Characterization of a lympho-inhibitory peptide produced by Mycoplasma bovis

• Published in: Biochemical and biophysical research communications Vol. 315; no. 2; pp. 336 - 341
• Main Authors: Bush, Tony J.Vanden, Rosenbusch, Ricardo F
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 05-03-2004
• Subjects: Amino Acid Sequence; Animals; Antigens, Bacterial; Bacterial Outer Membrane Proteins - chemistry; Blotting, Western; Cattle; Cell Division; Cell Membrane - metabolism; Cells, Cultured; Chromatography; Concanavalin A - chemistry; Glutathione Transferase - metabolism; Immunosuppression; Immunosuppressive Agents - chemistry; Lymphocyte; Lymphocytes - metabolism; Lymphocytes - microbiology; Molecular Sequence Data; Mycoplasma bovis; Mycoplasma bovis - metabolism; Ninhydrin - chemistry; PBMC; Peptide; Peptides - chemistry; Protein Structure, Tertiary; Recombinant Proteins - chemistry; Silicon - chemistry; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Immunosuppression; Mycoplasma bovis; Lymphocyte; Peptide; PBMC
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2004.01.063

Mycoplasma bovis is able to inhibit the mitogen-induced proliferation of bovine lymphocytes. Herein is described the isolation of an immuno-inhibitory peptide from
M. bovis. Using size exclusion chromatography, three lympho-suppressive fractions were isolated from
M. bovis free supernatant. MALDI-TOF analysis revealed a common peak throughout the suppressive fractions. The purest of these fractions was subjected to N-terminal sequencing, revealing an 84% homologous match with the C-terminus of the
M. bovis surface protein VspL (variable surface protein—L). A recombinant of the 26 amino acid peptide was also able to suppress Concanavalin A (ConA)-induced proliferation of bovine lymphocytes. This describes a unique immunosuppressive peptide produced by the bovine respiratory pathogen,
M. bovis.