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Inflammatory Lipoproteins Purified from a Toxigenic and Arthritogenic Strain of Mycoplasma arthritidis Are Dependent on Toll-Like Receptor 2 and CD14

Division of Rheumatology, Department of Internal Medicine, University of Utah School of Medicine, Salt Lake City, Utah 84132,¹ Division of Basic Biomedical Sciences, Sanford School of Medicine, University of South Dakota, Vermillion, South Dakota 57069²

Received 29 March 2006/ Returned for modification 29 May 2006/ Accepted 23 January 2007

Mycoplasma arthritidis is a naturally occurring murine pathogen, and the disease model has been used extensively to understand inflammatory mechanisms. Recently, Triton X-114 extracts of a virulent strain of M. arthritidis were found to be more potent in activating macrophages than were those from an avirulent strain, suggesting a role in disease. Here, octyl glucoside extraction of cells was used to identify four distinct bioactive moieties, with molecular masses of 41, 37, 34, and 17 kDa. Their bioactivities were resistant to proteinase K but were destroyed by alkaline hydrolysis and oxidation. As for MALP-2, all were dependent upon Toll-like receptor 2, but unlike MALP-2, they were also dependent upon CD14. The M. arthritidis lipoproteins exhibited infrared absorbances at 2,900 cm^–1 and 1,662 cm^–1, similar to those seen in Pam₃-Cys-Ser-(Lys)₄. Edman degradation failed to reveal N-terminal sequences, suggesting that they were blocked and therefore might be triacylated. However, mass spectrometry of fragments revealed that the 41-kDa moiety, which binds to serum apolipoprotein A-1, had similarity with the recently described MlpD lipoprotein of M. arthritidis.

Published ahead of print on 5 February 2007.

Editor: J. L. Flynn