Trypanosoma carassii calreticulin binds host complement component C1q and inhibits classical complement pathway-mediated lysis

Oladiran, Ayoola; Belosevic, Miodrag

doi:10.1016/j.dci.2009.11.005

Cited by 37 publications

(26 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Goldfish CRP contains a pentraxin (PTX) domain, which has been reported to recognize PAMPs such phosophorylcholine that is present on the surface of parasites. Binding of CRP to these parasites moieties apparently confers anti-parasitic properties, however the mechanism(s) are unclear (Oladiran and Belosevic, 2010;Suchitra et al, 2008). In addition to its anti-parasitic properties, CRP acts as a pro-coagulant that may hinder the ability of the extracellular parasite to establish and proliferate in the host (Singh et al, 2005;Suchitra et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

“…Although CRP mRNA and protein levels were up-regulated upon parasite challenge, parasites have evolved mechanisms to evade complement-mediated lysis. For example, T. carassii secretes calreticulin which can effectively bind to C1q and inhibit the activation of the classical complement pathway (Oladiran and Belosevic, 2010), allowing the parasite to establish and proliferate in the host. Fig.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

The analysis of the acute phase response during the course of Trypanosoma carassii infection in the goldfish ( Carassius auratus L.)

Hagen

Xie

Belosevic

2015

Developmental & Comparative Immunology

Self Cite

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The analysis of the acute phase response during the course of Trypanosoma carassii infection in the goldfish ( Carassius auratus L.)

Hagen

Xie

Belosevic

2015

Developmental & Comparative Immunology

Self Cite

View full text Add to dashboard Cite

“…CRT from diverse origins binds C1, interfering with the function of this molecule. [21][22][23][24][25] By Western Blot, we showed that rTiS also binds C1, as detected by an anti-C1 antibody (Figures 5A and Supplemental Figure 1).…”

Section: Resultsmentioning

confidence: 99%

“…CRT binds to C1, as shown for HuCRT 21 and CRTs from Necator americanus, 22 Haemonchus contortus, 23 Trypanosoma carasii, 24 T. cruzi, 25 Entamoeba histolytica, and Entamoeba dispar. 32 Resulting inhibition of the classical pathway of the complement system is detectable.…”

Section: Discussionmentioning

confidence: 99%

Triatoma infestans Calreticulin: Gene Cloning and Expression of a Main Domain That Interacts with the Host Complement System

Weinberger

Collazo

Aguillón

et al. 2017

The American Society of Tropical Medicine and Hygiene

View full text Add to dashboard Cite

Abstract. Triatoma infestans is an important hematophagous vector of Chagas disease, a neglected chronic illness affecting approximately 6 million people in Latin America. Hematophagous insects possess several molecules in their saliva that counteract host defensive responses. Calreticulin (CRT), a multifunctional protein secreted in saliva, contributes to the feeding process in some insects. Human CRT (HuCRT) and Trypanosoma cruzi CRT (TcCRT) inhibit the classical pathway of complement activation, mainly by interacting through their central S domain with complement component C1. In previous studies, we have detected CRT in salivary gland extracts from T. infestans. We have called this molecule TiCRT. Given that the S domain is responsible for C1 binding, we have tested its role in the classical pathway of complement activation in vertebrate blood. We have cloned and characterized the complete nucleotide sequence of CRT from T. infestans, and expressed its S domain. As expected, this S domain binds to human C1 and, as a consequence, it inhibits the classical pathway of complement, at its earliest stage of activation, namely the generation of C4b. Possibly, the presence of TiCRT in the salivary gland represents an evolutionary adaptation in hematophagous insects to control a potential activation of complement proteins, present in the massive blood meal that they ingest, with deleterious consequences at least on the anterior digestive tract of these insects.

show abstract

“…T. cruzi and T. carassii CRT ( Tc CRT) bind human or fish C1q, respectively, and specifically inhibit the classical complement pathway. This suggests an evolutive conserved interaction between CRT and C1q [14, 15]. …”

Section: Introductionmentioning

confidence: 99%

Entamoeba histolyticaandE. disparCalreticulin: Inhibition of Classical Complement Pathway and Differences in the Level of Expression in Amoebic Liver Abscess

Ximénez

González

Nieves

et al. 2014

BioMed Research International

View full text Add to dashboard Cite

The role of calreticulin (CRT) in host-parasite interactions has recently become an important area of research. Information about the functions of calreticulin and its relevance to the physiology of Entamoeba parasites is limited. The present work demonstrates that CRT of both pathogenic E. histolytica and nonpathogenic E. dispar species specifically interacted with human C1q inhibiting the activation of the classical complement pathway. Using recombinant EhCRT protein, we demonstrate that CRT interaction site and human C1q is located at the N-terminal region of EhCRT. The immunofluorescence and confocal microscopy experiments show that CRT and human C1q colocalize in the cytoplasmic vesicles and near to the surface membrane of previously permeabilized trophozoites or are incubated with normal human serum which is known to destroy trophozoites. In the presence of peripheral mononuclear blood cells, the distribution of EhCRT and C1q is clearly over the surface membrane of trophozoites. Nevertheless, the level of expression of CRT in situ in lesions of amoebic liver abscess (ALA) in the hamster model is different in both Entamoeba species; this molecule is expressed in higher levels in E. histolytica than in E. dispar. This result suggests that EhCRT may modulate some functions during the early moments of the host-parasite relationship.

show abstract

Trypanosoma carassii calreticulin binds host complement component C1q and inhibits classical complement pathway-mediated lysis

Cited by 37 publications

References 41 publications

The analysis of the acute phase response during the course of Trypanosoma carassii infection in the goldfish ( Carassius auratus L.)

The analysis of the acute phase response during the course of Trypanosoma carassii infection in the goldfish ( Carassius auratus L.)

Triatoma infestans Calreticulin: Gene Cloning and Expression of a Main Domain That Interacts with the Host Complement System

Entamoeba histolyticaandE. disparCalreticulin: Inhibition of Classical Complement Pathway and Differences in the Level of Expression in Amoebic Liver Abscess

Contact Info

Product

Resources

About