A novel mechanism of complement inhibition unmasked by a tick salivary protein that binds to properdin.

A novel mechanism of complement inhibition unmasked by a tick salivary protein that binds to properdin. Research Abstract Details 

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A novel mechanism of complement inhibition unmasked by a tick salivary protein that binds to properdin. Abstract Text:

Ixodes scapularis salivary protein 20 (Salp20) is a member of the Ixodes scapularis anti-complement protein-like family of tick salivary proteins that inhibit the alternative complement pathway. In this study, we demonstrate that the target of Salp20 is properdin. Properdin is a natural, positive regulator of the alternative pathway that binds to the C3 convertase, stabilizing the molecule. Salp20 directly bound to and displaced properdin from the C3 convertase. Displacement of properdin accelerated the decay of the C3 convertase, leading to inhibition of the alternative pathway. S20NS is distinct from known decay accelerating factors, such as decay accelerating factor, complement receptor 1, and factor H, which directly interact with either C3b or cleaved factor B.

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A novel mechanism of complement inhibition unmasked by a tick salivary protein that binds to properdin. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of immunology (Baltimore, Md. : 1950)

VOLUME: 180

Page Numbers: 3964-8

Journal Abbreviation: J. Immunol.

ISSN: 0022-1767

DAY: 15

MONTH: Mar

YEAR: 2008

A novel mechanism of complement inhibition unmasked by a tick salivary protein that binds to properdin. Information

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LANGUAGE: eng

NlmUniqueID: 2985117

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Grant and Affiliation Information for A novel mechanism of complement inhibition unmasked by a tick salivary protein that binds to properdin.

AFFILIATION: Department of Microbiology and Immunology and.

Country: United States

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MEDLINETA: J Immunol

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