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Echinococcus multilocularis Calreticulin Interferes with C1q-Mediated Complement Activation.

Siqi Xian¹, Lujuan Chen¹, Yan Yan¹

¹Department of Pathogenic Biology, School of Basic Medical Sciences and Forensic Medicine, Baotou Medical College, Baotou 014040, China.

Tropical Medicine and Infectious Disease

|January 20, 2023

Summary

Echinococcus multilocularis uses calreticulin (EmCRT) to evade host immunity by blocking complement activation. This parasitic protein interferes with immune cell responses, aiding parasite survival.

Keywords:

Echinococcus multilocularis calreticulin classical complement activation complement C1q immune evasion mast cell

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Area of Science:

Immunology
Parasitology
Molecular Biology

Background:

Alveolar echinococcosis (AE) is a severe zoonotic disease caused by Echinococcus multilocularis.
E. multilocularis employs complex immune evasion strategies, but the mechanisms are not fully understood.

Purpose of the Study:

To investigate the interaction between E. multilocularis calreticulin (EmCRT) and human complement C1q.
To determine EmCRT's role in inhibiting classical complement activation and C1q-mediated immune cell responses.

Main Methods:

ELISA, Far Western blotting, and immunoprecipitation were used to assess EmCRT-C1q binding.
The effect of recombinant EmCRT (rEmCRT) on C1q binding to IgM and complement activation (C4/C3 deposition, cell lysis) was measured.
rEmCRT's impact on C1q binding to human mast cells (HMC-1) and subsequent chemotaxis was evaluated.

Main Results:

Both natural and recombinant EmCRT bound to human C1q.
rEmCRT inhibited C1q binding to IgM, suppressing classical complement activation and reducing C4/C3 deposition and cell lysis.
rEmCRT binding to C1q reduced C1q-induced mast cell chemotaxis.

Conclusions:

E. multilocularis expresses EmCRT, which binds to C1q.
EmCRT interferes with both complement-dependent and complement-independent immune functions mediated by C1q.
EmCRT likely serves as a crucial immune evasion mechanism for E. multilocularis survival within the host.