources of M. arthritidis strains 14152, 158, 14124, El, and PN have been described elsewhere (5,7). In addition, strains R6 and DL were isolated by the authors from a rat lung and an inflamed rat joint, respectively.…”

Section: Materlils and Methodsmentioning

confidence: 99%

“…Although quantitative data are not available, passage of the agent in rats appears to increase the virulence of the organism (8,13,24,27,35). A recent study by Cole, Miller, and Ward (7) demonstrated that significant differences existed between the ability of fresh isolates and laboratory-maintained strains to induce arthritis. It was also shown that if sufficient numbers of colony-forming units (CFU) were injected into rats even the less virulent strains would induce arthritis.…”

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confidence: 99%

Effect of Animal Passage on Arthritogenic and Biological Properties of Mycoplasma arthritidis

et al. 1970

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Determinations of the ED50 of cultures of Mycoplasma arthritidis disclosed the existence of great diversity in the arthritogenic properties of the various strains. In most cases, the ED50 values were lowered after passaging in rats, and a more severe arthritis with a shorter period of onset was observed. Heavy suspensions of arthritogenic M. arthritidis did not appear to induce any toxic symptoms. Prior injections of endotoxin did not enhance the toxicity of M. arthritidis suspensions. The more arthritogenic strains grew more slowly in the basal medium and remained viable for longer periods of time than those with lower arthritogenic properties. All strains were identical on the basis of complement-fixation tests. Minor differences observed between strains during gel-diffusion studies could not be correlated with arthritogenic properties. Arthritogenic strains appeared to be less susceptible to the inhibiting action of rabbit antisera than were the nonarthritogenic strains. 538 on July 31, 2020 by guest http://iai.asm.org/ Downloaded from

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“…M. arthritidis strains 158p10p9 (5), 158 (3), and H606 (9) and the LA variant derived from strain 158p10p9 (17) were used in this study. Mycoplasma cultures were grown in modified Edward broth (EB) containing 2% (wt/vol) BBL mycoplasma broth base (Becton Dickinson and Company, Sparks, MD) and supplemented with 20% (vol/vol) heat-inacti-vated equine serum (HyClone, Logan, UT), 0.5% (wt/vol) L-arginine HCl (SigmaAldrich, St. Louis, MO), 0.5% (vol/vol) BBL IsoVitaleX, 0.2% (wt/vol) denatured salmon sperm DNA (ICN, Aurora, OH), 50 g/ml ampicillin, and 0.002% (wt/vol) phenol red.…”

Section: Methodsmentioning

confidence: 99%

Mutation of Two Mycoplasma arthritidis Surface Lipoproteins with Divergent Functions in Cytadherence

et al. 2008

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Mycoplasma arthritidis is a natural pathogen of rats, causing an acute polyarthritis. Previous studies identified two membrane-bound lipoproteins, Maa1 and Maa2, thought to be associated with cytadherence of M. arthritidis strain 158p10p9. We have since confirmed that Maa1 is a major adhesin, although the role of Maa2 has proven more elusive. Both proteins were capable of eliciting protective immunity in rats against challenge with the virulent strain 158p10p9, suggesting that they may be important in pathogenesis. The purpose of this study was to better understand the roles of Maa1 and Maa2 in cytadherence in vitro. Insertion mutants were created for both genes by transposon mutagenesis. In vitro adherence of the Maa1 mutant KOMaa1 to rat L2 lung cells was reduced to the level previously reported for a spontaneous low-adherence mutant of 158p10p9 in which Maa1 is truncated and nonfunctional. Surprisingly, adherence of the Maa2 mutant KOMaa2 was approximately fivefold greater than that of the wild type. Complementation of KOMaa1 and KOMaa2 with wild-type alleles of maa1 and maa2, respectively, returned adherence to wild-type levels. This work confirms our earlier observation that Maa1 is a major adhesin for M. arthritidis strain 158p10p9. Maa2, on the other hand, may play a suppressive or modulatory role, possibly serving to release organisms from microcolonies at certain stages of infection.Survival and virulence of pathogenic mycoplasmas are generally considered to be highly dependent on very close associations with host cells. However, early reports that Mycoplasma arthritidis could neither hemadsorb nor attach to mouse fibroblasts or macrophages indicated that it might be deficient in that regard (4, 9, 11). We have since confirmed that M. arthritidis does not hemadsorb, but we also observed that it did, in fact, adhere very well to primary rabbit synovial fibroblasts (16). We subsequently showed that M. arthritidis could also attach to several other cell types, although not to kidney cells, suggesting that specific receptors may be involved. Adherence was dose dependent and reached saturation, adherent cells could be depleted from the population by serial passage over cultured L2 rat lung cells, and major adhesins were surface exposed and trypsin sensitive (17). Two monoclonal antibodies (MAbs) from a panel raised against M. arthritidis membrane antigens partially inhibited attachment. One, designated A9a, was directed against a 90-kDa protein, and the other, designated 7a, was directed against a 71-kDa protein (17). These proteins were designated Maa1 and Maa2, respectively. M. arthritidis produced both proteins during the course of infection, and both were capable of eliciting protective immunity in rats, suggesting roles in pathogenesis (20).Further characterization revealed that Maa1 was an 86.5-kDa, basic, largely hydrophilic lipoprotein. Maa2 was a 61.4-kDa lipoprotein that was also basic and hydrophilic. Both proteins contained 29-amino-acid lipoprotein signal peptides that were 90% identical and 93%...

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A Comparative Study on the Virulence of Mycoplasma arthritidis And "Mycoplasma hominis, Type 2" Strains in Rats.

Cited by 26 publications

References 0 publications

Comparison of Mycoplasma arthritidis strains by enzyme-linked immunosorbent assay, immunoblotting, and DNA restriction analysis

Comparison of Mycoplasma arthritidis strains by enzyme-linked immunosorbent assay, immunoblotting, and DNA restriction analysis

Effect of Animal Passage on Arthritogenic and Biological Properties of Mycoplasma arthritidis

Mutation of Two Mycoplasma arthritidis Surface Lipoproteins with Divergent Functions in Cytadherence

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