Apicomplexan perforin-like proteins

Kafsack, Björn F.C.; Carruthers, Vern B.

doi:10.4161/cib.3.1.9794

Cited by 39 publications

(41 citation statements)

References 40 publications

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“…Precise Generation of plp1ko Domain Deletion Complementation Strains-Whereas PLP1 has a highly conserved MACPF domain, the N-and C-terminal domains flanking it are unique (7,34). We hypothesized the MACPF domain to be required for oligomerization and membrane permeabilization.…”

Section: Loss Of Plp1 Leads To a Secondary Invasionmentioning

confidence: 99%

“…The PLP1 N-terminal domain sequence contains no conserved domains and is found only in Toxoplasma and the related Neospora sequences. It may be more distantly related to the N-terminal extensions seen on some of the Plasmodium MACPF proteins (34). N-terminal domains in other MACPF proteins include a low density lipoprotein receptor A domain and thrombospondin type I domains in several complement proteins (35,36).…”

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confidence: 99%

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Functional Dissection of Toxoplasma gondii Perforin-like Protein 1 Reveals a Dual Domain Mode of Membrane Binding for Cytolysis and Parasite Egress

Roiko

Carruthers

2013

Journal of Biological Chemistry

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Background: Toxoplasma gondii requires a perforin-like protein (PLP1) for rapid host cell egress. Results: Loss of the PLP1 N-terminal domain reduced parasite egress and lytic activity, but not virulence. Conclusion: PLP1 has a unique accessory N-terminal domain, which binds membranes and promotes rapid egress. Significance: Understanding the role of accessory domains is critical for defining the activity of pore-forming proteins.

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Section: Loss Of Plp1 Leads To a Secondary Invasionmentioning

confidence: 99%

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confidence: 99%

Functional Dissection of Toxoplasma gondii Perforin-like Protein 1 Reveals a Dual Domain Mode of Membrane Binding for Cytolysis and Parasite Egress

Roiko

Carruthers

2013

Journal of Biological Chemistry

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“…Our results demonstrate that the rBoSA1 produced in E. coli is a monomeric protein and forms oligomers under physiological conditions. A recent study indicated that a family of membrane attack complex/perforin (MACPF) domain proteins of Babesia bovis are expressed and oligomerized to form large prepore complexes on the surfaces of target cells (32), and a dissertation showed that heat shock protein 20 (HSP20) of Babesia bovis can exist as an oligomer (33). Further studies with a large number of infected blood samples are required to determine whether native BoSA1 exists in monomeric, dimeric, and tetrameric forms in vivo.…”

Section: Discussionmentioning

confidence: 99%

Identification and Expression of Babesia ovis Secreted Antigen 1 and Evaluation of Its Diagnostic Potential in an Enzyme-Linked Immunosorbent Assay

Sevinç

Cao

et al. 2015

J Clin Microbiol

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bIn order to identify immunoreactive proteins that are usable for the immunological diagnosis of Babesia ovis infections, a phage lambda cDNA expression library was constructed and screened using parasite-specific immune serum. Immunoscreening resulted in the identification of a full-length cDNA clone encoding a secreted protein designated Babesia ovis secreted antigen 1 (BoSA1). The full-length BoSA1 cDNA contained a 1,137-bp open reading frame that encoded a protein of 378 amino acids, with a signal peptide and 2 internal repeat domains. The theoretical molecular mass of the mature protein was 42.5 kDa. Recombinant BoSA1 (rBoSA1) protein was expressed in Escherichia coli strain DH5␣ cells as a glutathione S-transferase (GST) fusion protein and was purified by affinity chromatography. Purified rBoSA1 was tested for reactivity with sera from animals experimentally or naturally infected with B. ovis, in an indirect enzyme-linked immunosorbent assay (ELISA). The results showed that specific antibodies against rBoSA1 were detectable on days 7 and 8 of the experimental infection and were maintained during the sampling period. Additionally, 38 field sera taken from sheep naturally infected with B. ovis gave strong positive reactions in the ELISA between day 20 and day 30 of treatment. As a result, the identified recombinant BoSA1 protein seems to be a promising diagnostic antigen that is usable for the development of serological assays for the diagnosis of ovine babesiosis. This is the first report on the molecular cloning, expression, and potential use of a recombinant antigen for the diagnosis of ovine babesiosis. O vine babesiosis, caused by the tick-borne intraerythrocytic apicomplexan parasite Babesia ovis, is an acute disease characterized by clinical signs such as fever, hemolytic anemia, hemoglobinuria, and icterus in small ruminants. The disease is endemic in European, African, Asian, and Far Eastern countries (1-8). Babesia ovis is highly pathogenic and, in serious infections, causes pancytopenia. Untreated cases usually result in the death of sick animals, and even some treated animals may die as a result of heavy infection. Many recurrences also occur after the treatment period. Compensation for the abnormalities in the hematological profiles of acutely infected animals takes a long time after the treatment period (8). Currently, control of ovine babesiosis is based only on chemotherapy and limited tick control measures. In areas in which the status of B. ovis endemicity is unstable, an immunization program is needed (9). However, immunoprophylaxis is lacking for Babesia species in sheep.Currently, the diagnosis of ovine babesiosis includes microscopic examination of Giemsa-stained thin blood smears. Although intraerythrocytic parasites are apparent in clinical cases, it is very difficult to detect the organisms by microscopy in chronic infections, because of the low levels of parasitemia (10-12). The analysis of blood smears usually depends on the experience of the observer. The morphological changes in ...

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“…This protein also contains WD-40 domain. Proteins with MAC/perforin domains (XP_001351401.1) in Plasmodium and Toxoplasma are proved to be essential for breaching membranes during parasite egress and cell traversal (Kafsack and Carruthers, 2010). Membrane skeletal protein IMC1 related (XP_001347324.1) have functional role affecting cell morphology, strength, motility and infectivity (Tremp and Dessens, 2011).…”

Section: Annotation Transfer By Homologymentioning

confidence: 99%

Annotation transfer by homology among closely related genomes helps to identify protein function in Plasmodium species

Devaraj

Chandramohan

2017

IJBRA

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Malaria is a major killer disease causing heavy loss in terms of life and medical expenditure. The genome of Plasmodium falciparum sequenced in 2002 but more than 60% of its meaning still remains unknown. We compared protein sequences from P. falciparum in the genomic sequences with P. vivax and P. knowlesi through standalone blast tool from NCBI. We found many proteins annotated in one species sharing high similarity with unannotated proteins in the other/s species. Based on the 'annotation transfer by homology' method we annotated 715 hypothetical proteins. By the latest information available as of 1st September our method annotated 343 protein sequences .Gene Ontology annotation with BLAST2GO revealed 128 proteins with Enzyme Codes among the 561 sequences mapped with GO terms. The kognitor results showed 542 proteins similar to proteins belonging to various KOG categories. More attention should be paid to these 'hypothetical' proteins as they can reveal unknown insights on the biology of organisms and have an impact in the field of drug discovery and medicine.

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Apicomplexan perforin-like proteins

Cited by 39 publications

References 40 publications

Functional Dissection of Toxoplasma gondii Perforin-like Protein 1 Reveals a Dual Domain Mode of Membrane Binding for Cytolysis and Parasite Egress

Functional Dissection of Toxoplasma gondii Perforin-like Protein 1 Reveals a Dual Domain Mode of Membrane Binding for Cytolysis and Parasite Egress

Identification and Expression of Babesia ovis Secreted Antigen 1 and Evaluation of Its Diagnostic Potential in an Enzyme-Linked Immunosorbent Assay

Annotation transfer by homology among closely related genomes helps to identify protein function in Plasmodium species

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