Leishmania infantum chagasi: A genome-based approach to identification of excreted/secreted proteins

DebRoy, Sruti; Keenan, Alexandra B.; Ueno, Norikiyo; Jerônimo, Selma M. B.; Donelson, John E.; Wilson, Mary E.

doi:10.1016/j.exppara.2010.06.011

Cited by 16 publications

(18 citation statements)

References 58 publications

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“…Moreover, we found that BmCAT3, BmCAT4, BmCAT5, BmCAT6, and BmCAT7 had a signal peptide, respectively, and transmembrane domains except for BmCAT4. Since presence of signal peptide and absence of transmembrane domains can be used as indicators of a secreted protein (DebRoy et al., ), then BmCAT4 might be a putative secreted protein. In addition, BmCat1 , BmCat2 , BmCat3 , BmCat5 had one intron, whereas BmCat4 , BmCat6 , BmCat7 had two introns (Fig.…”

Section: Resultsmentioning

confidence: 99%

ANNOTATION AND EVOLUTION OF THE ANTIOXIDANT GENES IN THE SILKWORM, Bombyx mori

Guo-qing

Zhang

2012

Arch Insect Biochem Physiol

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Antioxidant system, which is composed of multiple gene families, plays a major role in reducing oxidative damage and xenobiotic detoxification in all living organisms. We identified 50 silkworm antioxidant genes from nine gene families based on the assembled genome sequence. A comparative analysis of the antioxidant genes of the silkworm with other order insects Anopheles gambiae, Apis mellifera, Drosophila melanogaster, and Tribolium castaneum, was performed. We found that most of the antioxidant gene families are highly conserved but Catalase (CAT) and heme-containing peroxidase (HPX) families were lineage-specifically expanded in the silkworm. The expression patterns of the silkworm antioxidant genes were investigated with the known ESTs, microarray data, and reverse transcription-polymerase chain reaction (RT-PCR). Forty two of the 50 silkworm antioxidant genes were transcribed and most of the transcribed genes showed tissue-specific expression patterns. More than a half of lineage-specifically expanded BmCATs lacked 15 or more than 15 of the 36 heme-binding residues and might lose catalase activities. However, the genes encoding these BmCATs showed almost a ubiquitous tissue expression pattern, indicating that they might have evolved new functions. In addition, the lineage-specifically expanded BmHPXs could function in maintaining cell homeostasis in the process of the synthesis of large amounts of silk proteins because they were predominantly expressed in silk gland of the silkworm. The lineage-specific expansion of antioxidant gene families in the silkworm provides useful information for understanding evolution and functional versatility of antioxidant genes in the silkworm even Lepidopteran insects.

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Section: Resultsmentioning

confidence: 99%

ANNOTATION AND EVOLUTION OF THE ANTIOXIDANT GENES IN THE SILKWORM, Bombyx mori

Guo-qing

Zhang

2012

Arch Insect Biochem Physiol

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“…The latter observation is probably caused by the inefficient transport of a type II secreted extracellular protease, PrtA (230). Mip-like PPIases are also not restricted to bacteria alone but have been reported for major protozoan parasites, such as T. cruzi and Leishmania infantum (44,231). For the Mip-like protein of T. cruzi, it is known that it facilitates invasion of mammalian epithelial cells (44).…”

Section: Mip-like Ppiases-a Special Class Of Virulence Factorsmentioning

confidence: 97%

Microbial Peptidyl-Prolyl cis / trans Isomerases (PPIases): Virulence Factors and Potential Alternative Drug Targets

Ünal

Steinert

2014

Microbiol Mol Biol Rev

156

146

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SUMMARY Initially discovered in the context of immunomodulation, peptidyl-prolyl cis/trans isomerases (PPIases) were soon identified as enzymes catalyzing the rate-limiting protein folding step at peptidyl bonds preceding proline residues. Intense searches revealed that PPIases are a superfamily of proteins consisting of three structurally distinguishable families with representatives in every described species of prokaryote and eukaryote and, recently, even in some giant viruses. Despite the clear-cut enzymatic activity and ubiquitous distribution of PPIases, reports on solely PPIase-dependent biological roles remain scarce. Nevertheless, they have been found to be involved in a plethora of biological processes, such as gene expression, signal transduction, protein secretion, development, and tissue regeneration, underscoring their general importance. Hence, it is not surprising that PPIases have also been identified as virulence-associated proteins. The extent of contribution to virulence is highly variable and dependent on the pleiotropic roles of a single PPIase in the respective pathogen. The main objective of this review is to discuss this variety in virulence-related bacterial and protozoan PPIases as well as the involvement of host PPIases in infectious processes. Moreover, a special focus is given to Legionella pneumophila macrophage infectivity potentiator (Mip) and Mip-like PPIases of other pathogens, as the best-characterized virulence-related representatives of this family. Finally, the potential of PPIases as alternative drug targets and first tangible results are highlighted.

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“…As already mentioned, efficient diagnosis and treatment of leishmaniasis are still a challenge. An alternative to improve therapy of the disease is by the identification and study of proteins important for parasite survival …”

Section: Potential Applications Of Proteomics In Leishmaniasismentioning

confidence: 99%

“…An efficient method for studying the protein content of EVs is through proteomics or exoproteomics, which have been used for identification of new pharmacological targets and potential candidates for vaccines . The efficacy of a vaccine based on exosomes shed by dendritic cells stimulated with L. major antigens was tested in BALB/c mice.…”

Section: Potential Applications Of Proteomics In Leishmaniasismentioning

confidence: 99%

Proteomics and Leishmaniasis: Potential Clinical Applications

Capelli-Peixoto

Mule

Tano

et al. 2019

Proteomics Clinical Apps

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Leishmaniases are diseases caused by protozoan parasites of the genus Leishmania. They are endemic in 98 countries, affect around 12 million people worldwide and may present several distinct clinical forms. Unfortunately, there are only a few drugs available for treatment of leishmaniasis, which are toxic and not always effective. Different parasite species and different clinical forms require optimization of the treatment or more specific therapies, which are not available. The emergence of resistance is also a matter of concern. Besides, diagnosis can sometimes be complicated due to atypical manifestations and associations with other pathologies. In this review, proteomic data are presented and discussed in terms of their application in important issues in leishmaniasis such as parasite resistance to chemotherapy, diagnosis of active disease in patients and dogs, markers for different clinical forms, identification of virulence factors, and their potential use in vaccination. It is shown that proteomics has contributed to the discovery of potential biomarkers for prognosis, diagnosis, therapeutics, monitoring of disease progression, treatment follow‐up and identification of vaccine candidates for specific diseases. However, the authors believe its capabilities have not yet been fully explored for routine clinical analysis for several reasons, which will be presented in this review.

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Leishmania infantum chagasi: A genome-based approach to identification of excreted/secreted proteins

Cited by 16 publications

References 58 publications

ANNOTATION AND EVOLUTION OF THE ANTIOXIDANT GENES IN THE SILKWORM, Bombyx mori

ANNOTATION AND EVOLUTION OF THE ANTIOXIDANT GENES IN THE SILKWORM, Bombyx mori

Microbial Peptidyl-Prolyl cis / trans Isomerases (PPIases): Virulence Factors and Potential Alternative Drug Targets

Proteomics and Leishmaniasis: Potential Clinical Applications

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