A 48-kilodalton Mycoplasma fermentans membrane protein induces cytokine secretion by human monocytes.

AUTOR(ES)

Kostyal, D A

RESUMO

Mycoplasma fermentans is one of several Mycoplasma species that have been reported to stimulate tumor necrosis factor (TNF) secretion from monocytes. This activity has been associated primarily with the mycoplasma membrane fraction. In this article, we have characterized a membrane protein that stimulates TNF and interleukin 1 beta secretion. The TNF-releasing activity partitioned into the Triton X-114 detergent phase, suggesting that the molecules is hydrophobic. The secretion of TNF is elevated in the presence of serum, which suggests that a serum component may play a role in the interaction between this mycoplasma protein and monocytes. Treatment of monocytes with monoclonal anti-CD14 antibody had no effect on the levels of TNF-releasing activity. By using the monocyte Western blot (immunoblot) technique, we have determined the molecular mass of the active molecule to be 48 kDa. This molecule appears to be distinct from the recently described family of variable lipoproteins of M. fermentans. Mycoplasma particulate material treated with proteinase K lost all inducing activity, whereas lipoprotein lipase-treated samples retained some level of activity.

Documentos Relacionados

• Molecular characterization of a common 48-kilodalton outer membrane protein of Actinobacillus pleuropneumoniae.
• Mycoplasma fermentans-derived high-molecular-weight material induces interleukin-6 release in cultures of murine macrophages and human monocytes.
• Mycoplasma hyorhinis molecules that induce tumor necrosis factor alpha secretion by human monocytes.
• Purified capsular polysaccharide of Cryptococcus neoformans induces interleukin-10 secretion by human monocytes.
• Borrelia burgdorferi induces secretion of pro-urokinase-type plasminogen activator by human monocytes.