Wolbachia surface protein (WSP) inhibits apoptosis in human neutrophils

• Published in: Parasite immunology Vol. 29; no. 2; pp. 73 - 79
• Main Authors: BAZZOCCHI, C, COMAZZI, S, SANTONI, R, BANDI, C, GENCHI, C, MORTARINO, M
• Format: Journal Article
• Language: English
• Published: Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.02.2007; Blackwell Publishing Ltd
• Subjects: Anaplasma; Animals; Annexin A5; apoptosis; Apoptosis - drug effects; Arthropoda; Bacterial Outer Membrane Proteins - pharmacology; Caspase 3 - metabolism; Ehrlichia; filariasis; Fluorescein-5-isothiocyanate; Humans; immunopathology; In Situ Nick-End Labeling; Interleukin-8 - metabolism; Nematoda; Nematoda - microbiology; Neutrophils - drug effects; Neutrophils - physiology; PMN; Wolbachia; Wolbachia - metabolism; Wolbachia surface protein
• ISSN: 0141-9838; 1365-3024
• DOI: 10.1111/j.1365-3024.2006.00915.x

Polymorphonuclear cells (PMNs) are essential for the innate immune response against invading bacteria. At the same time, modulation of PMNs' apoptosis or cell death by bacteria has emerged as a mechanism of pathogenesis. Wolbachia bacteria are Gram-negative endosymbionts of filarial nematodes and arthropods, phylogenetically related to the genera Anaplasma, Ehrlichia and Neorickettsia (family Anaplasmataceae). Although several pathogens are known to interfere with apoptosis, there is only limited information on specific proteins that modulate this phenomenon. This is the first evidence for the anti-apoptotic activity of a surface protein of Wolbachia from filarial nematode parasites (the Wolbachia surface protein, WSP). The inhibition of apoptosis was demonstrated on purified human PMNs in vitro by different methods. TUNEL assay showed that the percentage of dead cells was reduced after stimulation with WSP; Annexin V-FITC binding assay confirmed that cell death was due mainly to apoptosis and not to necrosis. Reduced caspase-3 activity in stimulated cells also confirmed an inhibition of the apoptotic process.