4. Discussion The present study describes the identification, expression, and immunological characterization of a member of the profilin family from three pathogenic Babesia species. The deduced amino acid sequence of PROFs from B. bigemina and B. microti is similar to those of other known apicomplexan parasites consisting of polypeptide binding and putative PIP2-interaction sites, profilin family domain, and GlcNAc glycosylation sites (Yarovinsky et al., 2005, 2006; Kursula et al., 2008; Kucera et al., 2010; Jenkins et al., 2010). A phylogenetic analysis revealed that PROF of Babesia species was clustered into a clade closely related to the PROF from other piroplasmids (identities 39.9e73.6% and similarities 55.9e80.5%), indicating that PROF of B. bovis, B. bigemina and B. microti possess a function similar to those of piroplasmids’PROF. The recombinant PROFs of B. bovis, B. bigemina, and B. microti were successfully produced as soluble GST fusion proteins, and they were found to cross-react. A high degree of homology may explain the serological cross-reactivity between the PROF proteins of B. bovis, B. bigemina, and B. microti. Another possible explanation is Babeisa PROF proteins share immunodominant epitopes and raises the possibility that such epitopes may be involved in a crossprotective immune response. Further, using anti-rPROFs mice sera, a native PROF proteins were observed in cytoplasm of the Babesia merozoites, suggesting that PROF proteins are shared antigens
rOmpA and rOmpA proteins are found across various strains of rickettsia rickettsii bacteria and play a role in pathogenesis through adhesion and invasion. It is noted that due to a premature stop codon, rOmpA is not produced in the avirulent strains of the rickettsia rickettsii bacteria and thus, it is thought that OmpA may play a role in virulence. This hypothesis was tested by inserting an isogenic ompA mutant – to create a premature stop codon – into a guinea pig infected with the highly virulent Shelia Smith strain. It was evident that this did not affect the duration or severity of illness versus the control guinea pig. From these findings it was concluded, and as the title of the article states, “the rickettsia rickettsii OmpA surface antigen does not diminish virulence in a mammalian model
Y. pestis has multiple virulence factors which is activated upon entering into the mammalian host (resulting in a change of temperature from lower temperature to around 37°C). For invasion, it has a protease called the plasminogen activator (Pla) that breaks down fibrin. This allows it to spread systemically from the original inoculation site (area of flea bite). This bacterium also has a hemin storage system, which enables it to survive in phagocytic cells and enhances uptake into eukaryotic (host’s) cells. Y. pestis also encode a type 3 secretion system (T3SS), which is a secretion system made up of macromolecular structures that lines the inner and outer membranes of the bacteria. It enables the direct translocation, from bacterial cytosol into host cells, of
The newly formed ookinete survives in the harsh protease rich environment of the midgut due to protease resistant covering (Gass and Yeates, 1979). Carter and Kumar (1985) observed that ookinete surface proteins are responsible for protecting ookinetes from protease enzymes attack (Carter et al., 1988). These and other parasite surface proteins are also candidates for an antizygote-ookinete transmission-blocking
Yersinia is a gram-negative bacteria causing plague pandemics in humans. They are facultative intracellular organisms that can very efficiently survive and replicate inside cells (1). They cause fatal plague and have destroyed millions of lives since 541 A.D (2). This review will highlight how these organisms subvert the immune system. It will elaborate on all the mechanisms and proteins utilized for the same. The main are the Yops or Yersinia outer proteins. But, there are other factors as
2004b), B. caballi (Bork et al., 2004b), and T. equi (U.S. Department of Agriculture) (AbouLaila et al., 2010b). Parasites were cultured in bovine or equine red blood cells by means of a continuous micro-aerophilous stationary phase culture system (AbouLaila et al., 2010b). The culture medium, M199, applied to B. bovis, B.bigemina, and T. equi (acquired from Sigma-Aldrich, Tokyo, Japan), was supplemented with 40 % bovine or equine serum and 60 U/ml of penicillin G, 60 μg/ml of streptomycin, and 0.15 μg/ml of amphotericin B (Sigma-Aldrich). TEShemisodium salt (229 mg/ml) N-tris- (hydroxymethyl)-methyl-2-aminoethansulfonic acid, 2-[(2-hydroxy-1,1-bis-
The article “The Beta Gamma subunits of GTP-binding proteins activate the muscarinic K+ channels in heart”, is a study that explores the role that G-protein subunits have on the activation of muscarinic-gated potassium (K+) channels (Mk channels). The article stated that essentially G-proteins are heterotrimers composed of alpha, beta, and gamma subunits. The alpha component of G proteins does not have a role in the activation of the Mk channels but it plays a role in the specificity and diversity of different effectors. This means that the beta-gamma subunits are solely responsible for the activation of K+ channels. The neurotransmitter Acetylcholine (ACh), binds to the muscarinic ACh receptor which affects the K+ current of the pacemaker and atrial cells. This background information poses the primary question of how the mAChR (ACh receptors) is coupled to the K+ channels and what are the G-proteins’ specific role in the interaction of the neurotransmitter ACh and the K+ channels.
Protist predators come in different forms one of them is called a parasite, it derives nutrition from its host. These parasite feed of from the host in order for it to survive (Mader 2010) Also, these parasites cause disease and sickness. There are three key forms of parasites which may stimulate disease in humans: protozoa, helminths, and ectoparasites. (CDC). types of parasites around the world, but for this essay will compare two parasites which are Toxoplasma gondii genus (is a type of roundworm) and Enterobius vermicularis. E.vermicular is a parasitic disease triggered by pinworm to humans. While T.gondii is a protozoan parasite which causes a disease identified as toxoplasmosis and this parasite affects warm blooded animals (Holm G, Roth E 2016), T.gondii is found in the faeces of cats and undercooked meals, lamb and pork as well, this parasite is transmitted through the partaking of the contaminated water meaning that it is easy to get this parasite in areas were water is fetched from the rivers. The Enterobius vermicularis is found to be under the domain of eukarya, the
Immunoelectron microscopy has shown that PI3P also localizes on the parasite apicoplast and the food vacuole6. During the asexual blood stage, the Plasmodium endocytoses hemoglobin (the major cytosolic constituent of red blood cells) and digests it within the food vacuole. This key catabolic process is largely attenuated in the presence of kinase inhibitors that block PI3P biosynthesis14. Further investigation into a PI3P-binding protein called FCP in P. falciparum reveals a similar phenotype (a stunted parasite size and defect in hemoglobin digestion) if its PI3P-binding domain is deleted15. Again, this finding demonstrates the importance of deciphering PI3P effector proteins in P. falciparum. These PI3P-regulated functions identified in the
F. verticillioides was first discovered in 1904 in Nebraska (USA). In 1935 Wollenweber and Reinking established the section Liseola based on the morphology of F. monoliforme Sheldon, F. lactis Pirotta and Riboni and F. neoceras Wollenw. and Reinking (Kvas et al., 2009). In 1945, Snyder and Hansen combined the three species under the name F. moniliforme as they felt that the characters Wollenweber and Reinking used were too unstable to separate the species (Snyder and Hansen, 1945; Kvas et al., 2009). Booth (1971) decided to separate F. subglutinans from F. moniliforme based on the morphology of their conidiogenous cells (Booth, 1971; Kvas et al., 2009). Nelson et al. (1983) divided Liseola further into F. anthophilum, F. proliferatum with the two that was already separated, F. moniliforme and F. subglutinans (Nelson et al., 1983; Kvas et al., 2009). After this split molecular, morphological and biological traits were used on a variety of Fusarium species and thus the Gibberella fujikuroi complex was established (Figure 2) (Kvas et al., 2009). F. verticillioides was one of the species that got separated from F. moniliforme during this time because it is heterothallic (Guo et al., 2015). Before 2013, F.
contains the necessary amino acids required for the parasite to live as well as replicate
Methods: Here we describe a protocol for the clumping assay using parasite line IT/C10 that gave consistent clumping assay results.
The research article results shows that A. tabida, has become dependent on W. pipientis to reproduce. W. pipientis affects the wasps oogenesis, but the specific mechanism responsible is yet unknown. Pannebakker et al. (2007) research shows the W. pipientis influences programmed cell death processes in A. tabida by making its presence essential for the wasps eggs to fully mature. In conclusion, this study suggests the bacterium’s strategy causes the host to be dependent through evolution, thus creating a quick transitioning phase from commensalism (parasitism) to mutualism, where both organisms benefit.
Pannebakker et al. (2007) wanted to closely understand the symbiotic relationship between Asobara tabida, a wasp, and Wolbachia. To conduct this study, they first understood that A. tabida is naturally infected by three strains of Wolbachia. The research team decided to infect A. tabida with just the wAtab3
The PI(3)P binding of the three selected candidate proteins (PfRan, PfAlba1 and PfHsp70-1) has been validated using a protein lipid overlay assay. To further profile the lipid-binding specificity, I utilized a membrane spotted with 15 different lipids and demonstrated that the selected proteins preferentially bound to PI(3,5)P2 and phosphatidylinositol monophosphates (e.g., PI(3)P) in vitro. Given that PI(5)P and PI(3,5)P2 were not found in P. falciparum, this finding may reveal a spatiotemporal regulation by PI(3)P and/or PI(4)P in vivo. The following competitive assays showed that both PI(3)P and ATP can compete out PI(3)P-bound PfHsp70-1 when compared to the control ligand phosphatidylinositol (PI). Further investigation into the PI(3)P binding specificity is needed before ruling out the possibility that PI(3)P may nonspecifically bind to the nucleotide-binding domains of the identified proteins.
Deliberated as one of the most dangerous parasites of the Plasmodium species, P. falciparum accounts for at least 75% of all malarial deaths each year (WHO, 2008). According to Hanspal, et al. (2002), P. falciparum has become resistant to antimalarial drugs; therefore the need to develop new approaches has become ubiquitous. Protein affiliations are responsible for not only invasion, but also the creation of a domicile type structure within a host cell which increases the probabilities of infection. By determining these factors, probable correlations to new vaccines or treatments can be drawn.