The Hemagglutination-Positive Phenotype of<i>Mycoplasma synoviae</i>Induces Experimental Infectious Synovitis in Chickens More Frequently than Does the Hemagglutination-Negative Phenotype

Narat, Mojca; Benčina, Dušan; Kleven, S. H.; Habe, F.

doi:10.1128/iai.66.12.6004-6009.1998

Cited by 41 publications

(38 citation statements)

References 31 publications

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“…It releases a superantigen whose structure has been elucidated and whose functional domains were identified (4). However, other mycoplasma species, which do not produce or release superantigens, may also be associated with rheumatoid arthritis in various animal hosts such as chickens (30), swine (17), goats (40,41), or cattle (34). In human adults and occasionally children, mycoplasma arthritis has been recorded in association with hypogammaglobulinemia (9,35).…”

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confidence: 99%

Effect of MALP-2, a Lipopeptide from Mycoplasma fermentans , on Bone Resorption In Vitro

et al. 1999

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Mycoplasmas may be associated with rheumatoid arthritis in various animal hosts. In humans, mycoplasma arthritis has been recorded in association with hypogammaglobulinemia. Mycoplasma fermentans is one mycoplasma species considered to be involved in causing arthritis. To clarify which mycoplasmal compounds contribute to the inflammatory, bone-destructive processes in arthritis, we used a well-defined lipopeptide, 2-kDa macrophage-activating lipopeptide (MALP-2) from M. fermentans, as an example of a class of macrophageactivating compounds ubiquitous in mycoplasmas, to study its effects on bone resorption. MALP-2 stimulated osteoclast-mediated bone resorption in murine calvaria cultures, with a maximal effect at around 2 nM. Antiinflammatory drugs inhibited MALP-2-mediated bone resorption by about 30%. This finding suggests that MALP-2 stimulates bone resorption partially by stimulating the formation of prostaglandins. Since interleukin-6 (IL-6) stimulates bone resorption, we investigated IL-6 production in cultured calvaria. MALP-2 stimulated the liberation of IL-6, while no tumor necrosis factor was detectable. Additionally, MALP-2 stimulated low levels of NO in calvaria cultures, an effect which was strongly increased in the presence of gamma interferon, causing an inhibition of bone resorption. MALP-2 stimulated the bone-resorbing activity of osteoclasts isolated from long bones of newborn rats and cultured on dentine slices without affecting their number. In bone marrow cultures, MALP-2 inhibited the formation of osteoclasts. It appears that MALP-2 has two opposing effects: it increases the bone resorption in bone tissue by stimulation of mature osteoclasts but inhibits the formation of new ones.

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confidence: 99%

Effect of MALP-2, a Lipopeptide from Mycoplasma fermentans , on Bone Resorption In Vitro

et al. 1999

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“…The M. synoviae strain ULB 925 was isolated from a swollen chicken tibiotarsal‐tarsometatarsal joint which had been inoculated with strain AAY‐4 of M. synoviae : it is likely to be a derivative of the AAY‐4 strain [8]. HA + and HA − cultures of the M. synoviae type strain WVU 1853 were received from Dr. Janet M. Bradbury, University of Liverpool.…”

Section: Methodsmentioning

confidence: 99%

“…The mAb 3E10/C9 was raised against the electroeluted M. synoviae AAY‐4 hemagglutinating protein using the procedure described [5]. The mAb 3E10 (IgG 1 ) inhibits binding of M. synoviae to chicken erythrocytes and reacts with major membrane proteins of M. synoviae of about 50 kDa [8]. We designated proteins detected by the mAb 3E10 as hemadherent proteins pMSA 1 .…”

Section: Methodsmentioning

confidence: 99%

“…For sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE), isoelectric focusing (IEF) and immunoblotting the PhastSystem (LKB Pharmacia) was used according to procedures described elsewhere [8]. In consecutive immunoblots, the first staining was conducted with diaminobenzidine tetrahydrochloride (DAB, Sigma).…”

Section: Methodsmentioning

confidence: 99%

“…We have already reported that hemagglutination in M. synoviae strain AAY‐4 involves immunogenic membrane proteins of 48–50 and 53 kDa which are antigenically distinct proteins and show phase variable expression [4]. Very recently we have reported that the inoculation with hemagglutination positive (HA + ) cultures of M. synoviae strain AAY‐4 induced acute synovitis significantly more frequently ( P = 0.001) in chicken hock joints than did the inoculation with hemagglutination negative (HA − ) cultures derived from the same clone of AAY‐4 [8]. Thus, at least in M. synoviae strain AAY‐4 HA + cultures, the presence of proteins involved in the hemadherence is associated with a higher pathogenicity.…”

Section: Introductionmentioning

confidence: 99%

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The characterization ofMycoplasma synoviaeEF-Tu protein and proteins involved in hemadherence and their N-terminal amino acid sequences

Benčina¹,

Narat

Dovč

et al. 1999

FEMS Microbiology Letters

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An abundant cytoplasmic 43-kDa protein from Mycoplasma synoviae, a major pathogen from poultry, was identified as elongation factor Tu. The N-terminal amino acid sequence (AKLDFDRSKEHVNVGTIGHV) has 90% identity with the sequence of the Mycoplasma hominis elongation factor Tu protein. Monoclonal antibodies reacting with the M. synoviae elongation factor Tu protein also reacted with 43-kDa proteins from the avian Mycoplasma species Mycoplasma gallinarum, Mycoplasma gallinaceum, Mycoplasma pullorum, Mycoplasma cloacale, Mycoplasma iners and Mycoplasma meleagridis, but not with the proteins from Mycoplasma gallisepticum, Mycoplasma imitans or Mycoplasma iowae. In addition, two groups of phase variable integral membrane proteins, pMSA and pMSB, associated with hemadherence and pathogenicity of M. synoviae strains AAY-4 and ULB925 were identified. The cleavage of a larger hemagglutinating protein encoded by a gene homologous to the vlhA gene of M. synoviae generates pMSB1 and pMSA1 proteins defined by mAb 125 and by hemagglutination inhibiting mAb 3E10, respectively. The N-terminal amino acid sequences of pMSA proteins (SENKLI ... and SENETQ ...) probably indicate the cleavage site of the M. synoviae strain ULB 925 hemagglutinin.

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Mycoplasmosis

Ferguson‐Noel¹,

Armour²,

Noormohammadi³

et al. 2019

Diseases of Poultry

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The Hemagglutination-Positive Phenotype ofMycoplasma synoviaeInduces Experimental Infectious Synovitis in Chickens More Frequently than Does the Hemagglutination-Negative Phenotype

Cited by 41 publications

References 31 publications

Effect of MALP-2, a Lipopeptide from Mycoplasma fermentans , on Bone Resorption In Vitro

Effect of MALP-2, a Lipopeptide from Mycoplasma fermentans , on Bone Resorption In Vitro

The characterization ofMycoplasma synoviaeEF-Tu protein and proteins involved in hemadherence and their N-terminal amino acid sequences

Mycoplasmosis

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