Proteomic analysis of <b><i>N</i></b>‐glycosylation in mosquito dopachrome conversion enzyme

Li, Junsuo S.; Vavricka, Christopher J.; Christensen, Bruce M.; Li, Jianyong

doi:10.1002/pmic.200601053

Cited by 8 publications

(5 citation statements)

References 17 publications

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“…A similar protein, which accelerates the melanization process, has also been reported in other insect species (Aso et al, 1984). Based on its function, a mosquito enzyme for melanization was discovered and named dopachrome conversion enzyme (DCE) (Li et al, , 2007.…”

Section: Insect Melanizationmentioning

confidence: 76%

Melanization in living organisms: a perspective of species evolution

Vavricka

Christensen

2010

Protein Cell

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Eumelanin is a heteropolymer that is generally composed of hydroxylated indole residues and plays diverse protective functions in various species. Melanin is derived from the amino acid tyrosine and production of melanin is a highly complex oxidative process with a number of steps that can either proceed enzymatically or non-enzymatically. Although melanin plays important protective roles in many species, during melanization, particularly in steps that can proceed non-enzymatically, many toxic intermediates are produced, including semiquinones, dopaquinone, indole-quinones and moreover, the production of many reactive oxygen species. To mitigate the production of reactive species, a number of proteins that regulate the biochemical process of melanization have evolved in various living species, which is closely related to adaptation and physiological requirements. In this communication, we discuss differences between non-enzymatic and enzymatic processes of melanization and the enzymatic regulation of melanization in difference species with an emphasis on differences between mammals and insects. Comparison between melanization and insect sclerotization is also emphasized which raises some interesting questions about the current models of these pathways.

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Section: Insect Melanizationmentioning

confidence: 76%

Melanization in living organisms: a perspective of species evolution

Vavricka

Christensen

2010

Protein Cell

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“…By lectin-binding assay, the authors detected the presence of α -D-mannose, α -D-N-acetyl-galactosamine, β -D-gal-(1,3) N-acetyl-galactosamine, β -D-galactose, N-acetyl-galactosamine, α -L-fucose, and β -N acetyl-glucosamine. Likewise, different oligosaccharide structures such as Man3GlcNAc2, Man3 (Fuc) 1-2GlcNAc2 were detected [ 55 ]. Recently, Francischetti et al [ 56 ] demonstrated the presence of sulfated glycans in the salivary gland of Anopheles gambiae .…”

Section: Discussionmentioning

confidence: 99%

Sialic Acid Expression in the MosquitoAedes aegyptiand Its Possible Role in Dengue Virus-Vector Interactions

Cime-Castillo

Delannoy

Mendoza‐Hernández

et al. 2015

BioMed Research International

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Dengue fever (DF) is the most prevalent arthropod-borne viral disease which affects humans. DF is caused by the four dengue virus (DENV) serotypes, which are transmitted to the host by the mosquito Aedes aegypti that has key roles in DENV infection, replication, and viral transmission (vector competence). Mosquito saliva also plays an important role during DENV transmission. In this study, we detected the presence of sialic acid (Sia) in Aedes aegypti tissues, which may have an important role during DENV-vector competence. We also identified genome sequences encoding enzymes involved in Sia pathways. The cDNA for Aedes aegypti CMP-Sia synthase (CSAS) was amplified, cloned, and functionally evaluated via the complementation of LEC29.Lec32 CSAS-deficient CHO cells. AedesCSAS-transfected LEC29.Lec32 cells were able to express Sia moieties on the cell surface. Sequences related to α-2,6-sialyltransferase were detected in the Aedes aegypti genome. Likewise, we identified Sia-α-2,6-DENV interactions in different mosquito tissues. In addition, we evaluated the possible role of sialylated molecules in a salivary gland extract during DENV internalization in mammalian cells. The knowledge of early DENV-host interactions could facilitate a better understanding of viral tropism and pathogenesis to allow the development of new strategies for controlling DENV transmission.

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“…Our lab has confirmed that of the 13 Drosophila yellow family genes, yellow‐f, and yellow‐f2 produce enzymes with DCE activity (Han et al ., ). We have also characterized a DCE from the yellow fever mosquito A. aegypti (Johnson et al ., ; Li et al ., ). Although, the functions of many remaining yellow genes still remain uncharacterized, it is likely that they are also involved in melanization or sclerotization pathways (Ferguson et al ., ).…”

Section: Melanization Enzymesmentioning

confidence: 97%

Tyrosine metabolic enzymes from insects and mammals: A comparative perspective

et al. 2013

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Differences in the metabolism of tyrosine between insects and mammals present an interesting example of molecular evolution. Both insects and mammals possess fine-tuned systems of enzymes to meet their specific demands for tyrosine metabolites; however, more homologous enzymes involved in tyrosine metabolism have emerged in many insect species. Without knowledge of modern genomics, one might suppose that mammals, which are generally more complex than insects and require tyrosine as a precursor for important catecholamine neurotransmitters and for melanin, should possess more enzymes to control tyrosine metabolism. Therefore, the question of why insects actually possess more tyrosine metabolic enzymes is quite interesting. It has long been known that insects rely heavily on tyrosine metabolism for cuticle hardening and for innate immune responses, and these evolutionary constraints are likely the key answers to this question. In terms of melanogenesis, mammals also possess a high level of regulation; yet mammalian systems possess more mechanisms for detoxification whereas insects accelerate pathways like melanogenesis and therefore must bear increased oxidative pressure. Our research group has had the opportunity to characterize the structure and function of many key proteins involved in tyrosine metabolism from both insects and mammals. In this mini review we will give a brief overview of our research on tyrosine metabolic enzymes in the scope of an evolutionary perspective of mammals in comparison to insects.

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Proteomic analysis of N‐glycosylation in mosquito dopachrome conversion enzyme

Cited by 8 publications

References 17 publications

Melanization in living organisms: a perspective of species evolution

Melanization in living organisms: a perspective of species evolution

Sialic Acid Expression in the MosquitoAedes aegyptiand Its Possible Role in Dengue Virus-Vector Interactions

Tyrosine metabolic enzymes from insects and mammals: A comparative perspective

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