Genomic organisation and expression of a differentially-regulated gene family from Leishmania major

21  Mitchell  

The sequence and gene group of the ribosomal RNA (rRNA) genes of Leishmania main Friedlin (LmjF) had been decided. Apparently, the rDNA repeat unit contained a duplicated 526 bp fragment on the 3′ finish of the unit with two copies of the LSUepsilon rRNA gene.

 

Our outcomes steered the presence of solely roughly 24 copies of the rRNA unit per diploid genome in LmjF. Repetitive components (IGSRE) of 63 bp occurred within the intergenic spacer (IGS) between the LSUepsilon and the SSU rRNA genes. Among the many completely different rDNA models, the area containing the IGSRE fluctuated in size from roughly 1.Three to roughly 18 kb.

The transcription initiation website (TIS) of the rRNA unit was localized by primer extension to 1043 bp upstream of the SSU gene and 184 bp downstream of the IGSRE. Sequence comparability amongst a number of species of Leishmania confirmed a excessive diploma of conservation across the TIS. Furthermore, the IGSRE additionally confirmed appreciable similarity between Leishmania species.

In transient transfection assays, a fraction containing the TIS directed a 164- to 178-fold enhance in luciferase exercise over the no-insert management, indicating the presence of a promoter inside this 391 bp fragment. The LmjF promoter area was additionally practical in different species of Leishmania. Nuclear run-on analyses demonstrated that solely the rRNA-coding strand is transcribed, downstream of this RNA polymerase I (pol I) promoter. These experiments additionally steered that transcription terminates upstream of the IGSRE.

 

Genomic group, transcription, splicing and gene regulation in Leishmania.

  1. The parasitic protozoan Leishmania is the aetiological agent of a spectrum of scientific illnesses, starting from disfiguring pores and skin lesions to life-threatening visceral an infection, and is a critical well being downside in tropical and subtropical areas world-wide. Leishmania parasites bear a dramatic transformation as they transfer between the completely different environments of an extracellular insect stage and an intracellular type within the vertebrate host.
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Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF-1), 152 (PlGF-2), and 203 (PlGF-3) amino acids (aa) respectively. Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF-2 has been identified. Mouse PlGF shares 60%, 92%, 62% and 59% aa identity with the appropriate isoform of human, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during human pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt-1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2-mediated angiogenesis. However, PlGF (especially human PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF-2, like VEGF164/165, shows heparin-dependent binding of neuropilin (Npn)-1 and Npn-2 and can inhibit nerve growth cone collapse. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis. Circulating PlGF often correlates with tumor stage and aggressiveness, and therapeutic P lGF antibodies are being investigated to inhibit tumor growth and angiogenesis.
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Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.
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Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.
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Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF-1, PlGF-2 and PlGF-3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF-2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF-2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.
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Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.
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Description: Placenta growth factor (PlGF) is a member of the vascular endothelial growth factor (VEGF) family of growth factors. PlGF and VEGF share primary structural as well as limited amino acid sequence homology with the A and B chains of PDGF. All eight cysteine residues involved in intra and interchain disulfides are conserved among these growth factors. As a result of alternative splicing, three PlGF RNAs encoding monomeric human PlGF1, PlGF2 and PlGF3 isoform precursors containing 149, 179 and 219 amino acid residues, respectively, have been described. In normal mouse tissues, only one mouse PlGF mRNA encoding the equivalent of human PlGF2 has been identified. Mouse PlGF shares 65% amino acid identity with human PlGF2. The gene for PlGF has been mapped to mouse chromosome 12 and human chromosome 14. PlGF binds with high affinity to Flt1, but not to Flk1/KDR.
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Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF-1), 152 (PlGF-2), and 203 (PlGF-3) amino acids (aa) respectively. Only PlGF-2 contains a highly basic heparin-binding 21 aa insert at the C-terminus. In rat only one PlGF that is the equivalent of human PlGF-2 has been identified. Rat PlGF shares 60%, 92%, 62% and 59% aa identity with the appropriate isoform of human, mouse, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during human pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt-1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2-mediated angiogenesis. However, PlGF (especially human PlGF-1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF-2, like VEGF164/165, shows heparin-dependent binding of neuropilin (Npn)-1 and Npn-2 and can inhibit nerve growth cone collapse. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis. Circulating PlGF often correlates with tumor stage and aggressiveness, and therapeutic PlGF antibodies are being investigated to inhibit tumor growth and angiogenesis.
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Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.
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Description: Placenta growth factor (PlGF) is a member of the PDGF/VEGF family of growth factors that share a conserved pattern of eight cysteines. Alternate splicing results in at least three human mature PlGF forms containing 131 (PlGF1), 152 (PlGF2), and 203 (PlGF3) amino acids (aa) respectively. Only PlGF2 contains a highly basic heparinbinding 21 aa insert at the C-terminus. In the mouse, only one P lGF that is the equivalent of human PlGF2 has been identified. Human PlGF1 shares 56%, 55%, 74% and 95% aa identity with the appropriate isoform of mouse, rat, canine and equine PlGF. PlGF is mainly found as variably glycosylated, secreted, 55 - 60 kDa disulfide linked homodimers. Mammalian cells expressing PlGF include villous trophoblasts, decidual cells, erythroblasts, keratinocytes and some endothelial cells. Circulating PlGF increases during pregnancy, reaching a peak in mid-gestation; this increase is attenuated in preeclampsia. However, deletion of PlGF in the mouse does not affect development or reproduction. Postnatally, mice lacking PlGF show impaired angiogenesis in response to ischemia. PlGF binds and signals through VEGF R1/Flt1, but not VEGF R2/Flk-1/KDR, while VEGF binds both but signals only through the angiogenic receptor, VEGF R2. PlGF and VEGF therefore compete for binding to VEGF R1, allowing high PlGF to discourage VEGF/VEGF R1 binding and promote VEGF/VEGF R2mediated angiogenesis. However, PlGF (especially PlGF1) and some forms of VEGF can form dimers that decrease the angiogenic effect of VEGF on VEGF R2. PlGF2, but not PLGF-1, shows heparindependent binding of neuropilin (Npn)-1 and Npn2. PlGF induces monocyte activation, migration, and production of inflammatory cytokines and VEGF. These activities facilitate wound and bone fracture healing, but also contribute to inflammation in active sickle cell disease and atherosclerosis.
  1. In an try and develop new methods for the remedy of leishmaniasis, the methods of molecular genetics have been utilised to elucidate the mechanisms which direct and management this cyclical differentiation.
  2. This overview discusses present information in regards to the group and regulation of the Leishmania nuclear genome and features a dialogue of chromosomal group, genomic association, transcription, transcript processing by trans-splicing and polyadenylation, and post-transcriptional regulation. The salient options in addition to the supporting proof for every subject are briefly reviewed.

 

  • Within the current paper we describe the isolation and characterization of 4 novel genes of the parasitic protozoan Leishmania infantum. These genes are organized as two unbiased gene clusters, and they’re associated by nucleotide sequence to eukaryotic genes encoding acidic ribosomal proteins. Every gene cluster incorporates two tandemly linked genes coding for similar proteins.

 

  • Every of the proteins coded by the gene clusters (known as LiP and LiP’) are extremely divergent in sequence, exhibiting the attribute options of eukaryotic P-proteins from the P2 group. Despite the sequence conservation of the coding areas of every of the genes within the cluster, the 5′- and three’-untranslated areas are heterogeneous in sequence.

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  • The evaluation of the expression of those genes signifies that logarithmic part promastigotes present elevated ranges of LiP– and LiP‘-specific transcripts in contrast with stationary part promastigotes. The regular state RNA ranges of the LiP and LiP’ genes present an analogous dependence of the expansion part of the parasite.

 

  • Utilizing particular probes for the divergent 3′-untranslated areas of every of the genes, it was discovered that the abundance of the mature transcripts is completely different even when the transcripts are derived from the identical gene cluster. These findings most likely point out that the three’-untranslated areas could affect the soundness or turnover of the transcripts derived from each LiP and LiP’ gene clusters.

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