Biomedical Engineering Reference
In-Depth Information
Analysis of the electrostatic and physical surface characteristics in the con-
text of the sequence diversity within the SMIPP family suggests that it is highly
unlikely that the observed features are general to the SMIPP family as a whole,
and indeed may represent specific adaptations important to the individual and
specialized roles of each SMIPP in the scabies mite lifecycle.
10.7 Conclusions
The structural, functional, and bioinformatic data suggest strongly that scabies
mites have adapted the protease fold to create a structurally and functionally
diverse family of molecules necessary for evading the multifaceted immune
system of the host. Taken together, these data suggest that SMIPPs have lost
the ability to bind substrates in a classical 'canonical' fashion, and instead have
evolved alternative functions in the lifecycle of the scabies mite.
Acknowledgments
A.M.B is a National Health and Medical Research Council of Australia Senior
Research Fellow. J.A.I is an NHMRC CJ Martin Postdoctoral Fellow. This
work was supported by the NHMRC, the Australian Research Council and the
State Government of Victoria (Australia). We thank Professor Mick Foley and
Dr Joanne Casey from La Trobe University, Melbourne for providing the
phage display peptide library and expert advice.
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