Biomedical Engineering Reference
In-Depth Information
complement system. Structural characterization of the same two SMIPP-Ss
elucidated the structural mechanism behind the family's inactivation and led to
the proposal of an alternative binding site mediating binding to the comple-
ment components. Identifying the binding sites for complement could lead to
the development of novel scabies therapeutics.
Comparing the anti-complement properties of the proteolytically inactive
SMIPP-Ss to a range of parasitic complement inhibitors and proteolytically
inactive protease paralogues indicates that while the existence of the SMIPP-Ss
is fascinating, similar strategies have been widely used by parasites.
Acknowledgment
This study was supported by Program Grant 496600, by fellowships to D. J.
Kemp from the Australian National Health and Medical Research Council and
an Australian Postgraduate Award to S. Reynolds, and by grants from the
Swedish Research Council and Swedish Foundation for Strategic Research.
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