Display Settings:

Format

Send to:

Choose Destination
Mol Biochem Parasitol. 2009 Jul;166(1):42-6. doi: 10.1016/j.molbiopara.2009.02.007. Epub 2009 Feb 24.

Mapping the complement C1q binding site in Haemonchus contortus calreticulin.

Author information

  • 1Division of Biochemistry, Indian Veterinary Research Institute, Izatnagar, UP, India.

Abstract

Haemonchus contortus is an economically important gastrointestinal parasite of domestic animals. The parasite secretes calreticulin (CalR), a Ca(++) binding protein which modulates the host immune response. One way by which this protein acts is by inhibiting the classical complement pathway by binding to complement C1q protein. Understanding CalR-C1q interaction is important to develop methods to enhance host immune response. In this study, we have mapped the regions in the N-domain of CalR that facilitates C1q binding by generating small recombinant fragments of the domain and using synthetic peptides. In addition to already identified C1q binding motifs in human CalR, two additional sites in the N-domain of H. contortus were revealed with the following sequences-GKYYDDAKRD and the AKFPKKFT. The significance of multiple C1q binding motifs in CalR is discussed in relation to host-parasite interactions.

PMID:
19428671
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk