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Scabies mite inactivated serine protease paralogs inhibit the human complement system.

In English

Författare

  • Frida Mohlin
  • Simone Reynolds
  • Masego Johnstone
  • Robert N Pike
  • Ashley M Buckle
  • David J Kemp
  • Katja Fischer
  • Anna Blom

Summary, in English

Infestation of skin by the parasitic itch mite Sarcoptes scabiei afflicts 300 million people worldwide and there is a need for novel and efficient therapies. We have previously identified a multigene family of serine proteases comprising multiple catalytically inactive members (scabies mite-inactivated protease paralogs (SMIPPs)), which are secreted into the gut of S. scabiei. SMIPPs are located in the mite gut and in feces excreted into the upper epidermis. Scabies mites feed on epidermal protein, including host plasma; consequently, they are exposed to host defense mechanisms both internally and externally. We found that two recombinantly expressed SMIPPs inhibited all three pathways of the human complement system. Both SMIPPs exerted their inhibitory action due to binding of three molecules involved in the three different mechanisms which initiate complement: C1q, mannose-binding lectin, and properdin. Both SMIPPs bound to the stalk domains of C1q, possibly displacing or inhibiting C1r/C1s, which are associated with the same domain. Furthermore, we found that binding of both SMIPPs to properdin resulted in prevention of assembly of the alternative pathway convertases. However, the SMIPPs were not able to dissociate already formed convertases. Immunohistochemical staining demonstrated the presence of C1q in the gut of scabies mites in skin burrows. We propose that SMIPPs minimize complement-mediated gut damage and thus create a favorable environment for the scabies mites.

Publiceringsår

2009

Språk

Engelska

Sidor

7809-7817

Publikation/Tidskrift/Serie

Journal of immunology

Volym

182

Issue

12

Dokumenttyp

Artikel i tidskrift

Förlag

American Association of Immunologists

Ämne

  • Immunology in the medical area

Nyckelord

  • Serine Endopeptidases: isolation & purification
  • Serine Endopeptidases: genetics
  • Scabies: pathology
  • Scabies: immunology
  • Complement System Proteins: immunology
  • Sarcoptes scabiei: enzymology
  • Serine Endopeptidases: metabolism

Status

Published

Forskningsgrupp

  • Protein Chemistry, Malmö

ISBN/ISSN/Övrigt

  • ISSN: 1550-6606