scholarly journals THE EFFECT OF PLASMODIUM FLORIDENSE ON RELATIVE LEUKOCYTE COUNTS OF ANOLIS SAGREI AND A. CAROLINENSIS IN FLORIDA, USA

2020 ◽  
pp. 42-48
Author(s):  
Lara B. Bessa ◽  
Nicole M. Ely ◽  
Erika K. Calle ◽  
Benjamin J. Lafond ◽  
Ryan P. Counsman ◽  
...  
Keyword(s):  
Malarial Parasite ◽  
Infection Status ◽  
Plasmodium Infection ◽  
Anolis Sagrei ◽  
Central Florida ◽  
Southwest Florida ◽  
Parasite Plasmodium ◽  
Immunological Effects ◽  
Protozoal Infection ◽  
Eosinophil Counts

Native Green Anoles, Anolis carolinensis, and invasive Brown Anoles, Anolis sagrei, are commonly found in Florida and may be infected with the malarial parasite, Plasmodium floridense. Because no studies have directly addressed health effects of the parasite on Florida anoles, we collected blood smears of infected and uninfected anoles from Central and Southwest Florida and compared the overall leukocyte (WBC) counts, eosinophil counts, and heterophil/lymphocyte ratios. Eosinophils are generally elevated in response to protozoal infection and heterophil/lymphocyte ratios are often altered due to stress. A generalized linear model that tested contributions to erythrocyte/leukocyte ratios included infection status and locality as significant factors. We found significant differences in WBC counts between infected and uninfected lizards in Central Florida but not in Southwest Florida. Central Florida anoles also had higher mean WBC counts than Southwest Florida anoles. We did not detect significant differences in eosinophil counts or H/L ratios related to infection status. Our project is the first to examine leukocyte effects of Plasmodium infection in anoles and to provide leukocyte profiles of Anolis lizards. It appears that infected anoles sustain some negative immunological effects, at least in Central Florida. The differences in regions may be caused by the fact that Central Florida anoles still are under continuous interspecific competition whereas the Southwest Florida Brown Anoles are not because of low populations of Green Anoles. Additional studies that address leukocyte levels related to Plasmodium infection are needed to tease out the health and fitness effects on the lizards of Florida.

scholarly journals Sequence identification of cytochrome b in Plasmodium gallinaceum.

1989 ◽  
Vol 9 (9) ◽  
pp. 3614-3620 ◽  
Author(s):  
S M Aldritt ◽  
J T Joseph ◽  
D F Wirth
Keyword(s):  
Cytochrome B ◽  
Open Reading Frame ◽  
Malarial Parasite ◽  
Plasmodium Gallinaceum ◽  
Primary Transcript ◽  
Present Evidence ◽  
Reading Frame ◽  
Sequence Identification ◽  
Parasite Plasmodium ◽  
Extrachromosomal Element

We have identified a gene that encodes the polypeptide cytochrome b in the avian malarial parasite Plasmodium gallinaceum. The gene containing the open reading frame was found to be located on a 6.2-kilobase multimeric extrachromosomal element. The amino acid translation from this gene demonstrated significant similarities to cytochrome b sequences from yeast, mammal, and fungus genomes. We present evidence that the P. gallinaceum cytochrome b transcript is part of a larger primary transcript from the element that is subsequently processed. The message for P. gallinaceum cytochrome b was found to be 1.2 kilobases in size. This is the first report identifying a mitochondrial nucleic acid sequence in malaria-causing organisms and suggests that a functional cytochrome system may exist in these parasites.

scholarly journals Localization of ferrochelatase in Plasmodium falciparum

2004 ◽  
Vol 384 (2) ◽  
pp. 429-436 ◽  
Author(s):  
Sundaramurthy VARADHARAJAN ◽  
B. K. Chandrashekar SAGAR ◽  
Pundi N. RANGARAJAN ◽  
Govindarajan PADMANABAN
Keyword(s):  
Plasmodium Falciparum ◽  
De Novo ◽  
Enzymic Activity ◽  
Malarial Parasite ◽  
Parasite Genome ◽  
Marker Proteins ◽  
Parasite Plasmodium ◽  
Theoretical Predictions ◽  
Parasite Plasmodium Falciparum

Our previous studies have demonstrated de novo haem biosynthesis in the malarial parasite (Plasmodium falciparum and P. berghei). It has also been shown that the first enzyme of the pathway is the parasite genome-coded ALA (δ-aminolaevulinate) synthase localized in the parasite mitochondrion, whereas the second enzyme, ALAD (ALA dehydratase), is accounted for by two species: one species imported from the host red blood cell into the parasite cytosol and another parasite genome-coded species in the apicoplast. In the present study, specific antibodies have been raised to PfFC (parasite genome-coded ferrochelatase), the terminal enzyme of the haem-biosynthetic pathway, using recombinant truncated protein. With the use of these antibodies as well as those against the hFC (host red cell ferrochelatase) and other marker proteins, immunofluorescence studies were performed. The results reveal that P. falciparum in culture manifests a broad distribution of hFC and a localized distribution of PfFC in the parasite. However, PfFC is not localized to the parasite mitochondrion. Immunoelectron-microscopy studies reveal that PfFC is indeed localized to the apicoplast, whereas hFC is distributed in the parasite cytoplasm. These results on the localization of PfFC are unexpected and are at variance with theoretical predictions based on leader sequence analysis. Biochemical studies using the parasite cytosolic and organellar fractions reveal that the cytosol containing hFC accounts for 80% of FC enzymic activity, whereas the organellar fraction containing PfFC accounts for the remaining 20%. Interestingly, both the isolated cytosolic and organellar fractions are capable of independent haem synthesis in vitro from [4-14C]ALA, with the cytosol being three times more efficient compared with the organellar fraction. With [2-14C]glycine, most of the haem is synthesized in the organellar fraction. Thus haem is synthesized in two independent compartments: in the cytosol, using the imported host enzymes, and in the organellar fractions, using the parasite genome-coded enzymes.

scholarly journals NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35

2010 ◽  
Vol 19 (8) ◽  
pp. 1577-1586 ◽  
Author(s):  
Reema Alag ◽  
Insaf A. Qureshi ◽  
Nagakumar Bharatham ◽  
Joon Shin ◽  
Julien Lescar ◽  
...  
Keyword(s):  
Plasmodium Vivax ◽  
Binding Domain ◽  
Malarial Parasite ◽  
Parasite Plasmodium ◽  
Crystallographic Structures

Nuclear and mitochondrial DNA of the primate malarial parasite Plasmodium knowlesi

1985 ◽  
Vol 14 (2) ◽  
pp. 199-209 ◽  
Author(s):  
Donald H. Williamson ◽  
Robert J.M. Wilson ◽  
Paul A. Bates ◽  
Shirley McCready ◽  
Francine Perler ◽  
...  
Keyword(s):  
Mitochondrial Dna ◽  
Plasmodium Knowlesi ◽  
Malarial Parasite ◽  
Parasite Plasmodium

scholarly journals Molecular cloning, characterization and localization of PfPK4, an eIF-2α kinase-related enzyme from the malarial parasite Plasmodium falciparum

1997 ◽  
Vol 328 (2) ◽  
pp. 677-687 ◽  
Author(s):  
Jörg J. MÖHRLE ◽  
Yi ZHAO ◽  
Barbara WERNLI ◽  
M. Richard FRANKLIN ◽  
Barbara KAPPES
Keyword(s):  
Amino Acids ◽  
Plasmodium Falciparum ◽  
Protein Kinase ◽  
Protein Kinases ◽  
Initiation Factor ◽  
Malarial Parasite ◽  
Kinase Gene ◽  
Western Blots ◽  
Parasite Plasmodium ◽  
Parasite Plasmodium Falciparum

PfPK4, a protein kinase gene from the human malarial parasite Plasmodium falciparum, has been cloned utilizing oligonucleotide probing. The gene encodes a protein of a predicted length of 1123 amino acids, and within this amino acid sequence all the conserved regions characteristic of protein kinases can be identified. The catalytic kinase domain possesses highest identities (34-37%) with eukaryotic initiation factor-2α (eIF-2α) kinases, especially haem-regulated inhibitory (HRI) protein kinases. There are two kinase inserts in PfPK4, located at positions common to eIF-2α kinases. The first insert separates kinase subdomains IV and VI by 559 amino acids, and the second subdomains VII and VIII by 41 amino acids. Both inserts are larger than their homologues in eIF-2α kinases. The sequence of PfPK4 has one putative haemin-binding site. The recombinant protein, expressed in Escherichia coli, phosphorylates a synthetic peptide representing a substrate of eIF-2α kinases. Autophosphorylation and substrate phosphorylation are inhibited by haemin. Thus PfPK4 appears to be the first protozoan protein kinase related to eIF-2α kinases and might be the first non-mammalian HRI kinase. Western blots indicated that the protein is expressed as major forms of 80 and 90 kDa. Whereas the 80 kDa form is present throughout the intraerythrocytic development and in merozoites, the two 90 kDa forms are only found in mature parasites. One of the latter is also present in the membrane fraction of erythrocytes harbouring segmenters. Confocal microscopy detected the protein distributed throughout the trophozoite, whereas it was found in discrete foci (punctate distribution) in segmenters. PfPK4 co-localizes with P. falciparum 83 kDa antigen/apical membrane antigen-1 at the apical complex in segmenters and merozoites, but does not co-localize with rhoptry-associated protein-1.

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