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Subproteomic analysis of soluble proteins of the microsomal fraction from two Leishmania species
Parasites of the genus Leishmania are the causative agents of a range of clinical manifestations collectively known as Leishmaniasis, a disease that affects 12 million people worldwide. With the aim of identifying potential secreted protein targets for further characterization, we have applied two-d...
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| Published in: | Comparative biochemistry and physiology. Part D, Genomics & proteomics Genomics & proteomics, 2006-09, Vol.1 (3), p.300-308 |
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| cites | cdi_FETCH-LOGICAL-c383t-8106ed9fbaac89d30de846b8a2d5184069d921e8ae8f18e11f10ecb1640b33413 |
| container_end_page | 308 |
| container_issue | 3 |
| container_start_page | 300 |
| container_title | Comparative biochemistry and physiology. Part D, Genomics & proteomics |
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| creator | de Oliveira, Arthur H.C. Ruiz, Jerônimo C. Cruz, Angela K. Greene, Lewis J. Rosa, José César Ward, Richard J. |
| description | Parasites of the genus
Leishmania are the causative agents of a range of clinical manifestations collectively known as Leishmaniasis, a disease that affects 12 million people worldwide. With the aim of identifying potential secreted protein targets for further characterization, we have applied two-dimensional gel electrophoresis and mass spectrometry methods to study the soluble protein content of the microsomal fraction from two
Leishmania species,
Leishmania L. major and
L. L. amazonensis. MALDI-TOF peptide mass fingerprint analysis of 33 protein spots from
L. L. amazonensis and 41 protein spots from
L. L. major identified 14 proteins from each sample could be unambiguously assigned. These proteins include the nucleotide diphosphate kinase (NDKb), a calpain-like protease, a tryparedoxin peroxidase (TXNPx) and a small GTP-binding Rab1-protein, all of which have a potential functional involvement with secretion pathways and/or environmental responses of the parasite. These results complement ongoing genomic studies in
Leishmania, and are relevant to further understanding of host/parasite interactions. |
| doi_str_mv | 10.1016/j.cbd.2006.05.003 |
| format | article |
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Leishmania are the causative agents of a range of clinical manifestations collectively known as Leishmaniasis, a disease that affects 12 million people worldwide. With the aim of identifying potential secreted protein targets for further characterization, we have applied two-dimensional gel electrophoresis and mass spectrometry methods to study the soluble protein content of the microsomal fraction from two
Leishmania species,
Leishmania L. major and
L. L. amazonensis. MALDI-TOF peptide mass fingerprint analysis of 33 protein spots from
L. L. amazonensis and 41 protein spots from
L. L. major identified 14 proteins from each sample could be unambiguously assigned. These proteins include the nucleotide diphosphate kinase (NDKb), a calpain-like protease, a tryparedoxin peroxidase (TXNPx) and a small GTP-binding Rab1-protein, all of which have a potential functional involvement with secretion pathways and/or environmental responses of the parasite. These results complement ongoing genomic studies in
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Leishmania are the causative agents of a range of clinical manifestations collectively known as Leishmaniasis, a disease that affects 12 million people worldwide. With the aim of identifying potential secreted protein targets for further characterization, we have applied two-dimensional gel electrophoresis and mass spectrometry methods to study the soluble protein content of the microsomal fraction from two
Leishmania species,
Leishmania L. major and
L. L. amazonensis. MALDI-TOF peptide mass fingerprint analysis of 33 protein spots from
L. L. amazonensis and 41 protein spots from
L. L. major identified 14 proteins from each sample could be unambiguously assigned. These proteins include the nucleotide diphosphate kinase (NDKb), a calpain-like protease, a tryparedoxin peroxidase (TXNPx) and a small GTP-binding Rab1-protein, all of which have a potential functional involvement with secretion pathways and/or environmental responses of the parasite. These results complement ongoing genomic studies in
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Leishmania are the causative agents of a range of clinical manifestations collectively known as Leishmaniasis, a disease that affects 12 million people worldwide. With the aim of identifying potential secreted protein targets for further characterization, we have applied two-dimensional gel electrophoresis and mass spectrometry methods to study the soluble protein content of the microsomal fraction from two
Leishmania species,
Leishmania L. major and
L. L. amazonensis. MALDI-TOF peptide mass fingerprint analysis of 33 protein spots from
L. L. amazonensis and 41 protein spots from
L. L. major identified 14 proteins from each sample could be unambiguously assigned. These proteins include the nucleotide diphosphate kinase (NDKb), a calpain-like protease, a tryparedoxin peroxidase (TXNPx) and a small GTP-binding Rab1-protein, all of which have a potential functional involvement with secretion pathways and/or environmental responses of the parasite. These results complement ongoing genomic studies in
Leishmania, and are relevant to further understanding of host/parasite interactions.</abstract><cop>Netherlands</cop><pub>Elsevier Inc</pub><pmid>20483262</pmid><doi>10.1016/j.cbd.2006.05.003</doi><tpages>9</tpages></addata></record> |
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| subjects | 2D-PAGE Leishmania MALDI-TOF Microsome Subproteome Trypanosomatidae |
| title | Subproteomic analysis of soluble proteins of the microsomal fraction from two Leishmania species |
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